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Effects of Whey and Fortified Collagen Hydrolysate Protein Supplements on Nitrogen Balance and Body Composition in Older Women
Abstract
Many elderly people have a low intake of dietary protein, yet their protein requirement may be higher than the current Recommended Dietary Allowance. High-quality protein supplements may be useful to enhance nitrogen retention and increase the availability of essential amino acids in elderly people. We compared the nitrogen balance of two protein supplements (Resource Beneprotein Instant Protein Powder, Nestlé HealthCare Nutrition, Minnetonka, MN, a whey protein concentrate; or Pro-Stat 101, Medical Nutrition USA, Englewood, NJ, a concentrated, fortified, collagen protein hydrolysate) varying in type but not amount of protein content using a crossover study design. The study consisted of two 15-day diet trials separated by a > or = 1-week washout period. Nine healthy elderly women (age 71+/-1 years) were provided a eucaloric diet containing approximately the protein Recommended Dietary Allowance of 0.8 g/kg body weight/day. The supplements constituted about half of the total protein provided to each subject. Nitrogen balance responses were assessed over days 6 to 10 and days 11 to 14 of each trial. Measured nitrogen content of the foods indicated that subjects consumed 0.81+/-0.02 g protein/kg/day and 0.85+/-0.05 g/kg/day for the whey and fortified collagen protein trials, respectively. Body weight decreased (P=0.02) after consumption of the whey supplement, with no significant changes in body weight or composition resulting from the consumption of the collagen supplement. Nitrogen excretion was higher during the whey supplement trial than during the collagen trial (P=0.047). Therefore, a concentrated, fortified, hydrolyzed collagen protein supplement maintained nitrogen balance and preserved lean body mass during 15 days of consumption of a relatively low-protein diet.
... Kimura et al. studies the improvement in vocal fold paralysis in human patients after collagen ingestion [48]. Hays et al. reports the effects of whey protein hydrolysate on different aspects (body composition and nitrogen balance) of women patients [49]. ...
... Hays et al. investigates the balance of nitrogen excretion and body weight in elderly women suffering sarcopenia [49]. Sarcopenia is a medical ailment related to muscle loss Kimura et al. reports the cure of dysphonia due to paralysis in the vocal folds with collagen [48]. ...
... Hays et al. investigates the balance of nitrogen excretion and body weight in elderly women suffering sarcopenia [49]. Sarcopenia is a medical ailment related to muscle loss with age due to the increase in body fats and decrease in bone mass and basal metabolic rate [122,123]. ...
The collagen hydrolysate, a proteinic biopeptide, is used for various key functionalities in humans and animals. Numerous reviews explained either individually or a few of following aspects: types, processes, properties, and applications. In the recent developments, various biological, biochemical, and biomedical functionalities are achieved in five aspects: process, type, species, disease, receptors. The receptors are rarely addressed in the past which are an essential stimulus to activate various biomedical and biological activities in the metabolic system of humans and animals. Furthermore, a systematic segregation of the recent developments regarding the five main aspects is not yet reported. This review presents various biological, biochemical, and biomedical functionalities achieved for each of the beforementioned five aspects using a systematic approach. The review proposes a novel three-level hierarchy that aims to associate a specific functionality to a particular aspect and its subcategory. The hierarchy also highlights various key research novelties in a categorical manner that will contribute to future research.
... However, despite CP being assigned of poor protein quality, there are reports of CP having biological effects. In some studies, CP have been shown to reduce nitrogen excretion and maintain body weight in supplemental trials of energy restriction and exercise [21], while having no effects in others [22]. Such effects of collagen-derived peptides may seem counter-intuitive in light of them being primarily nonessential amino acids (NEAA) by sequence, despite proposed anabolic signaling properties in cell culture [23]. ...
... placebo). Further, CP supplementation was shown to be more effective than whey at reducing nitrogen excretion and preserving body mass during a low protein diet [21]. As such, there is evidence that CP-derived proteins may have a supportive role in addition to those of EAA load, in human muscle. ...
... Further, CPþMP demonstrated augmented anabolic signalling that may have long term anabolic benefits. For instance, nitrogen excretion was reduced and body mass maintained when consuming CP vs whey protein during a low protein diet [21]. Nutritional composition and the balance between total nitrogen and EAA content may therefore play a significant role in fighting malnutrition and inactivity-significant clinical problems associated with age and disease related anabolic resistance. ...
Background & Aims
Nutritional composition is key for skeletal muscle maintenance into older age. Yet the acute effects of collagen protein blended with other protein sources, in relation to skeletal muscle anabolism, are ill-defined. We investigated human muscle protein synthesis (MPS) responses to a 20g blend of collagen protein hydrolysate + milk protein (CP+MP, 125ml) oral nutritional supplement (ONS) vs. 20g non-blended milk protein source (MP, 200ml) ONS, in older adults.
Methods
Healthy older men (N=8, 71±1y, BMI: 27±1kg·m⁻²) underwent a randomized trial of 20g protein, from either a CP+MP blend (Fresubin®3.2kcal DRINK), or a kcal-matched (higher in essential amino acids (EAA) ONS of MP alone. Vastus lateralis (VL) MPS and plasma AA were determined using stable isotope-tracer mass spectrometry; anabolic signaling was quantified via immuno-blotting in VL biopsies taken at baseline and 2/4 h after ONS feeding. Plasma insulin was measured via enzyme-linked immunosorbent assay (ELISA). Measures were taken at rest, after the feed (FED) and after the feed + exercise (FED-EX) conditions (unilateral leg exercise, 6×8, 75% 1-RM).
Results
MP resulted in a greater increase in plasma leucine (MP mean: 152 ± 6 μM, CP+MP mean: 113 ± 4 μM (Feed P<0.001) and EAA (MP mean: 917 ± 25 μM, CP+MP mean: 786 ± 15 μM (Feed P<0.01) than CP+MP. CP + MP increased plasma glycine (peak 385 ± 57 μM (P<0.05)), proline (peak 323 ± 29 μM (P<0.01)) and non-essential amino acids (NEAA) (peak 1621 ± 107 μM (P<0.01)) with MP showing no increase. Plasma insulin increased in both trials (CP+MP: 58±10 mU/mL (P<0.01), MP: 42±6 mU/mL (P<0.01), with peak insulin greater with CP+MP vs. MP (P<0.01). MPS demonstrated equivalent increases in response to CP+MP and MP under both FED (MP: 0.039±0.005%/h to 0.081±0.014%/h (P<0.05), CP+MP: 0.042±0.004%/h to 0.085±0.007%/h (P<0.05)) and FED-EX (MP: 0.039±0.005%/h to 0.093±0.013%/h (P<0.01), CP+MP: 0.042±0.004%/h to 0.105±0.015%/h, (P<0.01)) conditions. FED muscle p-mTOR fold-change from baseline increased to a greater extent with CP+MP vs. MP (P<0.05), whilst FED-EX muscle p-eEF2 fold-change from baseline decreased to a greater extent with CP+MP vs. MP (P<0.05); otherwise anabolic signaling responses were indistinguishable.
Conclusion
Fresubin®3.2kcal DRINK, which contains a 20g mixed blend of CP+MP, resulted in equivalent MPS responses to MP alone. Fresubin® 3.2 Kcal DRINK may provide a suitable alternative to MP for use in older adults and a convenient way to supplement calories and protein to improve patient adherence and mitigate muscle mass loss.
... In regard to ageing, older females consuming the RDA of protein with collagen constituting approximately half of the total protein provided, preserved lean body mass and maintained nitrogen balance [127]. In contrast, those consuming a similar quantity of whey protein experienced a loss in body weight with no change in body fat (potentially indicating a decline in lean body mass) and an increase in nitrogen excretion [127]. ...
... In regard to ageing, older females consuming the RDA of protein with collagen constituting approximately half of the total protein provided, preserved lean body mass and maintained nitrogen balance [127]. In contrast, those consuming a similar quantity of whey protein experienced a loss in body weight with no change in body fat (potentially indicating a decline in lean body mass) and an increase in nitrogen excretion [127]. Despite collagen being regarded as a low-quality protein (according to PDCAAS and DIAAS scores), the NEAA's it does contain either have a low molecular weight or possess more than one nitrogen atom (e.g., hydroxyproline, hydroxylysine), meaning the nitrogen content of collagen on a per gram basis is high [8], and possibly greater than whey protein [127], which may explain the ability of collagen to help maintain nitrogen balance. ...
... In contrast, those consuming a similar quantity of whey protein experienced a loss in body weight with no change in body fat (potentially indicating a decline in lean body mass) and an increase in nitrogen excretion [127]. Despite collagen being regarded as a low-quality protein (according to PDCAAS and DIAAS scores), the NEAA's it does contain either have a low molecular weight or possess more than one nitrogen atom (e.g., hydroxyproline, hydroxylysine), meaning the nitrogen content of collagen on a per gram basis is high [8], and possibly greater than whey protein [127], which may explain the ability of collagen to help maintain nitrogen balance. ...
Dietary protein is critical for the maintenance of musculoskeletal health, whereappropriate intake (i.e., source, dose, timing) can mitigate declines in muscle and bone mass and/orfunction. Animal-derived protein is a potent anabolic source due to rapid digestion and absorptionkinetics stimulating robust increases in muscle protein synthesis and promoting bone accretion andmaintenance. However, global concerns surrounding environmental sustainability has led to anincreasing interest in plant- and collagen-derived protein as alternative or adjunct dietary sources.This is despite the lower anabolic profile of plant and collagen protein due to the inferior essentialamino acid profile (e.g., lower leucine content) and subordinate digestibility (versus animal). Thisreview evaluates the efficacy of animal-, plant- and collagen-derived proteins in isolation, and asprotein blends, for augmenting muscle and bone metabolism and health in the context of ageing,exercise and energy restriction.
... Nonetheless, 2 studies have reported positive effects of supplementation with low quality CP on lean body mass (LBM) gains with resistance training in sarcopenic older men (14) (which showed an extraordinary gain in LBM) and premenopausal women (15). Interestingly, a CP supplement improved nitrogen balance in older women (16); however, to our knowledge no study has examined the muscle protein synthetic response, and thus whether muscle is the tissue affected by CP supplementation, that may be underpinning the ostensibly favorable CP supplementinduced changes in body composition (14,15) or improved nitrogen balance (16). Thus, the primary outcome of this study was to compare the acute and longer-term effects of WP or CP supplementation on MPS alone and when combined with RE. ...
... Nonetheless, 2 studies have reported positive effects of supplementation with low quality CP on lean body mass (LBM) gains with resistance training in sarcopenic older men (14) (which showed an extraordinary gain in LBM) and premenopausal women (15). Interestingly, a CP supplement improved nitrogen balance in older women (16); however, to our knowledge no study has examined the muscle protein synthetic response, and thus whether muscle is the tissue affected by CP supplementation, that may be underpinning the ostensibly favorable CP supplementinduced changes in body composition (14,15) or improved nitrogen balance (16). Thus, the primary outcome of this study was to compare the acute and longer-term effects of WP or CP supplementation on MPS alone and when combined with RE. ...
... A previous study from our laboratory showed no effect of CP supplementation on rates of MyoPS after 2 wk of reduced daily activity and 1 wk of recovery in healthy older adults (13). To date, 3 additional studies have looked at the efficacy of CP on body composition and showed that CP supplementation resulted in an extraordinary increase in LBM (not muscle) with resistance training in older men (14) and premenopausal women (15), and helped in maintaining nitrogen balance in older women (16). It should be noted that the effects of CP supplementation on LBM gains with RE shown by Zdzieblik et al. (14) were exceptional (∼5 kg) and have been questioned (27). ...
Background:
Aging appears to attenuate the response of skeletal muscle protein synthesis (MPS) to anabolic stimuli such as protein ingestion (and the ensuing hyperaminoacidemia) and resistance exercise (RE).
Objectives:
The purpose of this study was to determine the effects of protein quality on feeding- and feeding plus RE-induced increases of acute and longer-term MPS after ingestion of whey protein (WP) and collagen protein (CP).
Methods:
In a double-blind parallel-group design, 22 healthy older women (mean ± SD age: 69 ± 3 y, n = 11/group) were randomly assigned to consume a 30-g supplement of either WP or CP twice daily for 6 d. Participants performed unilateral RE twice during the 6-d period to determine the acute (via [13C6]-phenylalanine infusion) and longer-term (ingestion of deuterated water) MPS responses, the primary outcome measures.
Results:
Acutely, WP increased MPS by a mean ± SD 0.017 ± 0.008%/h in the feeding-only leg (Rest) and 0.032 ± 0.012%/h in the feeding plus exercise leg (Exercise) (both P < 0.01), whereas CP increased MPS only in Exercise (0.012 ± 0.013%/h) (P < 0.01) and MPS was greater in WP than CP in both the Rest and Exercise legs (P = 0.02). Longer-term MPS increased by 0.063 ± 0.059%/d in Rest and 0.173 ± 0.104%/d in Exercise (P < 0.0001) with WP; however, MPS was not significantly elevated above baseline in Rest (0.011 ± 0.042%/d) or Exercise (0.020 ± 0.034%/d) with CP. Longer-term MPS was greater in WP than in CP in both Rest and Exercise (P < 0.001).
Conclusions:
Supplementation with WP elicited greater increases in both acute and longer-term MPS than CP supplementation, which is suggestive that WP is a more effective supplement to support skeletal muscle retention in older women than CP.This trial was registered at clinicaltrials.gov as NCT03281434.
... It is often assumed that daily protein intake in elderly populations is even less than the recommended dietary allowance (RDA) or that even more protein per day is needed to ensure age-appropriate muscular system function [46]. In a study comparing the effects of whey and fortified collagen hydrolysate on nitrogen balance in elderly subjects, no difference was found between the high-and low-quality proteins [47]. Therefore, the authors suggested that collagen-based proteins can be seen as an appropriate supplement for elderly individuals and considered equal to whey protein. ...
... Therefore, the authors suggested that collagen-based proteins can be seen as an appropriate supplement for elderly individuals and considered equal to whey protein. Furthermore, the loss in body weight of the whey protein group could not be explained by a loss of fat mass, indicating a loss of FFM, which was not found in the collagen group [47]. It therefore could be suspected that the greater increase in FFM after collagen intake and RET in the study of Zdzieblik et al. [11] is the result of enhanced connective tissue adaptation as well as pronounced hypertrophy of contractile muscle cells; these mechanisms would explain the significant differences in strength enhancement. ...
... Due to the missing data about absolute macronutrient intake, it could be speculated that the daily protein intake was insufficient within a strength training regime. This would strengthen the assumption that a prolonged intake of CP may be equivalent to other protein intake strategies during the consumption of low-protein diets [47]. ...
We aimed to determine the effects of long-term collagen peptide (CP) supplementation and resistance exercise training (RET) on body composition, strength, and muscle fiber cross-sectional area (fCSA) in recreationally active men. Fifty-seven young men were randomly and double-blinded divided into a group receiving either collagen peptides (COL, 15 g/day) or a placebo (PLA). Strength testing, bioimpedance analysis, and muscle biopsies were used prior to and after an RET intervention. Food record protocols were performed during the RET intervention. The groups trained three times a week for 12 weeks. Baseline parameters showed no differences between groups, and the external training load and dietary food intake were also similar. COL showed a significant increase in fat-free mass (FFM) compared with the placebo group (p < 0.05). Body fat mass (BFM) was unchanged in COL, whereas a significant increase in BFM was observed in PLA. Both groups showed significant increases in all strength tests, with a trend for a slightly more pronounced effect in COL. The fCSA of type II muscle fibers increased significantly in both groups without differences between the two groups. We firstly demonstrated improved body composition in healthy, recreationally active men subsequent to prolonged CP supplementation in combination with RET. As the observed increase in FFM was not reflected in differences in fCSA hypertrophy between groups, we assume enhanced passive connective tissue adaptations in COL due to CP intake.
... Due to the dynamic nature of the training-induced adaptational process, it does not necessarily make sense to set protein requirements in training only with the aim of balancing nitrogen intake with nitrogen loss because the athlete in training is not in a state of equilibrium -they are in a process of anabolic adaptation. This principle applies to endurance training as well as it does to all forms of strength training (11,30,32). ...
... The best researched area regarding the effects of proteins and amino acids in sports is their influence on increasing muscle protein synthesis after strength training. This area has also yielded the most study data on different protein sources and different amino acid compositions (10, 11,16,25). With regard to physiological mechanism, studies to date have shown that particularly when combined with an insulin release triggered by carbohydrate intake, branched-chain amino acids can stimulate muscular protein synthesis via the mTOR signalling (mTOR=mechanistic target of rapamycin) (16). ...
Adequate intake of high quality proteins and amino acids
is essential for the body in order to build up structures such as
muscle, tendons, ligaments and bone. Protein intake also regulates
and affects various metabolic processes, including hormonal
regulation. Accordingly, proteins and amino acids are, to varying
extents, able to stimulate or inhibit anabolic signal transduction
pathways and the synthesis and secretion of various hormones
such as insulin, growth hormone and insulin-like growth factor
1 (IGF-1).
This means that tailoring protein intake to an athlete’s specific
type of sport and exercise intensity can be helpful in supporting
the training process and improving performance. The
aims of adjusting intake in this way may include maintaining or
building muscle mass or muscle strength, preventing a catabolic
state, and improving recovery following exercise.
Even though the importance of protein intake in the field of
sport is increasingly well-known, there is still much controversy
regarding intake levels, types of protein sources, optimal amino
acid composition, and ideal timing of intake. The lay press and
commercial websites in particular often provide biased or incorrect
recommendations without scientific evidence.
This position paper summarizes the current state of knowledge
regarding the physiological effects of protein intake in sports,
paying particular attention to the aspects of intake level and the
dose-response relationship.
... Four RCTs tested the effects of a daily administration of different protein supplements among older people along different periods (from 15 days to 2 years) [61][62][63][64]. In the USA, 15-day consecutive administration of 0.4 g/kg of body weight of tryptophan-fortified collagen to 9 older women resulted in a better nitrogen balance and lean mass than the same dose of WP [61]. ...
... Four RCTs tested the effects of a daily administration of different protein supplements among older people along different periods (from 15 days to 2 years) [61][62][63][64]. In the USA, 15-day consecutive administration of 0.4 g/kg of body weight of tryptophan-fortified collagen to 9 older women resulted in a better nitrogen balance and lean mass than the same dose of WP [61]. In Norway, a 12-week supplementation with a protein-enriched milk twice a day (for a total of 40 g protein/day), did not improved muscle mass and strength among 50 men and women aged over 70 years [62]. ...
Background:
To review currently available evidence on the effect of cow-milk proteins supplementation (CPS) on health in the elderly.
Methods:
Five electronic databases (Pubmed, Web of Science, Embase, Cochrane Library, ClinicalTrials.gov) were searched for studies about CPS among older people. All types of publications were included, with the exception of systematic reviews, meta-analyses, opinion letters, editorials, case reports, conference abstracts and comments. An additional search in Google Scholar and a manual review of the reference lists were performed.
Results:
Overall, 103 studies were included. Several studies explored the role of CPS in the preservation or improvement of muscle mass among healthy subjects (40 studies) and pre-frail, frail or sarcopenic patients (14), with evidence of beneficial effects. Other studies assessed the effect of CPS on bones (12), cardiovascular disease (8), inflamm-aging (7), chronic pulmonary disease (4), neurocognitive function (4), and vaccines (2), with weak evidence of positive effects. Seven studies in the field of protein metabolism investigated the role of CPS as an important contributor to nutritional needs. Other investigational areas are considered in the last five studies.
Conclusions:
The beneficial effects of CPS in achieving aged-related nutritional goals, in preserving muscle mass and in recovering after hospitalization may be particularly relevant in the elderly.
... While there are few reports on OA in its initial stage, recent studies have reported severe microscopic changes in bone cartilage in advanced stages of OA, such as an increase in the volume of subchondral bone, low bone mineralization and mechanical strength, as well as considerable deterioration in articular cartilage. This suggests a correlation of development of OA in patients with OP, which also means that OP treatment can help prevent the progression of OA. 22,23 A study carried out by Hays et al. 24 tested the supplementation of women aged between 65 and 85 years. The nitrogen balance was compared following supplementation with two protein compounds, "whey protein" and collagen hydrolysate. ...
... Furthermore, nitrogen excretion was lower with the collagen hydrolysate than with the whey, thus maintaining nitrogen balance and lean body mass. Also according to Hays et al. 24 the study data, combined with previous estimates of protein requirements in the diet of older people, strongly indicate that the current recommended dietary intake (RDA) may be inadequate or marginal, even in normocaloric diets. They also noted that although collagen hydrolysate is deficient in essential amino acids, combining it with a diet featuring adequate amounts of protein could promote nitrogen balance. ...
Introduction
Collagen hydrolysate is recognized as a safe nutraceutical, whose combination of amino acids stimulates the synthesis of collagen in the extracellular matrix of cartilage and other tissues.
Objective
to conduct a systematic review of literature on the action of collagen hydrolysate in bone and cartilaginous tissue and its therapeutic use against osteoporosis and osteoarthritis.
Method
a study of the PubMed, MEDLINE, LILACS, and SciELO databases was performed. Articles published in English and Portuguese in the period of 1994 to 2014 were considered. Results: the sample comprised nine experimental articles with in vivo (animals and humans) andin vitro (human cells) models, which found that the use of different doses of collagen hydrolysate were associated with the maintenance of bone composition and strength, and the proliferation and cell growth of cartilage.
Conclusion
hydrolyzed collagen has a positive therapeutic effect on osteoporosis and osteoarthritis with a potential increase in bone mineral density, a protective effect on articular cartilage, and especially in the symptomatic relief of pain.
... Collagen is generally regarded as having a relatively low biological value, mainly due to the low amount of BCAA and lysine (Table 1). Nevertheless, the mixture of amino acids has been shown to be superior compared with whey protein in maintaining N balance and body weight during a low-protein diet (18) . In addition, collagen contains relatively high amounts of arginine and glycine, both known to be important substrates for the synthesis of creatine in the human body (19) . ...
... The impact on body composition has not been in the focus, as it is generally believed that the relatively low biological value of collagen would not favour a significant improvement on muscular net protein synthesis. The results of the present investigation do not support this assumption, and the following findings could contribute to further explain the increase in FFM and strength following collagen peptides supplementation: it has been shown that collagen peptide intake was superior to whey protein in maintaining N balance and body weight during a low-protein diet (18) . Although collagen has a low protein digestibility corrected amino acid score, its N content may be higher compared with whey on a per gram basis due to a high proportion of amino acids having low molecular weight or containing more than one N atom. ...
Protein supplementation in combination with resistance training may increase muscle mass and muscle strength in elderly subjects. The objective of this study was to assess the influence of post-exercise protein supplementation with collagen peptides v. placebo on muscle mass and muscle function following resistance training in elderly subjects with sarcopenia. A total of fifty-three male subjects (72·2 (sd 4·68) years) with sarcopenia (class I or II) completed this randomised double-blind placebo-controlled study. All the participants underwent a 12-week guided resistance training programme (three sessions per week) and were supplemented with either collagen peptides (treatment group (TG)) (15 g/d) or silica as placebo (placebo group (PG)). Fat-free mass (FFM), fat mass (FM) and bone mass (BM) were measured before and after the intervention using dual-energy X-ray absorptiometry. Isokinetic quadriceps strength (IQS) of the right leg was determined and sensory motor control (SMC) was investigated by a standardised one-leg stabilisation test. Following the training programme, all the subjects showed significantly higher (P<0·01) levels for FFM, BM, IQS and SMC with significantly lower (P<0·01) levels for FM. The effect was significantly more pronounced in subjects receiving collagen peptides: FFM (TG +4·2 (sd 2·31) kg/PG +2·9 (sd 1·84) kg; P<0·05); IQS (TG +16·5 (sd 12·9) Nm/PG +7·3 (sd 13·2) Nm; P<0·05); and FM (TG -5·4 (sd 3·17) kg/PG -3·5 (sd 2·16) kg; P<0·05). Our data demonstrate that compared with placebo, collagen peptide supplementation in combination with resistance training further improved body composition by increasing FFM, muscle strength and the loss in FM.
... Dietary protein intake is relevant for the maintenance of muscle mass and strength in communitydwelling older adults (12)(13). Protein supplementation has been shown to enhance the muscle strengthening effect of resistance exercise (14)(15). Similarly, amino-acids supplementation (crucial for protein synthesis (16)) has shown beneficial effects on muscle mass (17). ...
... Protein supplementation has been shown to augment the muscle strengthening effect of resistance exercise (14,40). Older adults have a high risk of inadequate protein intake (41), and their synthetic response to protein intake may be blunted (42). ...
Objective: Sarcopenia, the age-related loss of skeletal muscle mass, is highly prevalent in older adults.
The aim of this study was to investigate the effects of the combination of resistance training and multinutrients supplementation (including vitamin D and protein) on muscle mass and physical performance in frail older adults. Methods: This trial was conducted in Japanese frail older adults (n=77), which underwent a standardized protocol of a 3-month physical exercise intervention. The sample population was divided into two groups, according to the adoption (S/Ex: n = 38) or not (Ex: n = 39) of the additional multinutrient supplementation. The outcome measures of interest for the present analyses were the skeletal muscle mass index (SMI) and several physical performance tests. Results: Participants in S/Ex group had significant improvements for the outcome measures, including SMI and maximum walking time (P<0.05), compared to those in Ex group. The prevalence of sarcopenia decreased from 65.7% to 42.9% in S/Ex group, while that in Ex group remained unchanged (68.6% to 68.6%) (relative risk = 1.60, 95% CI: 1.03-2.49). Conclusion: The results of this study suggest that the combination of resistance training and multinutritional supplementation may be more effective at improving muscle mass and walking speed than an intervention only based on resistance training.
... The results showed that nitrogen balance and body weight in the hydrolyzed collagen-treated group were better than those of whey protein-treated group, indicating that the effect of hydrolyzed collagen was superior to that of the unhydrolyzed whey protein. 72 In addition, many collagen hydrolysate-derived dipeptides called hydroxyprolyl-glycine (Hyp-Gly) were identified in human blood after the intake of collagen. 73 It has been reported that Hyp-Gly can significantly promote myogenic differentiation and myotube hypertrophy of murine skeletal muscle C 2 C 12 cells by increasing myogenic fusion index, myotube size, and myotube-specific protein expression, suggesting that Hyp-Gly may be a promising dietary supplement to help repair the damaged skeletal muscle or increase skeletal muscle mass. ...
Sarcopenia is an age-related progressive muscle disorder characterized by accelerated loss of muscle mass, strength, and function, which are important causes of physiological dysfunctions in the elderly. At present, the main alleviating method includes protein supplements to stimulate synthesis of muscle proteins. Food protein-derived peptides containing abundant branched-chain amino acids have a remarkable effect on the improvement of sarcopenia. Understanding the underlying molecular mechanism and clarifying the structure-activity relationship is essential for the mitigation of sarcopenia. This present review recaps the epidemiology, pathogenesis, diagnosis, and treatment of sarcopenia, which facilitates a comprehensive understanding of sarcopenia. Moreover, the latest research progress on food-derived antisarcopenic peptides is reviewed, including their antisarcopenic activity, molecular mechanism as well as structural characteristics. Food-derived bioactive peptides can indeed alleviate/mitigate sarcopenia. These antisarcopenic peptides play a pivotal role mainly by activating the PI3K/Akt/mTOR and MAPK pathways and inhibiting the ubiquitin-proteasome system and AMPK pathway, thus promoting the synthesis of muscle proteins and inhibiting their degradation. Antisarcopenic peptides alleviate sarcopenia via specific peptides, which may be absorbed into the circulation and exhibit their bioactivity in intact forms. The present review provides a theoretical reference for mitigation and prevention of sarcopenia by food protein-derived bioactive peptides.
... As a result of the people's desire for good health conditions, scientists have developed some foods for their specialized purposes [1]. For instance, the production of red wine-based beverages may both nourish the blood and stimulate the body's metabolism. ...
Type I collagen has a relatively stable quality while quite resistant to digestion because of the complex triple helix structure. This study was conducted to explore the acoustic conditions of ultrasound (UD)-assisted calcium lactate processing of collagen and control the processing process through its sono-physico-chemical effects. The findings demonstrated that UD might lower the average particle size of collagen and increase its zeta potential. In contrast, the rise in calcium lactate concentration could dramatically limit the impact of UD processing. This may be because of its low acoustic cavitation effect, as demonstrated by the phthalic acid method (the fluorescence value decreased from 81245.67 to 18243.67). Poor changes in tertiary and secondary structures confirmed the detrimental effect of calcium lactate concentration on UD-assisted processing. Although UD-assisted calcium lactate processing can significantly alter the structure of collagen, the integrity of the collagen is basically preserved. Furthermore, the addition of UD and a trace amount of calcium lactate (0.1%) increased the roughness of the fiber structure. At this relatively low calcium lactate concentration, ultrasound improved the gastric digestibility of collagen by nearly 20%.
... Considering that collagen peptides have antioxidant and antibacterial properties and vary in quality depending on the technique of extraction, they can be employed as a component in functional dietary supplements. In view of the fact that collagen oral supplementation reaches the deeper layers of the skin and improves skin physiology and appearance by enhancing hydration, elasticity, firmness, wrinkle reduction, and skin regeneration, oral collagen supplementation has gained popularity in recent years [123,144]. Many studies have concluded that hydrolyzed fish collagen applied as food supplement is able to provide positive effects on skin appearance with enhanced water-holding capacity, moisture absorption, retention, anti-aging, and anti-melanogenic effects [59,145]. ...
Fish collagen garnered significant academic and commercial focus in the last decades featuring prospective applications in a variety of health-related industries, including food, medicine, pharmaceutics, and cosmetics. Due to its distinct advantages over mammalian-based collagen, including the reduced zoonosis transmission risk, the absence of cultural-religious limitations, the cost-effectiveness of manufacturing process, and its superior bioavailability, the use of collagen derived from fish wastes (i.e., skin, scales) quickly expanded. Moreover, by-products are low cost and the need to minimize fish industry waste’s environmental impact paved the way for the use of discards in the development of collagen-based products with remarkable added value. This review summarizes the recent advances in the valorization of fish industry wastes for the extraction of collagen used in several applications. Issues related to processing and characterization of collagen were presented. Moreover, an overview of the most relevant applications in food industry, nutraceutical, cosmetics, tissue engineering, and food packaging of the last three years was introduced. Lastly, the fish-collagen market and the open technological challenges to a reliable recovery and exploitation of this biopolymer were discussed.
... In contrast to whey protein, collagen protein hydrolysate supplementation alone does not elicit an acute response on MPS as it is an incomplete protein [165,171e173]. A small crossover study testing the effects of supplementing the diet (0.8 g/kg body weight/d of protein) with either collagen or whey protein for 15 days reported no changes in lean soft tissue of older women; although nitrogen balance was maintained with collagen, nitrogen excretion was higher with whey protein supplementation [174]. Collagen is rich in non-EAAs, which may explain its positive effects on nitrogen balance [165]. ...
Low muscle mass and malnutrition are prevalent conditions among adults of all ages, with any body weight or body mass index, and with acute or chronic conditions, including COVID-19. This article synthesizes the latest research advancements in muscle health and malnutrition, and their impact on immune function, and clinical outcomes. We provide a toolkit of illustrations and scientific information that healthcare professionals can use for knowledge translation, educating patients about the importance of identifying and treating low muscle mass and malnutrition. We focus on the emerging evidence of mitochondrial dysfunction in the context of aging and disease, as well as the cross-talk between skeletal muscle and the immune system. We address the importance of myosteatosis as a component of muscle composition, and discuss direct, indirect and surrogate assessments of muscle mass including ultrasound, computerized tomography, deuterated creatine dilution, and calf circumference. Assessments of muscle function are also included (handgrip strength, and physical performance tests). Finally, we address nutrition interventions to support anabolism, reduce catabolism, and improve patient outcomes. These include protein and amino acids, branched-chain amino acids, with a focus on leucine; β-hydroxy-β-methylbutyrate (HMB), vitamin D; n-3 polyunsaturated fatty acids (n-3 PUFA), polyphenols, and oral nutritional supplements. We concluded with recommendations for clinical practice and a call for action on research focusing on evaluating the impact of body composition assessments on targeted nutrition interventions, and consequently their ability to improve patient outcomes.
... Loss of collagen in the human body begins at the age of 18-29 years, after 40 years, the human body can lose about 1 % a year, and at about 80 years, collagen production may decrease by 75 % compared to young adults [14]. ...
This study was carried out to determine the impact of the HACCP control system on the safety of the final products of collagen hydrolysate production. The object of the study was equine connective tissue. Using the FMEA model, established by a three-factor assessment of the risk priority number (RPN), critical control points (CCP) in the processes of hydrolysis, inactivation of the enzyme preparation, drying and storage were identified. For two CCP, measures for continuous monitoring were identified, and critical limits were developed. For CCT 1, the calculation of optimal fermentation processes using a mathematical model for the hydrolysis of raw materials is given. The optimal values of the Neutrase enzyme, providing a maximum content of water-soluble proteins of 55.0 mg/cm3, were determined: T=37 °C, dosage 5 Pa/g, t=210 min.
For CCP 2, to avoid protein denaturation during hydrolysis, a critical limit was developed by determining the heat inactivation point and optimum temperature. Experimental analyses show that the inactivation point of the Neutrase enzyme, estimated by the rate of FTN accumulation, which has 20 % at 60 °C, is reached at the 11th minute.
As a result of the study, the effect of enzyme preparations on the safety of collagen hydrolysate was also determined. The result confirms that the Neutrase enzyme preparation had a positive effect on all safety indicators compared to the Trypsin enzyme. The optimal parameters for reducing microbiological indicators, pesticides, antibiotic and toxic metals are: T=40 °C, duration 210 min, dosage of the Neutrase enzyme 5 units/Pa.
The results can be used in collagen hydrolysate production to better ensure the quality and safety of the final product
... Furthermore, nitrogen excretion was lower with the collagen hydrolysate than with the whey, thus maintaining nitrogen balance and lean body mass. Also according to Hays et al. [24] the study data, combined with previous estimates of protein requirements in the diet of older people, strongly indicate that the current recommended dietary intake (RDA) may be inadequate or marginal, even in normocaloric diets. They also noted that although collagen hydrolysate is deficient in essential amino acids, combining it with a diet featuring adequate amounts of protein could promote nitrogen balance. ...
Collagen hydrolysate is recognized as a safe
nutraceutical, whose combination of amino acids stimulates the
synthesis of collagen in the extracellular matrix of cartilage and other
tissues. Objective: to conduct a systematic review of literature on the
action of collagen hydrolysate in bone and cartilaginous tissue and its
therapeutic use against osteoporosis and osteoarthritis. Method: a study
of the PubMed, MEDLINE, LILACS, and SciELO databases was
performed. Articles published in English and Portuguese in the period
of 1994 to 2014 were considered. Results: the sample comprised nine
experimental articles with in vivo (animals and humans) and in vitro (human cells) models,
which found that the use of different doses of collagen hydrolysate was associated with the maintenance of bone composition and strength, and the proliferation and cell growth of cartilage. Conclusion: hydrolyzed collagen has a positive therapeutic effect on osteoporosis and osteoarthritis with a potential increase in bone mineral density, a protective effect on articular cartilage, and especially in the symptomatic relief of pain.
... Exemplos de peptídeos bioativos derivados de proteínas alimentares e seus mecanismos de ação. superior em comparação com a proteína do soro na manutenção do equilíbrio de nitrogênio e do peso corporal durante uma dieta de baixa proteína(Hays et al., 2009). Além disso, o colágeno contém quantidades relativamente altas de arginina e glicina, ambas conhecidas como importantes substratos para a síntese de creatina no corpo humano(Zdzieblik et al., 2015). ...
... In the cornea, collagen tissue gets mechanical and optical properties. It is present in biological functions of the cell such as proliferation, cell survival, and differentiation; so collagen is present in the human body as a whole in bones, tendons, ligament, hair, skin, and muscles [2,114,115]. ...
Hydrolyzed collagen (HC) is a group of peptides with low molecular weight (3–6 KDa) that can be obtained by enzymatic action in acid or alkaline media at a specific incubation temperature. HC can be extracted from different sources such as bovine or porcine. These sources have presented health limitations in the last years. Recently research has shown good properties of the HC found in skin, scale, and bones from marine sources. Type and source of extraction are the main factors that affect HC properties, such as molecular weight of the peptide chain, solubility, and functional activity. HC is widely used in several industries including food, pharmaceutical, cosmetic, biomedical, and leather industries. The present review presents the different types of HC, sources of extraction, and their applications as a biomaterial.
... This protein source is generally regarded as having low biological value, mainly due to its low amounts of BCAA, lysine and tryptophan [14]. Recently, the consumption of hydrolysed collagen has been used in the prevention of lesions and tissues repairment [15], weight loss [16], fat free mass and muscle strength improvements [17]. However, there is little scientific evidence to substantiate the clinical use of collagen protein. ...
Protein supplements are usually used to control body weight, however, the impact of protein quality on body fat attenuation is unknown. We investigated the effects of isocaloric isoproteic supplementation of either whey protein (WG) or hydrolysed collagen supplementation (CG) on dietary intake, adiposity and biochemical markers in overweight women.
Methods:
In this randomized double-blind study, 37 women, [mean ± SE, age 40.6 ± 1.7 year; BMI (kg/m2) 30.9 ± 0.6], consumed sachets containing 40 g/day of concentrated whey protein (25 g total protein, 2.4 leucine, 1.0 valine, 1.5 isoleucine, n = 17) or 38 g/day of hydrolysed collagen (26 g total protein, 1.02 leucine, 0.91 valine, 0.53 isoleucine, n = 20) in the afternoon snack. The compliance was set at >70% of the total theoretical doses. The dietary intake was evaluated by a 6-day food record questionnaire. At the beginning and after eight weeks of follow-up, body composition was evaluated by using dual-energy X-ray absorptiometry and lipid profile, insulin resistance, C-reactive protein, adiponectin, leptin and nesfastin plasma concentrations were analyzed.
Results:
Supplements were isocaloric and isoproteic. There were no differences in caloric intake (p = 0.103), protein (p = 0.085), carbohydrate (p = 0.797) and lipids (p = 0.109) intakes. The branched chain amino acids (BCAA) (GC: 1.8 ± 0.1 g vs. WG: 5.5 ± 0.3 g, p < 0.001) and leucine intake (CG: 0.1 ± 0.1 g vs. WG: 2.6 ± 0.1 g, p < 0.001) were higher in WG compared to CG. BMI increased in the CG (0.2 ± 1.1 kg/m2, p = 0.044) but did not change in WG. WG decreased the android fat (-0.1 ± 0.3 kg, p = 0.031) and increased nesfatin concentrations (4.9 ± 3.2 ng/mL, p = 0.014) compared to CG.
Conclusions:
Whey protein supplementation in overweight women increased nesfatin concentrations and could promote increase of resting metabolic rate as part of body composition improvement programs compared to collagen supplementation for 8 weeks. Additionally, our findings suggest that collagen may not be an effective supplement for overweight women who are attempting to alter body composition.
... Nevertheless, since the N content is higher than in whey on per gram basis, the combination of amino acids has been shown to be superior in maintaining N balance and body weight during a low-protein diet. 93 Moreover, this protein contains relatively high amounts of arginine and glycine, both known to be important substrates for the synthesis of creatine in the human body. 94 Although hydrolyzed collagen is contained in sports drinks and bars aimed at improving regeneration and post-exercise muscle recovery to our knowledge there are few studies on the use of this protein for nutritional supplementation with resistance exercise in elderly people. ...
Sarcopenia is a major contributor to the risk of physical frailty, functional decline, poor health-related quality of life and premature death in older people. Sarcopenia can be considered a geriatric syndrome. The term sarcopenia indicates the loss of muscle mass that accompanies aging. Muscle mass declines with aging process with differences between subjects in relation to the presence of chronic diseases, to lifestyles habits (mainly diet and physical activity), to cognitive status. Sarcopenia in the elderly is associated with poor health outcomes, such as falls, disability, loss of independence, and mortality; however, it is potentially treatable if recognized and intervened early. The prevalence of sarcopenia rates between 5% and 13% in community-dwelling older people aged 65 years and over, and is higher in those 80 years and older (20-25%). The cause of sarcopenia is generally thought to be multifactorial, with environmental causes, disease triggers, inflammatory pathway activation, and a large number of cellular and biochemical abnormalities. Resistance training and amino acid supplementation are a recommended practice for the prevention of sarcopenia. The essential elements for the management of the sarcopenic patient are the recognition of a condition of frailty, an accurate multidimensional geriatric assessment, with attention to cognitive problems, mood, functional problems, living conditions, using standardized instruments. Combining exercise with some pharmacological compounds such as β- Hydroxy-β-methylbutyrate (HMB) and dietary supplements (including proteins, aminoacids and vitamin D) may exert a beneficial effect on older adults thus influencing the progress to sarcopenia. The recommended daily amount of protein is greater for older people. Vitamin D and leucine enrichment seems mandatory in order to improve muscle mass and lowerextremity function among sarcopenic older adults. There are some evidences that collagen peptides in this setting might be even superior to whey protein in promoting muscle growth and increasing the mobility.
... In an attempt to make these possible, numerous products are now being developed and commercialized. Among them is collagen that has been widely used as a material in food, cosmetic, and pharmaceutical industries due to its biological and functional properties [5]. In a recent randomized controlled trial, post-exercise supplementation of a collagen peptide in combination with resistance training was seen to improve body composition and increase muscle strength in 148 elderly sarcopenic men [6]. ...
Recent animal studies found the potential of a collagen peptide derived from skate skin to have anti-obesity effects through the suppression of fat accumulation and regulation of lipid metabolism. However, no studies have yet been performed in humans. Here, this very first human randomized, placebo-controlled, and double-blinded study was designed to investigate the efficacy and tolerability of skate skin collagen peptides (SCP) for the reduction of body fat in overweight adults. Ninety healthy volunteers (17 men) aged 41.2 ± 10.4 years with a mean body mass index of 25.6 ± 1.9 kg/m² were assigned to the intervention group (IG), which received 2000 mg of SCP per day or to the control group (CG) given the placebo for 12 weeks and 81 (90%) participants completed the study. Changes in body fat were evaluated using dual energy X-ray absorptiometry as a primary efficacy endpoint. After 12 weeks of the trial, the percentage of body fat and body fat mass (kg) in IG were found to be significantly better than those of subjects in CG (−1.2% vs. 2.7%, p = 0.024 and −1.2 kg vs. 0.3 kg, p = 0.025). Application of SCP was well tolerated and no notable adverse effect was reported from both groups. These results suggest the beneficial potential of SCP in the reduction of body fat in overweight adults.
... unbalanced dietary intake [6][7][8], while potentially limiting the risks of excessive protein intake [4]. Fortified milk products have also emerged for adolescent or adult populations such as the elderly, offering a means of caloric regulation [9] or micronutrient and protein enrichment [10,11] of the diet. ...
Fortified milk drinks are predominantly manufactured from bovine (cow) sources. Alternative formulations include those prepared with hydrolysed bovine milk proteins or from alternate bovidae species, such as caprine (goat) milk. Currently, there is little data on protein digestive and metabolic responses following ingestion of fortified milk drinks. To examine the digestive and metabolic responses to commercially-available fortified milks, young adults (n = 15 males: 15 females), in a randomised sequence, ingested isonitrogenous quantities of whole cow-protein (WC), whole goat-protein (WG), or partially-hydrolysed whey cow-protein (HC), commercial fortified milks. Plasma amino acid (AA) and hormonal responses were measured at baseline and again at 5 h after ingestion. Paracetamol recovery, breath hydrogen, and subjective digestive responses were also measured. Postprandial plasma AA was similar between WC and WG, while AA appearance was suppressed with HC. Following HC, there was a negative incremental AUC in plasma branched-chain AAs. Further, HC had delayed gastric emptying, increased transit time, and led to exaggerated insulin and GLP-1 responses, in comparison to whole protein formulas. Overall, WC and WG had similar protein and digestive responses with no differences in digestive comfort. Contrastingly, HC led to delayed gastric emptying, attenuated AA appearance, and a heightened circulating insulin response.
... 21 Collagen has also acquired importance in protein supplements, where they have been shown to be useful in maintaining the nitrogen balance in older people. 22 The analysis of collagen can be an aid in meat authentication because different amounts of collagen are present in different meat cuts 23 and collagen content has also been used as an index of the quality for meat sausages. 24 The quantity and type of the collagen present in biomaterials must be thoroughly evaluated as collagen plays an important role in refining cellular behaviour and tissue function. ...
Collagen is the most abundant protein in the extracellular matrix of animals and is mainly composed of amino acids glycine, proline and hydroxyproline.Collagen has been used in haemostatic sponges, dermal equivalents, injectables, and as a vehicle for drug delivery. The quantity and properties of the collagen present in biomaterials must be thoroughly evaluated as the collagen may influence the properties of biomaterials. Hydroxyproline (Hyp) plays key role in collagen stability by permitting the sharp twisting of collagen helix and quantification of Hyp is an indicator of collagen content. The main objective of this study is to validate different tissue hydrolysis methods in order achieve simple, fast and reproducible method for quantification of collagen in biomaterials. Bovine pericardium used in cardiovascular surgery was used as a source material for collagen in the present study. We estimated amounts of collagen present in the bovine pericardium by hydrolysing with collagenase type 1, trypsin, sodium hydroxide (NaOH), hydrochloric acid (HCl) and sulphuric acid (H 2 SO 4) singularly. We have observed 13.5 mg of collagen/100 mg of in pericardial tissue hydrolysed by collagenase type 1 treatment and similarly 4.45 mg by trypsin, 16.9 mg by NaOH, 7.55 mg by HCl and 29.45 mg of collagen / 100 mg tissue by H 2 SO 4 was quantified. Simultaneously we have tested the robustness and reproducibility of H 2 SO 4 hydrolysis method. Our study shows tissue hydrolysis by H 2 SO 4 is more efficient, simple and fast for estimation of collagen in biomaterials.
... Protein supplements (e.g. collagen hydrolysates) may be useful to enhance nitrogen retention [10]. ...
Paper reviews literature data connected with properties of collagen hydrolysates applied as diet supplements. Biological and health promoting activity of collagen derived peptides has been well documented in many studies, especially for the therapeutical treatment of bones and joints diseases as well as for the improvement of skin, hair and nails conditon. High tolerance of patients for long-term ingested collagen hydrolysates make them attractive for use as health promoting diet supplement.
... 37,38 In fact, protein supplementation has been shown to augment the muscle strengthening effect of resistance exercise. 39,40 Therefore, the Society for Sarcopenia, Cahexia, and Wasting Disease (SSCWD) recently recommended the combination of exercise with protein and/or vitamin D supplementation for reducing the agerelated skeletal muscle decline. 41 The results of the current study also supported the SSCWD recommendation, and the nutritional supplementation provided added benefits to those with walking exercise for increasing muscle mass. ...
The aim of the Intervention by Nutrition and Exercise (INE) study was to investigate the effects of a mail-based intervention for sarcopenia prevention on muscle mass and anabolic hormones in community-dwelling older adults.
A cluster-randomized controlled trial.
This trial recruited community-dwelling adults aged 65 years and older in Japan. The 227 participants were cluster randomized into a walking and nutrition (W/N) group (n = 79), a walking (W) group (n = 71), and a control (C) group (n = 77). We analyzed the physical and biochemical measurements in this substudy.
Six months of mail-based intervention (a pedometer-based walking program and nutritional supplementation).
The skeletal muscle mass index (SMI) using the bioelectrical impedance data acquisition system, biochemical measurements, such as those of insulinlike growth factor (IGF-1), dehydroepiandrosterone sulfate (DHEA-S), and 25-hydroxy vitamin D (25[OH]D), as well as frailty, were assessed by the Cardiovascular Health Study criteria.
Participants in the W/N and W groups had significantly greater improvements in SMI, IGF-1, and 25(OH)D (P < .05) than those in the C group. Participants in the W/N group had significantly greater improvements in DHEA-S (P < .05) than in the other groups. These effects were more pronounced in frail, older adults.
These results suggest that the mail-based walking intervention of the remote monitoring type for sarcopenia prevention can increase anabolic hormone levels and SMI in community-dwelling older adults, particularly in those who are frail.
Copyright © 2015 AMDA – The Society for Post-Acute and Long-Term Care Medicine. Published by Elsevier Inc. All rights reserved.
... In the food industry, this protein is widely used to improve the elasticity, consistency and stability of foods (Santana, Sato, & da Cunha, 2012) in a wide variety of products, such as drinks, soups, noodles, candies and meat products (Taffin & Pluvinet, 2006). Collagen hydrolysates have also acquired importance in protein supplements, where they have been shown to be useful in maintaining the nitrogen balance in older people (Hays, Kim, Wells, Kajkenova, & Evans, 2009). The analysis of collagen can be an aid in meat authentication because different amounts of collagen are present in different meat cuts (Ballin, 2010). ...
... Both whey and caseinate supplementation induced a similar increase in protein synthesis after heavy resistance training in healthy elderly participants [12]. Interestingly, a fortified, hydrolyzed collagen protein supplement added to a relatively low-protein diet maintained LBM to a greater extent than whey protein [34]. In some studies [7,11,13], supplementation with essential amino acids improved LBM or muscle protein synthesis rate in elderly subjects; however, another study did not find any benefit of supplementing with amino acids [14]. ...
Objective
A major reason for the loss of mobility in elderly people is the gradual loss of lean body mass known as sarcopenia. Sarcopenia is associated with a lower quality of life and higher healthcare costs. The benefit of strategies that include nutritional intervention, timing of intervention, and physical exercise to improve muscle loss unclear as finding from studies investigating this issue have been inconsistent. We have performed a systematic review and meta-analysis to assess the ability of protein or amino acid supplementation to augment lean body mass or strength of leg muscles in elderly patients.
Methods
Nine studies met the inclusion criteria of being a prospective comparative study or randomized controlled trial (RCT) that compared the efficacy of an amino acid or protein supplement intervention with that of a placebo in elderly people (≥65 years) for the improvement of lean body mass (LBM), leg muscle strength or reduction associated with sarcopenia.
Results
The overall difference in mean change from baseline to the end of study in LBM between the treatment and placebo groups was 0.34 kg which was not significant (P = 0.386). The overall differences in mean change from baseline in double leg press and leg extension were 2.14 kg (P = 0.748) and 2.28 kg (P = 0.265), respectively, between the treatment group and the placebo group.
Conclusions
These results indicate that amino acid/protein supplements did not increase lean body mass gain and muscle strength significantly more than placebo in a diverse elderly population.
... Regarding our second strategy, replacing casein by whey proteins had also no effects on lean body mass, muscle protein synthesis and degradation rates. This result is in accordance with recent long term studies in rats [38] and in humans [39], and is also consistent with studies showing that long-term leucine supplementation had no effects on lean body mass or muscle mass in rats [40,41] and in humans [42,43]. However, studies are also in agreement to show that acute supplementation with leucine or whey proteins restore stimulation of muscle protein synthesis in old rats [9] or elderly humans [44]. ...
Our aim was to compare and combine 3 nutritional strategies to slow down the age-related loss of muscle mass in healthy old rats: 1) increase protein intake, which is likely to stimulate muscle protein anabolism; 2) use leucine rich, rapidly digested whey proteins as protein source (whey proteins are recognized as the most effective proteins to stimulate muscle protein anabolism). 3) Supplement animals with a mixture of chamomile extract, vitamin E, vitamin D (reducing inflammation and oxidative stress is also effective to improve muscle anabolism). Such comparisons and combinations were never tested before. Nutritional groups were: casein 12% protein, whey 12% protein, whey 18% protein and each of these groups were supplemented or not with polyphenols/antioxidants. During 6 months, we followed changes of weight, food intake, inflammation (plasma fibrinogen and alpha-2-macroglobulin) and body composition (DXA). After 6 months, we measured muscle mass, in vivo and ex-vivo fed and post-absorptive muscle protein synthesis, ex-vivo muscle proteolysis, and oxidative stress parameters (liver and muscle glutathione, SOD and total antioxidant activities, muscle carbonyls and TBARS). We showed that although micronutrient supplementation reduced inflammation and oxidative stress, the only factor that significantly reduced the loss of lean body mass was the increase in whey protein intake, with no detectable effect on muscle protein synthesis, and a tendency to reduce muscle proteolysis. We conclude that in healthy rats, increasing protein intake is an effective way to delay sarcopenia.
For the mixed aqueous solution of LSL and COP, the interaction mode and mechanism have been comprehensively studied using multispectral methods including fluorescence spectrum, ultraviolet‐visible adsorption spectrum (UV‐Vis), and circular dichroism spectrum (CD). Then its surface activity, particle size, foaming, emulsifying, viscosity, and antibacterial properties are evaluated in detail by surface tension measurement (ST), dynamic light scattering (DLS), oscillametric method, spectrophotometer, ubbelohde viscometer and zone of inhibition separately. Compared with the single LSL or COP aqueous solution, the mixed system shows different performance optimizations in different aspects. The surface activity and foaming properties are mainly attributed to LSL, and the viscosity is attributed to COP. Fluorescence spectroscopy results show that the fluorescence distribution of COP has significant changes by the LSL addition and a static quenching mechanism is proved. The results of UV‐Vis and CD spectra also show the changing conformation of COP by the LSL addition. The data of thermodynamic parameters prove that the combination of LSL and COP is a spontaneous exothermic process and is an enthalpy‐driven process. The interaction mechanism between LSL and COP is very helpful for the application and development of the mixed mild biosurfactant‐protein system used in the cosmetic and food industries.
Osteoarthritis (OA) is the most common joint disease that significantly affects the patients’ quality of life and requires significant medical and social investments for treatment and rehabilitation. There are no therapeutic agents which would be able to regenerate lost or damaged hyaline cartilage. The objective: to assess the efficacy and safety of the chondroprotective parapharmaceutical agent Flexogial in the complex treatment of patients with initial stages of the knee ОА. Materials and methods. 12-weeks study was conducted with the participation of 60 patients with knee OA aged 53,7±2,9 years, women – 36 (60%), men – 24 (40%) with the initial stages of the disease (I–II radiological stage). The main clinical group consisted of 30 patients who took the chondroprotective complex agent Flexogial 15 ml once a day; the comparison group included 30 patients who were administered glucosamine sulfate 1500 mg in a monopreparation taken once a day. Efficacy of the treatment was evaluated using the VAS scale, Tegner’s scale, Lisholm scale at the beginning of treatment, after 6 and 12 weeks in dynamics with subsequent statistical processing of the results. Results. The study demonstrated better indicators of functional activity and less pain intensity in the affected joints in patients of the main group who took the parapharmaceutical agent Flexogial compared to the group of patients who took glucosamine monopreparation with the same number of registered adverse events in both groups of patients (5%). Conclusions. The results of the presented clinical study proved the advantage of use of the combined chondroprotective drinking complex Flexogial in comparison with the monopharmaceutical preparation glucosamine sulfate in the treatment of patients with early stages knee OA in terms of the effect on the intensity of pain and improvement in the parameters of the functional activity of patients after 6 and 12 weeks with the same frequency of registered adverse events.
The encapsulation efficiency of spray-dried cocona pulp encapsulated with a blend of maltodextrin (MD) and hydrolyzed collagen (HC) (CP-ENC) and the stability, color parameters, antioxidant capacity (FRAP and ABTS), and 5-caffeoylquinic acid content were evaluated through 120 days of storage, at every 15 days, at 25 and 35°C. The results of CP-ENC were compared to those of pure freeze-dried cocona pulp (CP-nENC). The sorption iso-therms and glass transition temperatures (Tg) were determined in order to evaluate the stability of the cocona powder. The GAB model fitted well the experimental data for moisture sorption of samples. The high Tg for CP-ENC (132.02°C) was attributed to the high molecular weight of encapsulating agents. The encapsulation efficiency and color parameters for CP-ENC kept constant values for 120 days. A loss of 30% in the antioxidant capacity occurred on day 75 for CP-ENC. The values of retention of 5-CQA for CP-ENC (83% and 68% when stored at 25 and 35°C, respectively) were greater than those observed for CP-nENC. At 25°C, stored CP-ENC had a higher retention and a longer half-life of 5-CQA (14.4 months) than CP-nENC. The results suggest that it is suitable to microencapsulate cocona pulp with MD and HC to improve protection of antioxidant compounds, throughout storage at 25°C.
Background and objectives:
The present study was conducted to evaluate the effect of cod skin peptide (CSPE) on chemotherapy-induced toxicity in gastric cancer patients.
Methods and study design:
A cohort of 60 gastric cancer patients for chemotherapy was randomly divided into two groups (n=30 per group), who were orally treated with either supplemental CSPE or placebo apart from chemotherapy. The hematologic and gastrointestinal toxicities experienced by the patients, as well as their Karnofsky Performance Status (KPS) as an index of quality of life was evaluated.
Results:
Leukocyte counts and haemoglobin levels were significantly reduced in the group treated with peptide (p<0.05), while gastrointestinal toxicity was not affected (p>0.05). KPS consists of 11 categories of quality of life, and the score denoted in deciles ranges from 100 (asymptomatic, normal function) to 0 (death). The KPS score is used to evaluate a cancer patient's ability to function at work and home, the severity of symptoms, and the patient's need for personal and medical care. Treatment with CSPE significantly improved the quality of life of patients, as indicated by increased KPS scores (p<0.05).
Conclusions:
CSPE can potentially be considered as a food supplement that can be used to improve the quality of life of cancer patients.
The goal of the present work was to prepare bioactive hydrolysates and peptides from sunflower protein isolate (free of chlorogenic acid). To reach this goal the protein isolate was hydrolysed using several enzymes and enzyme mixtures, including: pepsin, trypsin, chymotrypsin and a mixture of the three enzymes (mixture I); also alcalase, flavourzyme and a mixture of the two enzymes (mixture II). These enzymes were used at 2% concentration and at pH and temperature reported by the manufacturer. During hydrolysis, at certain time intervals, 30, 60 and 120 min. aliquots were withdrawn from the reaction mixture to give peptide fractions and at the end of 3h give hydrolysate. The peptic fractions exhibited prooxidant activities at 30, 60 and 120 min. Other hydrolysis products revealed moderate antioxidant activity (AOA). Tryptic peptide at 60 min. hydrolysis showed the highest AOA (94.32%), followed by 61.21% for the hydrolysate at 180 min. and very low AOA values were exhibited by all chymotryptic peptides and hydrolysate. The peptides resulting from enzyme mixture I were prooxidative after 30 and 60 min. because they resulted from peptic hydrolysis then on adding the two other enzymes, the AOA was raised to 38.75 and 44.06% after 120 and 180 min., respectively. Hydrolysis using alcalase and flavourzyme gave peptides with moderate AOA ranging from 31.10-48.44% and from 10.5- 43.19%, respectively. Upon using the mixture II the AOA was improved to 53.05 and 79.37%, after 120 and 180 min., respectively. Some peptides and hydrolysates were chosen for testing their anti-microbial activity. All tested hydrolysis products showed different antimicrobial activity. Enzymatic hydrolysis of the protein isolate with enzyme mixture II (alcalase and flavourzyme) resulted in products that inhibited all the five microbial strains tested. Chymotryptic hydrolysate, mixture I Hydrolysate and a peptide fraction from flavourzyme inhibited four bacterial strains.
Introduction:
hydrolysate Collagen (HC) consists of small peptides with a molecular weight lower than 5.000 Da. produced from gelatinization and subsequent enzymatic hydrolysis of native collagen which is found in rich collagenic animal tissues. There is much evidence about the HC ingestion positive effect over degenerative joint and bones diseases.
Objective:
the aim of this article is to review the present scientific studies about HC and to evaluate the HC ingestion therapeutical effects on some collagenic tissues as cartilage, bones and skin.
Results:
up to date, there are more than 60 scientific studies (in vitro, in vivo, clinics and on bioavailability) about HC ingestion efficacy on reducing collagen damage and loss consequences as joint pain and erosion (osteoarthritis), bone density loss (osteoporosis) and skin ageing Conclusions: preclinical studies show that HC stimulates collagenic tissue regeneration by increasing not only collagen synthesis but minor components (glycosaminoglycans and hyaluronic acid) synthesis as well. Clinical studies show that HC continual ingestion helps to reduce and prevent joint pain, bone density loss and skin ageing. These results as well as its high level of tolerance and safety make HC ingestion attractive for a long-term use in bone and joint degenerative diseases and in fight against skin ageing.
Aging is associated with a decline in skeletal muscle mass that accelerates the process of sarcopenia. An acute condition of the elderly that necessitates intensive care unit admission may aggravate the loss of lean body mass and increase the formation of free radicals. Enteral nutrition is the preferred route for early feeding in critically ill elderly patients. Whey protein may have antioxidant properties due to the rich concentration of cysteine, which is essential for the production of glutathione, one of the most important organic scavengers. There is clinical evidence that enteral nutrition with formulas containing whey proteins may benefit the elderly in acute conditions, especially in oxidative stress. Vitamins, such as E, C, and carotene, and trace elements, such as copper, manganese, zinc, iron, and selenium, are required for antioxidant defenses. Recently, a meta-analysis showed a reduction in mortality, infectious complications, and days on the ventilator in critically ill patients who received a diet containing micronutrients and vitamins.
The primary objective of the present systematic review and meta-analysis was to synthesize the available literature relating to leucine supplementation in the elderly with respect to its effects on anthropometrical parameters and muscle strength. The secondary aim was to perform a selective subgroup analysis when possible differentiating between healthy and sarcopenic subjects.
Literature search was performed using the electronic databases MEDLINE, EMBASE, SportDiscus, and the Cochrane Central Register of trials with restrictions to randomized controlled trials or studies following a cross-over design. Parameters taken into account were body weight, body mass index, lean body mass, fat mass, percentage of body fat, hand grip strength, and knee extension strength. Moreover, biomarkers of glucose metabolism (fasting glucose, fasting insulin, albumin, and HOMA index) were extracted when possible. For each outcome measure of interest, a meta-analysis was performed in order to determine the pooled effect of the intervention in terms of weighted mean differences between the post-intervention (or differences in means) values of the leucine and the respective control groups. Data analysis was performed using the Review Manager 5.2.4. software.
A total of 16 studies enrolling 999 subjects met the inclusion criteria. Compared with control groups, leucine supplementation significantly increased gain in body weight [mean differences 1.02 kg, 95%-CI (0.19, 1.85), p=0.02], lean body mass [mean differences 0.99 kg, 95%-CI (0.43, 1.55), p=0.0005], and body mass index [mean differences 0.33 kg/m2, 95%-CI (0.13, 0.53), p=0.001], when compared to the respective control groups. With respect to body weight and lean body mass, leucine supplementation turned out to be more effective in the subgroup of study participants with manifested sarcopenia. All other parameters under investigation were not affected by leucine supplementation in a fashion significantly different from controls.
It is concluded that leucine supplementation was found to exert beneficial effects on body weight, body mass index, and lean body mass in older persons in those subjects already prone to sarcopenia, but not muscle strength. However, due to the heterogeneity between the trials included in this systematic review, further studies adopting a homogenous design with respect to participant characteristics duration as well as the kind and amount of daily supplement in use are required.
This study assessed the current EAR, RDA, and AMDR for protein, which were set in 2005 and revised in 2010 as the DRIs for Koreans. A classical approach to establish the EAR for protein has been the nitrogen balance method. This method has practical limitations and problems in statistical analysis by giving over estimations of nitrogen balance. Thus, the present EAR for protein might be lower than the true requirement. Recent reevaluations of nitrogen balance studies by bilinear regression analysis and the IAAO method have indicated that the EAR of 0.66 g/kg bw/d should be increased by 39% to give 0.92 g/kg bw/d. The AMDR for protein in the Korean DRIs was set at 7-10%, which covers almost the entire population's protein intake. Since the 5th percentile of Korean protein intake is close to 10% of energy and due to the beneficial effects of protein beyond the maintenance of nitrogen equilibrium, the lower range of 7% needs to be increased up to 10%. For practical meal arrangement, 15% of energy as protein, which is close to the average protein intake of Koreans, seems to be proper, although the value is almost two times the EAR.
The purpose of this systematic review is to assess the evidence behind the dietary requirement of protein and to assess the health effects of varying protein intake in healthy elderly persons in order to evaluate the evidence for an optimal protein intake. The literature search covered year 2000-2011. Prospective cohort, case-control, and intervention studies of a general healthy population in settings similar to the Nordic countries with protein intake from food-based sources were included. Out of a total of 301 abstracts, 152 full papers were identified as potentially relevant. After careful scrutiny, 23 papers were quality graded as A (highest, n=1), B (n=18), or C (n=4). The grade of evidence was classified as convincing, probable, suggestive, or inconclusive. The evidence is assessed as: probable for an estimated average requirement (EAR) of 0.66 g good-quality protein/kg body weight (BW)/day based on nitrogen balance (N-balance) studies and the subsequent recommended dietary allowance (RDA) of 0.83 g good-quality protein/kg BW/day representing the minimum dietary protein needs of virtually all healthy elderly persons. Regarding the optimal level of protein related to functional outcomes like maintenance of bone mass, muscle mass, and strength, as well as for morbidity and mortality, the evidence is ranging from suggestive to inconclusive. Results from particularly prospective cohort studies suggest a safe intake of up to at least 1.2-1.5 g protein/kg BW/day or approximately 15-20 E%. Overall, many of the included prospective cohort studies were difficult to fully evaluate since results mainly were obtained by food frequency questionnaires that were flawed by underreported intakes, although some studies were 'calibrated' to correct for under- or over-reporting. In conclusion, the evidence is assessed as probable regarding the EAR based on N-balance studies and suggestive to inconclusive regarding an optimal protein intake higher than the estimated RDA assessed from N-balance studies, but an exact level cannot be determined. Potentially adverse effects of a protein intake exceeding 20-23 E% remain to be investigated.
The progressive aging of populations coupled with the increasing prevalence of cancer in elderly people, due to their long exposure to potential oncogenic factors, represents a formidable challenge for the health system. Moreover, whereas in many adult cancer patients, malignancy represents the primary basic target to be treated, in the elderly patients a concurrent status of sarcopenia multiplies the risk of aggressive therapies and forces the clinician to maintain a holistic view of his patient.A common problem for the elderly cancer patient is the progressive malnutrition which is due to coexistence and/or potentiation of the metabolic alterations related to sarcopenia with underlying cancer cachexia. Both processes lead to loss of body weight, lean body mass, and muscle function, as well as a progressive deterioration of function of many organ/systems, a poor quality of life and finally to a poor adaptation to any stress event.Although neither sarcopenia nor cancer cachexia may be reduced to a condition of simple starvation, an adequate nutritional intake is the conditio sine qua non which can make possible any attempt of aggressive oncologic therapies which are validated in adult subjects.This paper, after a short review of topics including the interaction between sarcopenia and cancer cachexia, the nutritional status as a component of geriatric assessment tools, the prevalence of malnutrition and the negative prognostic role of malnutrition, focuses on the theoretical and practical aspects of the nutritional support of the elderly cancer patient.
Background: Recent studies suggested that pedometer-based walking programs are applicable to older
adults. Objectives: The purpose of this study was to evaluate the use of pedometer in sedentary older adults to improve physical activity, fear of falling, physical performance, and leg muscle mass. Design: This was a pilot randomized controlled trial (RCT). Setting and participants: Eighty-seven community dwelling sedentary older
adults living in Japan. Intervention: The intervention group (n=43) received a pedometer-based behavioural change program for 6 months, while the control group (n=44) did not. The participants in the intervention group were instructed to increase their mean daily steps by 10% each month. Thus, at the end of 6 months, participants in the intervention group were expected to have 77 % more daily steps than their baseline step counts. Written activity logs were monthly averaged to determine whether the participants were achieving their goal.
Measurements: Outcome measures were physical activity, fear of falling, physical performances, and leg muscle mass. Results: In this 6-month trial 40 older adults (93%) completed the pedometer protocol with good adherence. In the intervention group, average daily steps were increased by 83.4% (from 20311323 to 3726 1607) during the study period, but not in the control group (from 20471698 to 22671837). The pedometer-based behavioral change program was more effective to improve their physical activity, fear of falling, locomotive function, and leg muscle mass than control (P<0.05). Conclusion: These results suggested that the pedometer-based behavioral change program can effectively improve the physical activity, fear of falling, physical
performance, and leg muscle mass in sedentary older adults.
The aging process is a continuum throughout life and often associated with deterioration of body function as well as accumulation of chronic disabilities and of disease. The impact of nutritional status on morbidity and mortality is unquestioned. Malnutrition increases the risk for frailty and nutritional deficits can influence immune status, response to medical treatments and recovery from acute illnesses, including surgery. Health-promoting interventions implemented individually, such as exercise programs, preventive home visits, comprehensive geriatric evaluation and management, and attention to adequate nutrition with or without nutritional supplements, have been shown in separate studies to be both feasible and effective in reducing age-related deterioration. Protein and its constituent amino acids (AA) are key components of any healthy diet. Sarcopenia, the slow but progressive loss of lean muscle mass associated with advancing age, has been the focus of many studies but there is no clear-cut answer to the question of how to restrain the process. The more general question of how the requirements for protein and specific AA change with age continues to be investigated. A shift towards studying the efficacy and safety of specific AA or combination of AA that may sustain and/or enhance physiologic processes, ranging from specific tissue metabolism to overall function (e.g. exercise performance, immune function, cognition, and chronic disease development) has occurred. This review focuses on recent studies examining the use of specific AA or mixtures as supplements in the elderly and whether/how AA may assist in the maintenance of health and independence.
PURPOSE:: To enhance the learner's competence with knowledge of nutritional strategies for frail older adults. TARGET AUDIENCE:: This continuing education activity is intended for physicians and nurses with an interest in skin and wound care. OBJECTIVES:: After participating in this educational activity, the participant should be better able to:1. Analyze how normal aging, sarcopenia, anorexia, malnutrition, and Alzheimer's disease impact the nutrition of older adults.2. Apply evidence-based guidelines to improve nutritional status and wound healing in older adults. ABSTRACT: The objectives of this continuing education article are to analyze the aging process and its effect on the nutritional status of frail older adults; determine how sarcopenia, anorexia, malnutrition, and Alzheimer disease increase the risk for pressure ulcer development and impact the healing process; and to apply evidence-based nutrition guidelines and implement practical solutions for wound healing.
Dietary proteins are found in animal products, plant products and single-cell organisms. Proteins are present in variable proportions in these different food sources and the different proteins also differ in their amino acid composition, dietary indispensable amino acid content and physico-chemical properties. Different criteria can be used to define dietary protein requirements and different markers can be used to assess nutritional protein quality according to the criteria used for protein requirement estimation. The current approach to determining protein requirements is related to nitrogen balance and the dietary indispensable amino acid score approach relates protein quality to the capacity of protein to allow reaching nitrogen balance by providing nitrogen and indispensable amino acids. A second approach considers more directly protein nitrogen utilization by the body and includes measurement of protein digestibility and of the efficiency of dietary nitrogen retention at maintenance or for protein deposition at the whole body level or in more specific body areas. Another approach is related to protein turnover and protein synthesis in relation to maintenance and/or efficiency for deposition or development (growth) at the whole body level or for different and more specific target tissues such as muscle or bone. Lastly, protein quality can also be evaluated from different markers used as risk factors for metabolic dysfunction and disorders related for instance to insulin resistance, diabetes and obesity or cardio-vascular disease. The accuracy and relevance of these different approaches is discussed regarding the capacity of the different protein sources (i.e. animal as meat, milk or eggs, legume as soya or pea, or cereal as wheat or rice) to satisfy protein requirements according to these different criteria and markers.
Age-related cognitive decline (ARCD) and dementia are of increasing concern to an ageing population. In recent years, there has been considerable research focused on effective dietary interventions that may prevent or ameliorate ARCD and dementia. While a number of studies have considered the impact that dairy products may have on physiological health, particularly with regard to the metabolic syndrome and cardiovascular health, further research is currently needed in order to establish the impact that dairy products have in the promotion of healthy brain function during ageing. The present review considers the available evidence for the positive effects of dairy products on the metabolic syndrome and glucose regulation, with consideration of the implications for neurocognitive health. A literature search of current (September 2010) meta-analyses/reviews and original research regarding dairy products and cognition was conducted through SCOPUS using the following search terms for dairy consituents: dairy, milk, cheese, yoghurt, probiotics, whey protein, alpha lactalbumin, calcium, B-12, bioactive peptides and colostrinin (CLN). These search terms for dairy products were combined with the following search terms related to cognition and health: cognition, cognitive decline, dementia, Alzheimer's disease, metabolic syndrome, diabetes, insulin resistance and glucose regulation. Concerns regarding SFA and other fatty acids found in dairy products are also reviewed in relation to different forms of dairy products. The review also considers recent evidence for positive neurocognitive effects associated with bioactive peptides, CLN and proline-rich polypeptides, α-lactalbumin, vitamin B12, calcium and probiotics. Future directions for the extraction and purification of beneficial constituents are also discussed. It is concluded that low-fat dairy products, when consumed regularly as part of a balanced diet, may have a number of beneficial outcomes for neurocognitive health during ageing.
The aim of this study was to investigate the effects of an early enteral formula containing whey protein, in comparison to a standard enteral formula containing casein as the protein source, on the levels of glutathione and inflammatory markers in aged patients with acute ischemic stroke.
Thirty-one elderly patients (12 males and 19 females; median age = 74 [range,65-90] y old) with ischemic stroke were randomized to receive early nasogastric feeding (35 kcal/kg/d and 1.2 g of protein/kg/d) with either a formula containing polymeric [corrected] casein (casein group, n =16) or another isocaloric and isonitrogenous formula containing hydrolyzed whey protein (WP group, n = 15) for 5 d. The primary endpoints of the study were the changes in the serum levels of glutathione peroxidase, C-reactive protein (CRP), and interleukin 6 (IL-6).
Twenty-five patients completed the study (10 in the WP group and 15 in the casein group). Mortality was similar between groups (33%; P = 1.00) and was associated with higher serum IL-6 (73.7 ± 24.7 versus 16.6 ± 2.4 pg/dL; P = 0.04) and CRP (82.0 ± 35.6 versus 48.3 ± 14.5 mg/L; P = 0.02) levels. Albumin levels dropped from the first to the fifth feeding day only in the casein group (P < 0.01). Serum IL-6 decreased (62.7 ± 47.2 to 20.6 ± 10.3 pg/dL; P = 0.02) and glutathione increased (32.2 ± 2.1 to 39.9 ± 6.8 U/G Hb; P = 0.03) only in the WP group. Serum IL-6 was lower (P = 0.03) and glutathione was higher (P = 0.03) in whey protein-fed patients than in the casein group.
Enteral formula containing whey protein may decrease inflammation and increase antioxidant defenses in elderly patients with ischemic stroke, compared to casein-containing formula.
Seven elderly men, ages 68 to 74 years, and seven elderly women, ages 70 to 84 years, participated in short-term studies to determine nitrogen balance response to graded intakes of whole egg protein within the sub-maintenance to near-maintenance range of nitrogen intake. After 1 week of consuming an adequate, free-choice diet, the subjects received a "protein-free" diet for 1 day to facilitate adaptation to a decreased level of dietary protein and three randomly assigned levels of egg protein for 10 days. A 4-day break with a normal diet followed each 10-day diet period. The levels of egg protein intake tested (gram protein (N x 6.25) per kilogram of body weight per day) were: for women, 0.52, 0.65, and 0.80 g and, for men, 0.57, 0.70, and 0.85 g. All the women were in negative nitrogen balance at the 0.52 g level of protein intake, and only two subjects achieved positive nitrogen balance at the higher intakes. Of the elderly men, four subjects were in positive balance at the 0.57 and 0.70 g levels, and fivewere in positive balance at the 0.85 g level. The calculated mean protein requirement for elderly women was 0.83 g of protein per kilogram per day, or twice the level arrived at by the factorial method (Scrimshaw, N.S., W.D.A. Perera and V.R. Young. J. Nutr. 106: 665, 1976). The factorial method thus fails to predict a suitable protein allowance for the elderly. It is concluded that a typical U. S. diet providing about 12 to 14% protein calories should be adequate for the elderly. Am. I. Clin. Nutr. 31: 779-785, 1978.
The effects of regular submaximal exercise on dietary protein requirements, whole body protein turnover, and urinary 3-methylhistidine were determined in six young (26.8 +/- 1.2 yr) and six middle-aged (52.0 +/- 1.9 yr) endurance-trained men. They consumed 0.6, 0.9, or 1.2 g.kg-1.day-1 of high-quality protein over three separate 10-day periods, while maintaining training and constant body weight. Nitrogen measurements in diet, urine, and stool and estimated sweat and miscellaneous nitrogen losses showed that they were all in negative nitrogen balance at a protein intake of 0.6 g.kg-1.day-1. The estimated protein requirement was 0.94 +/- 0.05 g.kg-1.day-1 for the 12 men, with no effect of age. Whole body protein turnover, using [15N]glycine as a tracer, and 3-methylhistidine excretion were not different in the two groups, despite lower physical activity of the middle-aged men. Protein intake affected whole body protein flux and synthesis but not 3-methylhistidine excretion. These data show that habitual endurance exercise was associated with dietary protein needs greater than the current Recommended Dietary Allowance of 0.8 g.kg-1.day-1. However, whole body protein turnover and 3-methylhistidine excretion were not different from values reported for sedentary men.
A 9-wk study of adaptation to marginal protein intakes was conducted in 12 elderly women. Subjects were randomly assigned to two groups fed a weight-maintenance diet containing either 1.47 (low) or 2.94 (adequate) g protein.kg body cell mass-1.d-1 (0.45 and 0.92 g.kg body wt-1.d-1, respectively). Mean nitrogen balance in the low-protein group remained negative throughout the study. These subjects experienced significant losses in lean tissue, immune response, and muscle function. The adequate-protein group was in nitrogen balance throughout the study, without changes in lean tissue, and with improvements in immune response, serum immunoglobulins, albumin, total protein values, and muscle function. Thus, elderly women fed the low-protein diet accommodated to the diet by compromising functional capacity, whereas those fed the adequate diet maintained functional capacity.
Nitrogen (N) balance, fed-state leucine kinetics, and urinary 3-methylhistidine (3-MeH) excretion were examined in 12 men and women, aged 56-80 yr, before and during 12 wk of resistance training (RT). Subjects were randomized to groups that consumed diets providing either 0.80 +/- 0.02 g protein.kg-1.day-1 (lower protein, LP) or 1.62 +/- 0.02 g protein.kg-1.day-1 (higher protein, HP). At baseline, mean N balance was negative for LP (-4.6 +/- 3.4 mg N.kg-1.day-1) and positive for HP (13.6 +/- 1.0 mg N.kg-1.day-1). N retention increased similarly in LP and HP at the 11th wk of RT by 12.8 and 12.7 mg N.kg-1.day-1, respectively. Thus LP had an increased efficiency of N retention. LP had decreased leucine flux (P < 0.001), oxidation (P < 0.001), and uptake for protein synthesis (P < 0.02), relative to HP, both at baseline and after RT. Leucine flux increased with RT in both diet groups (P < 0.05) and was associated mainly with an increase in protein synthesis in LP (91% of change in flux) and an increase in oxidation in HP (72% of change in flux; RT-diet interaction, P < 0.05). RT increased actomyosin protein breakdown (increased 3-MeH-to-creatinine ratio, P < 0.01). Diet-related differences in protein metabolism did not influence body composition changes with RT. These data show that the efficiency of N retention and protein utilization during RT is higher in older subjects who consume 0.8 vs. 1.6 g protein.kg-1.day-1 dietary protein.
Body composition and the components of energy metabolism were examined in 12 men and women, aged 56-80 y, before and after 12 wk of resistance training. Subjects were randomly assigned to groups that consumed diets that providing either 0.8 or 1.6 g protein.kg-1.d-1 and adequate total energy to maintain baseline body weight. Fat mass decreased 1.8 +/- 0.4 kg (P < 0.001) and fat-free mass (FFM) increased 1.4 +/- 0.4 kg (P < 0.01) in these weight-stable subjects. The increase in FFM was associated with a 1.6 +/- 0.4 kg increase in total body water (P < 0.01) but no significant change in either protein plus mineral mass or body cell mass. With resistance training, the mean energy intake required for body weight maintenance increased by approximately 15%. Increased energy expenditure included increased resting metabolic rate (P < 0.02) and the energy cost of resistance exercise. Dietary protein intake did not influence these results. Resistance training is an effective way to increase energy requirements, decrease body-fat mass, and maintain metabolically active tissue mass in healthy older people and may be useful as an adjunct to weight-control programs for older adults.
Dietary protein requirements of elderly people were determined by short-term nitrogen-balance techniques and using calculations recommended by the 1985 Joint FAO/WHO/UNU Expert Consultation. Twelve men and women aged 56-80 y were randomly assigned to groups that consumed either 0.80 +/- 0.01 or 1.62 +/- 0.02 g protein.kg-1.d-1 (mean +/- SEM). Net nitrogen balance was negative for the lower-protein group (-4.6 +/- 3.4 mg N.kg-1.d-1) and positive for the higher-protein group (13.6 +/- 1.0 mg N.kg-1.d-1); the intake required for nitrogen equilibrium was estimated to be 1.00 g.kg-1.d-1. Nitrogen-balance data from three previous protein requirement studies in elderly people were recalculated by using the same balance formula and combined with the current study data to provide an overall weighted mean protein requirement estimate of 0.91 +/- 0.043 g.kg-1.d-1. Together, the current and retrospective nitrogen-balance data suggest that the mean protein requirement in elderly adults is considerably greater than the 0.60 g.kg-1.d-1 established by the 1985 Joint FAO/WHO/UNU Expert Consultation. A safe protein intake for elderly adults would be 1.0-1.25 g.kg-1.d-1 of high-quality protein.
Inadequate dietary protein intake results in loss of skeletal muscle mass. Some shorter-term nitrogen balance studies suggest that the Recommended Dietary Allowance (RDA) of protein may not be adequate for older people. The aim of this study was to assess the adequacy of the RDA of protein for older people by examining longer-term responses in urinary nitrogen excretion, whole-body protein metabolism, whole-body composition, and mid-thigh muscle area.
This was a 14-week precisely controlled diet study. Ten healthy, ambulatory men and women, aged 55 to 77 years, were provided eucaloric diets that contained 0.8 g protein.kg(-1).day(-1). The study was conducted at a General Clinical Research Center using an outpatient setting for 11 weeks and an inpatient setting for 3 weeks. The main outcome measures included urinary nitrogen excretion, postabsorptive and postprandial whole-body leucine kinetics via infusion of L-[1-(13)C]-leucine, whole-body density via hydrostatic weighing, total body water via deuterium oxide dilution, and mid-thigh muscle area via computed tomography scans.
Mean urinary nitrogen excretion decreased over time from Weeks 2 to 8 to 14 (p =.025). At Week 14, compared with Week 2, there were no changes in postabsorptive or postprandial leucine kinetics (turnover, oxidation, incorporation into protein via synthesis, release via breakdown, or balance). Whole-body composition (% body fat, fat-free mass, and protein + mineral mass) did not change over time in these weight-stable subjects. Mid-thigh muscle area was decreased by -1.7 +/- 0.6 cm(2) (p =.019) at Week 14 compared with Week 2. The loss of mid-thigh muscle area was associated with the decrease in urinary nitrogen excretion (Spearman r =.83, p =.010).
The maintenance of whole-body leucine metabolism and whole-body composition is generally consistent with a successful adaptation to the RDA for protein. However, the decrease in mid-thigh muscle area and the association with decreased urinary nitrogen excretion are consistent with a metabolic accommodation. These results suggest that the RDA for protein may not be adequate to completely meet the metabolic and physiological needs of virtually all older people.
For elderly women, insufficient data exist to assess the accuracy of the assumed mean protein requirement of 0.6 g of protein x kg(-1) x day(-1), and the adequacy of the current Recommended Dietary Allowance (RDA) of 0.8 g of protein x kg(-1) x day(-1). The aims of this study were to assess the mean protein requirement and suggested safe and adequate protein intake (protein allowance) of elderly women using a shorter-term nitrogen balance protocol.
During three separate 18-day trials, 11 elderly women (age range, 70-81 years) were randomly fed eucaloric diets designed to provide either 0.50, 0.75, or 1.00 g of protein x kg(-1) x day(-1). Nitrogen balance was determined at Weeks 2 and 3 (Days 7-10 and 14-17, respectively) of each trial using data from total nitrogen analyses of duplicate food composites, 24-hour urine collections, and stool collections. The mean protein requirement was calculated using linear regression of individual women's data from all three trials and inverse prediction.
At protein intakes of 0.53 +/- 0.02, 0.76 +/- 0.02, or 1.06 +/- 0.05 g of protein x kg(-1) x day(-1), net nitrogen balances during Week 2 were -14.5 +/- 3.1, 3.8 +/- 2.5 and 23.4 +/- 3.3 mg of nitrogen x kg(-1) x day(-1), respectively, for these body weight- and body composition-stable women. At Week 3, the net nitrogen balances were -0.1 +/- 2.7, 8.5 +/- 3.6 and 42.0 +/- 3.0 mg of nitrogen x kg(-1) x day(-1). From Week 2 to Week 3, shifts to more positive nitrogen balances occurred due to decreases in urinary nitrogen excretion. The mean protein requirement at Week 2 was calculated to be 0.70 +/- 0.09 g of protein. kg(-1) x day(-1) (coefficient of variation [CV] = 13%) and at Week 3 was calculated to be 0.56 +/- 0.09 g of protein x kg(-1) x day(-1) (CV = 17%). From these data, an adequate protein allowance was estimated to be greater than the RDA at Week 2 (0.90 g of protein x kg(-1) x day [d](-1)), and not different than the RDA at Week 3 (0.76 g of protein x kg(-1) x d(-1)).
The decrease over time in urinary nitrogen excretion from Week 2 to Week 3 suggests that these elderly women did not achieve a metabolic steady state during this shorter-term nitrogen balance study. Collectively, these data suggest that the total protein needs of elderly women are at or above the current RDA for protein. However, the results of this study indicate that shorter-term nitrogen balance protocols are insufficient to firmly establish the RDA for protein of elderly women, and further research is required using alternative criteria measures.
Laboratory-based body-composition techniques include hydrostatic weighing (HW), dual-energy X-ray absorptiometry (DXA), measurement of total body water (TBW) by isotope dilution, measurement of total body potassium, and multicompartment models. Although these reference methods are used routinely, each has inherent practical limitations. Whole-body air-displacement plethysmography is a new practical alternative to these more traditional body-composition methods. We reviewed the principal findings from studies published between December 1995 and August 2001 that compared the BOD POD method (Life Measurement, Inc, Concord, CA) with reference methods and summarized factors contributing to the different study findings. The average of the study means indicates that the BOD POD and HW agree within 1% body fat (BF) for adults and children, whereas the BOD POD and DXA agree within 1% BF for adults and 2% BF for children. Few studies have compared the BOD POD with multicompartment models; those that have suggest a similar average underestimation of approximate 2-3% BF by both the BOD POD and HW. Individual variations between 2-compartment models compared with DXA and 4 -compartment models are partly attributable to deviations from the assumed chemical composition of the body. Wide variations among study means, -4.0% to 1.9% BF for BOD POD - HW and -3.0% to 1.7% BF for BOD POD - DXA, are likely due in part to differences in laboratory equipment, study design, and subject characteristics and in some cases to failure to follow the manufacturer's recommended protocol. Wide intersubject variations between methods are partly attributed to technical precision and biological error but to a large extent remain unexplained. On the basis of this review, future research goals are suggested.
Previous evidence suggests that aging in healthy persons does not result in decreased incorporation of muscle proteins after a bolus ingestion of 15 g essential amino acids (EAAs).
We sought to examine whether ingestion of a smaller bolus of EAAs is associated with diminished accretion of muscle proteins in the elderly when compared with the young.
Eleven elderly subjects (mean +/- SEM: 68 +/- 2 y) and 8 young control subjects (mean +/- SEM: 31 +/- 2 y) were studied in the postabsorptive state and for 3.5 h after a bolus ingestion of approximately 7 g EAAs. Muscle protein accretion and synthesis were measured with the femoral arteriovenous phenylalanine net balance technique during a constant infusion of L-[ring-(2)H5]phenylalanine.
Similar to previous observations, no significant differences in the postabsorptive phenylalanine net balance were observed between the groups. However, the mean (+/-SEM) net phenylalanine uptake after EAA ingestion was significantly less in the elderly (9.9 +/- 3.7 mg/leg) than in the young (25.1 +/- 3.7 mg/leg; P < 0.05). The mean (+/-SEM) rate of disappearance of phenylalanine during the same period significantly increased above basal rates in the young (36 +/- 3 compared with 30 +/- 3 nmol x min(-1) x 100 mL leg volume(-1); P < 0.05) but not in the elderly (30 +/- 3 compared with 28 +/- 5 nmol x min(-1) x 100 mL leg volume(-1); P > 0.05).
These data indicate that aging results in a diminished accretion of muscle proteins after ingestion of a small dose of EAAs. These findings may have practical implications with respect to the amount of protein contained in supplements given to the elderly for enhancing the stimulation of muscle protein synthesis.
Protein and energy undernutrition is common in older people, and further deterioration may occur during illness.
To assess whether oral protein and energy supplementation improves clinical and nutritional outcomes for older people in the hospital, in an institution, or in the community.
Cochrane Central Register of Controlled Trials (CENTRAL), MEDLINE, EMBASE, HealthStar, CINAHL, BIOSIS, and CAB abstracts. The authors included English- and non-English-language studies and hand-searched journals, contacted manufacturers, and sought information from trialists. The date of the most recent search of CENTRAL and MEDLINE is June 2005.
Randomized and quasi-randomized controlled trials of oral protein and energy supplementation compared with placebo or control treatment in older people.
Two reviewers independently assessed trials for inclusion, extracted data, and assessed trial quality. Differences were resolved by consensus.
Fifty-five trials were included (n = 9187 randomly assigned participants). For patients in short-term care hospitals who were given oral supplements, evidence suggested fewer complications (Peto odds ratio, 0.72 [95% CI, 0.53 to 0.97]) and reduced mortality (Peto odds ratio, 0.66 [CI, 0.49 to 0.90]) for those undernourished at baseline. Few studies reported evidence that suggested any change in mortality, morbidity, or function for those given supplements at home. Ten trials reported gastrointestinal disturbances, such as nausea, vomiting, and diarrhea, with oral supplements.
The quality of most studies, as reported, was poor, particularly for concealment of allocation and blinding of outcome assessors. Many studies were too small or the follow-up time was too short to detect a statistically significant change in clinical outcome. The clinical results are dominated by 1 very large recent trial in patients with stroke. Although this was a high-quality trial, few participants were undernourished at baseline.
Oral nutritional supplements can improve nutritional status and seem to reduce mortality and complications for undernourished elderly patients in the hospital. Current evidence does not support routine supplementation for older people at home or for well-nourished older patients in any setting.
Modular protein supplements are added to either the diet or enteral formula to increase the protein or amino acid intakes of people who are nutritionally compromised. Protein supplements are aggressively marketed to long-term care clinicians because protein energy malnutrition and wounds are a common problem in this care setting. It can be challenging for clinicians to distinguish one product from another and to determine the best product for a specific application or nutrition care goal. Modular protein products can be sorted into 4 categories: (1) protein concentrates derived from a complete protein such as milk, soy, or eggs; (2) protein concentrates derived from collagen, either alone or in combination with a complete protein; (3) doses of 1 or more dispensable (nonessential) amino acids; and (4) hybrids of the complete or collagen-based proteins and amino acid dose. Modular protein supplements are generally provided either as a substrate for protein synthesis or as a source of 1 or more amino acids that may be conditionally indispensable (conditionally essential) under certain disease conditions. This review provides guidelines for the use of modular protein supplements according to their intended physiologic function and the assessment and nutrition care goals of the long-term care resident.
OBJECTIVE: To compare Pressure Ulcer Scale for Healing (PUSH) scores at 8 weeks in long-term-care residents with pressure ulcers who were given standard care plus a concentrated, fortified, collagen protein hydrolysate supplement vs. residents who were given standard care plus placebo. DESIGN: Randomized, prospective, controlled, multicenter trial at 23 long-term-care facilities in 4 states. SUBJECTS: A total of 89 residents with Stage II, III, or IV pressure ulcers were entered into the trial; 71 residents completed the study. INTERVENTION: Residents were randomized to receive standard care plus a concentrated, fortified, collagen protein hydrolysate supplement (n = 56) or standard care plus placebo (n = 33) 3 times daily for 8 weeks. Wound healing was assessed biweekly using the PUSH tool, version 3.0. This tool categorizes pressure ulcers by surface area, exudate, and type of wound tissue. PRIMARY OUTCOME MEASURE: Change in PUSH tool scores in each group at 8 weeks. RESULTS: After 8 weeks of treatment, residents who received standard care plus the concentrated, fortified, collagen protein hydrolysate supplement had significantly better PUSH tool scores compared with those who received standard care plus placebo (3.55 +/- 4.66 vs 3.22 +/- 4.11, respectively; P < .05). CONCLUSION: By week 8, PUSH tool scores-a measurement of pressure ulcer healing-showed approximately twice the rate of pressure ulcer healing in the treatment group compared with the control group. A concentrated, fortified, collagen protein hydrolysate supplement may be of benefit to residents of long-term-care facilities who have pressure ulcers.
The capacity of older men and women to adapt to regularly performed exercise has been demonstrated by many laboratories. Aerobic exercise results in improvements in functional capacity and reduced risk of developing type II diabetes in the elderly. High intensity resistance training (above 60% of the 1 repetition maximum) causes large increases in strength in the elderly, and resistance training significant increases muscle size. Resistance training also significantly increases energy requirements and insulin action of the elderly. We recently demonstrated that resistance training has a positive effect on multiple risk factors for osteoporotic fractures in previously sedentary post-menopausal women. Because the sedentary lifestyle of individuals in a long-term care facility may exacerbate losses of muscle function, we applied this same training program to frail, institutionalized elderly men and women. In a population of 100 nursing home residents, a randomly assigned high intensity strength training program resulted in significant gains in strength and functional status. In addition, spontaneous activity, measured by activity monitors, increased significantly in those participating in the exercise program; there was no change in the sedentary control group. Before the strength training intervention, the relationship of whole-body potassium and leg strength was relatively weak (r2 = 0.29, P < 0.001), indicating that in very old persons muscle mass is an important but not the only determiner of functional status. Thus exercise may minimize or reverse the syndrome of physical frailty prevalent among very old individuals. Because of their low functional status and high incidence of chronic disease, there is no segment of the population that can benefit more from exercise training than the elderly.
Background: Protein and energy undernutrition is common in older people, and further deterioration may occur during illness. Purpose: To assess whether oral protein and energy supplementation improves clinical and nutritional outcomes for older people in the hospital, in an institution, or in the community. Data Sources: Cochrane Central Register of Controlled Trials (CENTRAL), MEDLINE, EMBASE, HealthStar, CINAHL, BIOSIS, and CAB s. The authors included English- and non-English-language studies and hand-searched journals, contacted manufacturers, and sought information from trialists. The date of the most recent search of CENTRAL and MEDLINE is June 2005. Study Selection: Randomized and quasi-randomized controlled trials of oral protein and energy supplementation compared with placebo or control treatment in older people. Data Extraction: Two reviewers independently assessed trials for inclusion, extracted data, and assessed trial quality. Differences were resolved by consensus. Data Synthesis: Fifty-five trials were included (n = 9187 randomly assigned participants). For patients in short-term care hospitals who were given oral supplements, evidence suggested fewer complications (Peto odds ratio, 0.72 [95% Cl, 0.53 to 0.97]) and reduced mortality (Peto odds ratio, 0.66 [Cl, 0.49 to 0.90]) for those undernourished at baseline. Few studies reported evidence that suggested any change in mortality, morbidity, or function for those given supplements at home. Ten trials reported gastrointestinal disturbances, such as nausea, vomiting, and diarrhea, with oral supplements. Limitations: The quality of most studies, as reported, was poor, particularly for concealment of allocation and blinding of outcome assessors. Many studies were too small or the follow-up time was too short to detect a statistically significant change in clinical outcome. The clinical results are dominated by 1 very large recent trial in patients with stroke. Although this was a high-quality trial, few participants were undernourished at baseline. Conclusions: Oral nutritional supplements can improve nutritional status and seem to reduce mortality and complications for undernourished elderly patients in the hospital. Current evidence does not support routine supplementation for older people at home or for well-nourished older patients in any setting.
Sodalite membrane has been successfully fabricated on tubular porous a-Al 2 O 3 supports by secondary growth method with vacuum seeding. In the seeding process, the colloidal seeding particles were agglutinated not only onto the surface of alumina support but also within the pores by vacuum sucking method. To obtain defect-free sodalite membrane, the sodalite crystals were grown directly on the alumina support in a mixture solution containing alumina and silica species under the hydrothermal reaction condition. The as-synthesized sodalite membranes were characterized by X-ray diffraction (XRD) analysis and scanning electron microscopy (SEM). The thickness and the quality of sodalite membrane could be controlled by the hydrothermal reaction time (12¨24 h) and temperature (100¨150 -C) under the mother solution of 5Na 2 O : 2SiO 2 : Al 2 O 3 : 1000H 2 O. D 2005 Elsevier B.V. All rights reserved.
The BOD POD, a new air-displacement plethysmograph for measuring human body composition, utilizes the inverse relationship between pressure and volume (Boyle's law) to measure body volume directly. The quantity of air in the lungs during tidal breathing, the average thoracic gas volume (Vtg), is also measured by the BOD POD by using a standard plethysmographic technique. Alternatively, the BOD POD provides the use of a predicted Vtg (Vtgpred). The validity of using Vtgpred in place of measured Vtg (Vtgmeas) to determine the percentage of body fat (%BF) was evaluated in 50 subjects (36 women, 14 men; ages 18-56 yr). There was no significant difference between Vtgmeas and Vtgpred (mean difference +/- SE, 53.5 +/- 63.3 ml) nor in %BF by using Vtgmeas vs. Vtgpred (0.2 +/- 0.2 %BF). On an individual basis, %BF measured by using Vtgmeas vs. Vtgpred differed within +/-2.0% BF for 82% of the subjects; maximum differences were -2.9 to +3.0% BF. For comparison, data from 24 subjects who had undergone hydrostatic weighing were evaluated for the validity of using predicted vs. measured residual lung volume (VRpred vs. VRmeas, respectively). Differences between VRmeas and VRpred and in %BF calculated by using VRmeas vs. VRpred were significant (187 +/- 46 ml and 1.4 +/- 0.3% BF, respectively; P < 0.001). On an individual basis, %BF determined by using VRmeas vs. VRpred differed within +/-2.0% BF for 46% of the subjects; maximum differences were -2.9 to +3.8% BF. With respect to %BF measured by air displacement, our findings support the use of Vtgpred for group mean comparisons and for purposes such as screening in young to middle-aged individuals. This contrasts with the use of VRpred in hydrostatic weighing, which leads to significant errors in the estimation of %BF. Furthermore, although the use of Vtgpred has some application, determining Vtgmeas is relatively simple in most cases. Therefore, we recommend that the use of Vtgmeas remain as standard experimental and clinical practice.
The egg protein requirements of men over age 60 were determined by the same techniques previously used to establish requirements of younger men, in the same laboratory. The six subjects were healthy but somewhat obese; their basal metabolic rates, lean body mass, and urinary creatinine excretion were 12 to 15% less than values for young men of about the same height. They were given a protein-free diet for 17 days to determine endogenous nitrogen (N) losses, with energy sufficient to maintain body weight (BW) nearly constant. Endogenous fecal and urinary N losses were 0.79 ± 0.18 and 2.27 ± 0.22 g/day, respectively. Endogenous urinary N was equivalent to 27 ± 2 mg/kg BW, 1.45 ± 0.20 mg/basal kcal, 1.64 ± 0.15 g/g creatinine, and 43 ± 1 mg/kg lean body mass (LBM). The value for elderly men was less than that for young men per day and per kg BW, but the same when expressed in relation to creatinine excretion, LBM, and basal energy. In two sequential periods, eggwhite protein was given in amounts equal to 1.34 to 1.88 times the measured endogenous nitrogen output. Urinary, fecal, integumental, and miscellaneous N losses were measured to determine true balance. The minimum dietary requirement to maintain N equilibrium was computed from regression analysis of balances at the three levels of intake. Average N requirement was predicted to be 6.16 ± 0.24 g/day; this is equal to 74 mg/kg actual BW or 88 mg/kg 'ideal' BW (standard for height at age 25). Minimum requirement was not correlated with BW, creatinine, basal metabolic rate, or height, but was associated with the magnitude of the endogenous loss and the efficiency of protein utilization. The 'safe level' of egg protein for healthy older men, as defined by the FAO/WHO, i.e., the average N requirement for balance plus 2 standard deviations, was calculated to be 95 mg N or 0.59 g protein/kg ideal BW, under the conditions of this study. This figure is negligibly higher than the present FAO/WHO 'safe level' of 0.57 g egg protein/kg reference weight.
The protein requirement and the efficiency of protein used were studied in young and old adult human subjects. Protein intake levels (N X 6.25) of 0.4, 0.8, and 1.6 g/kg body weight per day from a combination wheat-soy-milk mixture were fed. Caloric intake was held constant at 40 kcal/kg body weight per day throughout the 11-day study of each dietary period. No significant differences were observed in their protein requirement, efficiency of protein use or the ability to adapt to changes of protein intake levels. Protein digestibility was not impaired in the aged. It is concluded that the protein requirement and the efficiency of protein use are not affected by the aging process.
The daily flux of amino acids in the body is extensive. Protein synthesis is estimated to be 300 g daily in an adult man. This requires uptake and release of 150 g essential amino acids, yet the dietary requirement for essential amino acids in only 6 g. This indicates extensive and efficient recycling of essential amino acids released by protein breakdown. The catabolism of essential amino acids by the liver is sensitively regulated in relation to requirements. A study of availability of tryptophan to rats receiving various levels of tryptophan in the diet shows that plasma tryptophan increases only when intake exceeds requirements and at these higher levels of intake tryptophan oxygenase activity in the liver becomes increased shortly after meals. In addition, the carbohydrate content of the diet causes tryptophan to become deposited in the free amino acid pool of muscle through an insulin-dependent mechanism. Dietary carbohydrate also effects plasma tryptophan due to a fall in the plasma level of non-esterified fatty acids which compete with tryptophan for binding sites on serum albumin. Consequently, after carbohydrate the proportion of plasma tryptophan bound to serum albumin increases, so that there is less nonbound tryptophan in the plasma. The metabolic significance of this has yet to be demonstrated. Finally, protein metabolism in skeletal muscle exhibits considerable efficiency of reutilization of essential amino acids, since the main products passing into the blood are alanine and glutamine. It has been shown that 3-methylhistidine present in muscle protein in not reutilized for synthesis of protein and that its excretion in the urine can provide a useful index of muscle catabolism. In prolonged starvation of adults or protein deficiency in children, output of 3-methylhistidine is much reduced, suggesting an adaptive reduction in muscle protein catabolism. It is emphasized that, because of its function in monitoring dietary amino acid intake, liver protein metabolism responds rapidly to changes in protein intake and in consequence protein deficiency causes early depletion, whereas muscle protein undergoes depletion later and is subject to adaptive processes that restrict the loss.
Nitrogen (N) sparing and even equilibrium have been achieved in obese subjects with all-protein weight-reducing very low energy diets (VLED) apparently independently of the content of essential amino acids. This study assessed whether the metabolic response observed at week 3 of an all-protein VLED with 46% of amino acids (aa) as essential was modified during week 4, when consuming a protein source that provided 16% of amino acids as essential. Six healthy obese subjects (BMI: 35.3 +/- 1.3 kg/m2, weight 90 +/- 9 kg) were given a 1.72 MJ (400 kcal) all protein (93 g) VLED and a multi-vitamin-mineral supplement daily for four weeks. During weeks 1 to 3, the protein was casein-soy (46% essential aa) and during week 4, tryptophan- and methionine-supplemented collagen hydrolysate (16% essential aa). At week 3, decreases in plasma glucose, insulin, cholesterol, blood pH and bicarbonate, and increases in plasma free fatty acids, serum urea, uric acid and blood and urine ketones occurred compared to baseline. These adaptations were unchanged at week 4. N balance returned toward equilibrium by day 23 remaining at values close to 0 despite the change in diet composition. Mean negative N balance did not differ between weeks 3 and 4 (-1.1 +/- 0.5 g vs. -0.6 +/- 0.5 g/day) and neither did mean urinary ammonium N excretion (0.71 +/- 0.08 vs. 0.73 +/- 0.07 g/day). Urinary urea N excretion tended to increase with the collagen-based diet reflecting the greater proportion of N in this protein source (18 vs. 15%).(ABSTRACT TRUNCATED AT 250 WORDS)
In conventional experiments, nitrogen balance is taken to be the difference between the amount given in the diet and the sum of urinary and fecal nitrogenous wastes. Sustained positive balance is ascribed either to expansion of the body nitrogen pool or to loss from the body surface as sweat, desquamated cells, hair and nails. To refine these estimates, we accumulated information on the 3- or 6-day dermal nitrogen loss recovered in bath water and washings of underwear and socks of sedentary men fed diets containing 0.5 to 96 g nitrogen per day. Dermal nitrogen output varied systematically with nitrogen intake, be ing 112 ± 42 mg with protein-free diet, 149 ± 51 mg with normal (75 g protein) intake, and 514 ± 161 mg with 600 g protein in the daily diet. This relationship appears to be due to differences in blood urea nitrogen associated with protein intake. All material lost from the body surface was collected in double layers of special clothing over a 9-day period from another three men, two of whom were confined to bed. Data from this more complete collection suggest that the usual values are about 45% lower than the true total when all surfaces are covered. Sweat was collected from men working at rates of 2 to 15 kcal per minute for short periods in the laboratory and while playing soccer in the field. Dermal nitrogen loss increased with increasing work rate and was about 0.3 mg per m2 body surface area per kilocalorie per minute in laboratory studies and 0.36 mg in the athletes. Other unavoidable but usually ignored nitrogen losses were found to amount to about 115 mg per day (toothbrushing, toilet tissues, plate wastes, exhaled ammonia). Additional potential routes of loss are blood (32 mg N/100 ml), saliva (0.9 mg per gram) and semen (37 mg per ejaculate). The total error in balances if the dermal and miscellaneous losses are disregarded is about 0.5 g nitrogen per day for sedentary men in a comfortable envirenment. J. Nutr. 101: 775-786, 1971.
A continuous 30-day metabolic N balance study was conducted in seven elderly men (75 +/- 4 yr) and eight elderly women (78 +/- 9 yr) to evaluate the current protein Recommended Dietary Allowance for older men and women. The subjects received a diet providing 0.8 g egg protein (N x 6.25) kg-1 day-1. Energy intake computed to meet needs averaged 32 and 29 kcal kg-1 day-1 for males and females, respectively. N balances, including an estimate for integumental and other miscellaneous losses, were determined for the last 5 days of three consecutive 10-day diet periods and blood biochemical measurements were made at the end of each diet period. Three of seven males and four of eight females were not in body N balance during the final 5 days of the 30-day period. These N balance data indicate that 0.8 g egg protein kg-1 day-1 is not sufficient to achieve N equilibrium in a majority of subjects older than 70 yr and confirm the results and conclusions of a previous, short-term N balance study (Uauy et al., Am J Clin Nutr 1978;31:779-85). Hence, where energy intake approximates requirement, the current Recommended Dietary Allowance is not adequate for a majority of male and female subjects age 70 yr and above.
Advancing adult age is associated with profound changes in body composition, the principal component of which is a decrease in skeletal muscle mass. This age-related loss in skeletal muscle has been referred to as sarcopenia. Age-related reduction in muscle is a direct cause of the age-related decrease in muscle strength. Muscle mass (not function) appears to be the major determinant of the age- and sex-related differences in strength. This relationship is independent of muscle location (upper vs lower extremities) and function (extension vs flexion). Reduced muscle strength in the elderly is a major cause for their increased prevalence of disability. With advancing age and extremely low activity levels seen in the very old, muscle strength is a critical component of walking ability. The high prevalence of falls among the institutionalized elderly may be a consequence of their lower muscle strength. Daily energy expenditure declines progressively throughout adult life. In sedentary individuals, the main determinant of energy expenditure is fat-free mass, which declines by about 15% between the third and eighth decade of life, contributing to a lower basal metabolic rate in the elderly. Data indicate that preservation of muscle mass and prevention of sarcopenia can help prevent the decrease in metabolic rate. In addition to its role in energy metabolism, skeletal muscle and its age-related decline may contribute to such age-associated changes as reduction in bone density, insulin sensitivity, and aerobic capacity.(ABSTRACT TRUNCATED AT 250 WORDS)
The metabolic mechanisms of accommodation to a low-protein diet in elderly women were studied. Diets containing 1.47 (low) or 2.94 (adequate) g protein.kg body cell mass-1.d-1 (0.45 or 0.92 g.kg body weight-1.d-1, respectively) were fed for 10 wk. Fed state leucine kinetics, fasted and fed metabolic rate, and acute-phase responses to a bout of exercise were measured. Leucine uptake into protein, breakdown, and acute-phase responses were not significantly different within or between diet groups. In the low-protein group, leucine flux and oxidation were lower after 3 wk and oxidation continued to decrease throughout the 10-wk study. When expressed per body cell mass, metabolic rate increased over time in the low-protein group only. Leucine oxidation was a more sensitive index of the adequacy of protein intake than synthesis, flux, metabolic rate, or acute-phase response.
Based on N balance calculated in accord with the recommendations of the 1985 Joint FAO/WHO/UNU Expert Consultation, a summary of conclusions from the six N balance studies in elderly people is presented in Table 3. The data, with one flawed exception, indicate that the safe level of protein intake for older adults may be higher than currently recommended. In the only study directly comparing elderly and young subjects (Cheng et al, 1978), no differences in protein requirement were found. However, the data suggest that the 0.8 g protein/kg/d would be inadequate for both groups. Additional direct comparisons between younger and older adults are desirable as a basis for any revised recommendations. In the only study directly comparing the protein requirements of both elderly men and women (Uauy et al, 1978), the variability was too great to allow adequate assessment of possible gender differences. More research is needed to determine whether gender-related differences occur.
Estimates of protein and amino acid requirements in this paper are proposed for healthy elderly people. The estimate of protein requirement was based on nitrogen (N) balance, as well as functional indicators such as immune function or muscle strength. Data suggest that the protein requirement for nitrogen equilibrium in the elderly, is greater than 0.8 gm/kg body weight/day. There do not appear to be any adverse consequences with protein intakes that are about 1 gm/kg body weight/day. The tentative recommendation in this paper is higher than the current mean recommended intake of protein (FAO/WHO/UNU, 1985). However, because of methodological difficulties, the data does not allow for a confident prediction of what the exact level of protein intake should be. Further studies are needed to come to a firm conclusion on the exact protein requirement. Indispensable amino acid requirements based on nitrogen balance data, in the elderly, are fragmentary and conflicting. These requirements can alternatively be based on obligatory nitrogen loss, for which data is available in the elderly. The overlap of the obligatory nitrogen loss between the young and the elderly, suggest that the amino acid requirement based on this technique is similar in young and elderly individuals. Tracer based techniques measuring amino acid balance at different amino acid intakes, also support the view that there are no differences in the amino acid requirements between young and elderly people. In general, these amino acid requirement studies have been performed in healthy USA subjects, and data is needed to know if these estimates can be extended to populations from other, less-developed countries.
This study assessed the effects of long-term consumption of the United States Recommended Dietary Allowance (RDA) for protein by older people who were sedentary or performed resistive training (RT) on body composition, skeletal muscle size and protein metabolism, and if the number of muscle groups trained influenced the muscle hypertrophy response to RT. Twelve men and 17 women (age range 54-78 years) completed this 14 week controlled diet and exercise study. Throughout the study, each subject completely consumed daily euenergetic menus that provided the RDA of 0.8 g protein kg(-1) day(-1). From study weeks 3-14 (weeks RT1-RT12), 10 subjects (four men, six women) performed whole body RT (WBRT), nine subjects (four men, five women) performed lower body RT (LBRT) and 10 subjects (four men, six women) remained sedentary (SED). Both the LBRT and WBRT groups performed knee extension and flexion exercises, and the WBRT group also performed chest press and arm pull exercises (three sets per exercise at 80 % of one repetition maximum, 3 days per week for 12 weeks). From week 2 (baseline) to week RT12, muscle strength increased in muscle groups trained in the LBRT and WBRT groups, and was not changed in the SED group. From baseline to week RT12, whole body muscle mass and protein-mineral mass were not changed, fat-free mass (P = 0.004) and total body water (P = 0.013) were decreased, and percentage body fat was increased (P = 0.011) in these weight-stable older people, independent of group assignment. The RT-induced increases in mid-thigh muscle area (from computed tomography scans) were comparable in the LBRT and WBRT groups (2.13 +/- 1.26 cm(2) and 2.17 +/- 1.24 cm(2), respectively), and were different from those in the SED group, which lost muscle area (-1.74 +/- 0.57 cm(2); group-by-time P < 0.05). From baseline to week RT12, 24 h urinary total nitrogen excretion decreased (P < 0.001), nitrogen balance shifted from near equilibrium to positive, whole body leucine oxidation (from the infusion of L-[(13)C]leucine) decreased (P < 0.05) and net (postabsorptive vs. postprandial) leucine balance (P < 0.05) increased from near equilibrium to positive, with no differences in responses over time among the three groups. In conclusion, the number of muscle groups trained did not influence whole body protein metabolism or RT-induced muscle hypertrophy in older people. Most of these data are consistent with a successful adaptation to the RDA for protein. However, research should continue to question whether the decreases in fat-free mass and total body water observed in all subjects, and the decrease in mid-thigh muscle area in the SED group, are physiological accommodations, and whether the RDA for protein might be marginally inadequate for older people to maintain skeletal muscle.
To compare Pressure Ulcer Scale for Healing (PUSH) scores at 8 weeks in long-term-care residents with pressure ulcers who were given standard care plus a concentrated, fortified, collagen protein hydrolysate supplement vs. residents who were given standard care plus placebo.
Randomized, prospective, controlled, multicenter trial at 23 long-term-care facilities in 4 states.
A total of 89 residents with Stage II, III, or IV pressure ulcers were entered into the trial; 71 residents completed the study.
Residents were randomized to receive standard care plus a concentrated, fortified, collagen protein hydrolysate supplement (n = 56) or standard care plus placebo (n = 33) 3 times daily for 8 weeks. Wound healing was assessed biweekly using the PUSH tool, version 3.0. This tool categorizes pressure ulcers by surface area, exudate, and type of wound tissue.
Change in PUSH tool scores in each group at 8 weeks.
After 8 weeks of treatment, residents who received standard care plus the concentrated, fortified, collagen protein hydrolysate supplement had significantly better PUSH tool scores compared with those who received standard care plus placebo (3.55 +/- 4.66 vs 3.22 +/- 4.11, respectively; P < .05).
By week 8, PUSH tool scores-a measurement of pressure ulcer healing-showed approximately twice the rate of pressure ulcer healing in the treatment group compared with the control group. A concentrated, fortified, collagen protein hydrolysate supplement may be of benefit to residents of long-term-care facilities who have pressure ulcers.
To compare the dietary intake of elderly living in 11 long-term care facilities (LTCFs) to the Estimated Average Requirement set as part of the Dietary Reference Intake for older adults.
A cross-sectional assessment of dietary intake using a 3 days food record among 407 elderly with mean age of 85.2 +/- 7.7 years and BMI of 23.8 +/- 5.7 kg/m(2). This population sample was similar to the one living in LTCFs in the province of Ontario.
The daily energy intake was 1513 +/- 363 kcal (6330.4 +/- 1518.8 kJ). Percentage of energy from fat, saturated fat, polyunsaturated fat, protein, and carbohydrate were 30%, 11%, 5.2%, 15%, and 56%, respectively. Although these values were close to the recommendations, 29.5% had protein intake below the recommended 0.8 g/kg; and 38.3% of subjects had cholesterol intake more than the recommended 300 mg/d. More than 50% of the subjects had suboptimal intake of calcium, magnesium, zinc and vitamins E, B(6), and folate. In addition, greater than 15% had suboptimal intakes of other micronutrients such as vitamins A, C, niacin, and copper.
Elderly subjects living in LTCFs in Toronto despite having a normal body mass index (BMI), do not meet the recommended levels of intake for protein and many of the micronutrients. LTCFs staff should monitor dietary intake. Menu modification and micronutrient supplementation may be required in order to meet the daily requirements of these elderly.
Pre-study sample size calculations for clinical trial research protocols are now mandatory. When an investigator is designing a study to compare the outcomes of an intervention, an essential step is the calculation of sample sizes that will allow a reasonable chance (power) of detecting a pre-determined difference (effect size) in the outcome variable, at a given level of statistical significance. Frequently studies will recruit fewer patients than the initial pre-study sample size calculation suggested. Investigators are faced with the fact that their study may be inadequately powered to detect the pre-specified treatment effect and the statistical analysis of the collected outcome data may or may not report a statistically significant result. If the data produces a "non-statistically significant result" then investigators are frequently tempted to ask the question "Given the actual final study size, what is the power of the study, now, to detect a treatment effect or difference?" The aim of this article is to debate whether or not it is desirable to answer this question and to undertake a power calculation, after the data have been collected and analysed.
In recent years there has been considerable interest in the benefits of high-protein diets. This study determined current usual intake of protein in America. Using the most recent data from the National Health and Nutrition Examination Survey, 2003-2004, usual protein intake for Americans aged 2+ years was estimated. Usual protein intake was calculated on a grams per day, grams per kilogram ideal body weight, and a percentage of calories basis. Protein intake averaged 56 +/- 14 g/d in young children, increased to a high of approximately 91 +/- 22 g/d in adults aged 19-30 y, and decreased to approximately 66 +/- 17 g/d in the elderly. The percentage of the male population who consumed less than the estimated average requirement was very low. Our estimates indicated that 7.7% of adolescent females and 7.2-8.6% of older adult women reported consuming protein levels below their estimated average requirement. The median intake of protein on a percentage of calories basis ranged from 13.4% in children aged 4-8 y to 16.0% in men aged 51-70 y. Even the 95th percentile of protein intake did not approach the highest acceptable macronutrient distribution range of 35% for an age/sex group. The highest 95th percentile of protein intake was 20.8% of calories in men aged 51-70 y. Given the demonstrated benefits of higher protein intake on weight management, sarcopenia, and other physiologic functions, efforts should be undertaken to ensure that Americans consume the recommended amount of protein (17-21% of calories as expected from MyPyramid food patterns).
Report of a Joint FAO/WHO/UNU Expert Consultation. Geneva, Switzerland: World Health Organiza-tion
- Energy
Energy and Protein Requirements. Report of a Joint FAO/WHO/UNU Expert Consultation. Geneva, Switzerland: World Health Organiza-tion; 1985. Technical Report Series 724.
Report of a Joint FAO/WHO/UNU Expert Consultation
- Protein Energy
- Requirements
Energy and Protein Requirements. Report of a Joint FAO/WHO/UNU
Expert Consultation. Geneva, Switzerland: World Health Organization; 1985. Technical Report Series 724.
Increased protein requirements in the elderly: New data and retrospective reassessments
- Campbell