No full-text available
To read the full-text of this research,
you can request a copy directly from the authors.
Effect of daily gelatin ingestion on human scalp hair
Abstract
The effect of daily gelatine ingestion on human scalp hair was studied in a normal adult population. The most dramatic effect of supplementing the normal diet with 14 grams of gelatine daily was an increase in hair diameter averaging 9.3% in the first study and 11.3% in the second study. Approximately seventy percent of the subjects in both studies showed increases in hair diameter ranging from 5% to 45%. It is postulated that this increase constitutes an improvement in the mechanical properties of the hair. Further, it was shown that the increase in hair diameter was generally inversely proportional to the initial, predosing value. Within 6 months after cessation of gelatine dosing, hair diameter reversed back its original level. The increase was therefore directly attributable to gelatine ingestion. Yield point and yield extension increased with increases in hair diameter. Furthermore, yield stress values indicated that strength changes in the hair fibers were due mainly to increases in diameter and not to changes in hair structure. Gelatine ingestion did not affect linear hair growth. Increases in hair diameter was not affected by age of subjects or diet quality. Generally, male subjects exhibited smaller increases than females, possibly as a consequence of greater initial hair thickness. A proposed mechanism of action for the effect of gelatine on scalp hair is discussed.
... Hair. The effect of daily gelatine ingestion on human scalp hair was studied in a normal adult population [68]. The most dramatic effect of supplementing the normal diet with 14 grams of gelatine daily was an increase in hair diameter averaging 9.3 % in the first study and 11.3 % in the second study. ...
... Increases in hair diameter was not affected by age of subjects or diet quality. Generally, male subjects exhibited smaller increases than females, possibly as a consequence of greater initial hair thickness [68]. ...
Колаген є основним компонентом дерми. Він складає 75 % сухої ваги шкіри. З віком вміст колагену зменшується в шкірі через зменшення продукування його фібробластами і більш високою швидкістю обміну речовин. Це призводить до загальних ознак старіння шкіри, тобто до зниження еластичності шкіри, появи тонких ліній і зморщок. Таким чином, існує потреба в додатковому колагені в шкіру. Це неможливо зробити за допомогою (місцевого нанесення) кремів, оскільки розмір молекули (колагену) не дозволяє їй абсорбуватися через шкіру. Навпаки, пероральні гідролізати колагену легко засвоюються кишечником і досягають шкіри в достатній кількості, де вони залишаються протягом певного часу. Багато досліджень, розглянутих у цій статті, показують переваги перорального прийому гідроліту колагену не тільки для шкіри, а й для нігтів, росту волосся і навіть при целюліті.
... Gelatin has a collapsed triple helical structure and has been used in foods, pharmaceuticals, cosmetics, and photographic film at the industrial scale. It has been suggested that ingestion of gelatin improves conditions of joints, skin, nails, and hair [2][3][4]. The enzymatically degraded product of gelatin, referred to as "collagen hydrolysate" or "collagen peptide", has been developed in order to enhance the absorption and solubility of the molecule. ...
Levels of short linear hydroxyproline (Hyp)-containing peptides, such as prolyl-hydroxyproline (Pro-Hyp), increase in human blood after the ingestion of collagen hydrolysate, which has been associated with beneficial effects for human skin and joints. The present study demonstrates the presence of a novel food-derived collagen peptide, cyclic Pro-Hyp, in human blood after the ingestion of collagen hydrolysate. The cyclic Pro-Hyp levels in plasma samples were estimated by liquid chromatography mass spectrometry (LC-MS). Cyclic Pro-Hyp levels significantly increased in the plasma after ingestion of collagen hydrolysate, reaching a maximum level after 2 h and then decreasing. The maximum level of cyclic Pro-Hyp in plasma ranged from 0.1413 to 0.3443 nmol/mL, representing approximately 5% of linear Pro-Hyp in plasma after ingestion of collagen hydrolysate. Addition of cyclic Pro-Hyp in medium at 7 nmol/mL significantly enhanced the growth rate of mouse skin fibroblasts on collagen gel more extensively compared to linear Pro-Hyp.
... In addition, consumption of collagen peptides has been reported to improve strength of nails [30][31][32][33], increase blood flow to the fingers [34], thicken thinning hair [35,36], in addition to other beneficial effects. ...
The skin is said to be “a mirror reflecting who you are inside”. Indeed, beauty is not simply one’s external appearance, but it also comes from within; beauty also comes from paying attention to both physical and mental health. Attention to have attractive skin has been on the rise in many age groups over the last decade; even women in their 20’s often expresses the desire to look younger and fresher. Products containing collagen peptides drive the growth of the health and beauty and food and beverage industry. These products moisturize the skin, leading to their widespread popularity. Oral intake of collagen peptides has been found to increase the moisture content of the stratum corneum, thereby increasing the moisturizing capacity of the skin. Hydroxyproline (Hyp), produced as a result of digesting collagen peptides, increases the expression of serine palmitoyltransferase-2 and β-glucocerebrosidase, enzymes involved in ceramide synthesis in the stratum corneum. When taken orally, collagen peptides are absorbed by the body as Hyp or dipeptide, and this is believed to improve the moisturizing capacity of the skin by increasing the amount of ceramides in the stratum corneum. Consuming foods that beautify the skin is essential to maintain beautiful and healthy skin. Ingredients with skin-enhancing effects are absorbed by the body when ingested as food, and then distributed throughout the skin. This provides effective skin clarifying and anti-aging benefits. Substances that offer these actions are attracting the attention of not only consumers but also researchers interested in the science of beauty.
... The gelatin oral intakes showed the beneficial effect on nails (Rosenberg & Oster, 1955;Rosenberg et al. 1957), hair (Scala et al., 1976) and skin (Morganti et al., 1988). Adam (1991) and Moskowitz (2000) have investigated the valuable effect of collagen hydrolysate on two diseases: osteoarthritis and osteoporosis. ...
Novel and innovative functional supplements and bioactive ingredients can be explored from the vast diversity of Malaysian natural based resources. These include freshwater fish and its by-products, edible bird nest, marine seaweeds, and phytochemicals. Enzymatic hydrolysates of food proteins contained many physiologically functional peptides. Among the bioactive peptides, Angiotensin I-Converting Enzyme (ACE) inhibitory and antioxidant peptides derived from food proteins have attracted attention and have been studied comprehensively. Biodiversified resources and their by-products are natural sources of high quality proteins with functional properties beneficial to mankind. Collagen in particular is of interest to enhance its usage from fish skin and bone waste to yield lower molecular weights micro size particles for efficient absorption to target organs related to anti-aging and life extension. Edible bird nests (EBN) are a valuable source of high quality functional proteins. Micro sized protein hydrolysates, collagen and EBN will be explored to study the therapeutic and nutraceutical value in response of delivery system to the target organs and its effectiveness. Selected seaweeds are utilized in the production of low fat small good meat products. Research and development of seaweed will explore the potential of micro particles of these important marine resources, and extracts of phytochemicals to enhance food quality will also be exploited for functional properties which include anti-oxidative, anti-microbial as well as anti-diabetic and anti-inflammatory effects via blending in meat and other food products, using optimized conditions of microemulsion system and nanotechnology.
... Skin damage induced by repeated UVB irradiation in mice is suppressed by CP ingestion (Tanaka et al., 2009). Brittle nails are improved (Rosenburg et al., 1957), and hair diameter increases following the ingestion of gelatin (Scala et al., 1976). In addition, it was reported recently that serum triacylglycerides are decreased following ingestion of CP (Wu et al., 2004;Saito et al., 2009), suggesting the possibility that ingested CP modulates lipid metabolism by altering the function of the liver and/or adipocytes. ...
Beneficial effects of collagen peptide ingestion to reduce serum triacylglycerides have been reported, suggesting that the physiological conditions of adipocytes are modulated following collagen peptide ingestion. In this study, the effects of prolylhydroxyproline, a major digestive product of ingested collagen peptide in the blood, on the differentiation of mouse 3T3-L1 preadipocytes in vitro were investigated. 3T3-L1 preadipocytes were induced to differentiate to adipocytes and treated with prolylhydroxyproline, or with an amino acid mixture of proline and hydroxyproline as a control. The amount of lipid was not affected by these treatments. However, the size of the lipid droplet was significantly smaller when treated with prolylhydroxyproline compared to the amino acid mixture or the non-treated control. Proton-coupled oligopeptide transporters were expressed in non-differentiated and/or differentiated 3T3-L1 cells. These results suggest that prolylhydroxyproline might modulate the morphology of lipid droplets by incorporation into adipocytes through the transporters.
... The oldest description of beneficial health effects associated with gelatin ingestion was written in 1175 by St. Hildegard, who indicated that gelatin ingestion improves joint conditions by reducing pain (Moskowitz, 2000). Other human studies have demonstrated that daily ingestion of gelatin leads to improvement of brittle nails and increases in hair diameter (Rosenberg, Oster, Kallos, & Burroughs, 1957;Scala, Hollies, & Sucher, 1976). ...
The presence of hydroxyproline (Hyp)-containing peptides in human blood after collagen hydrolysate ingestion is believed to exert beneficial effects on human health. To estimate the effective beneficial dose of these peptides, we examined the relationship between ingested dose and food-derived Hyp levels in human plasma. Healthy volunteers (n = 4) ingested 30.8, 153.8 and 384.6 mg per kg body weight of collagen hydrolysate. The average plasma concentration of Hyp-containing peptides was dose-dependent, reaching maximum levels of 6.43, 20.17 and 32.84 nmol/ml following ingestion of 30.8, 153.8 and 384.6-mg doses of collagen hydrolysate, respectively. Ingesting over 153.8 mg of collagen hydrolysate significantly increased the average concentrations of the free and peptide forms of Hyp in plasma. The Hyp absorption limit was not reached with ingestion of as much as 384.6 mg of collagen hydrolysate. These finding suggest that ingestion of less than 30.8 mg of collagen hydrolysate is not effective for health benefits.
... For examples, collagen peptides as a food supplement may improve low bone mineral density in people in malnutrition and people suffering degenerative joint diseases [7][8][9]. Reports also indicated that consumption of collagen can thicken hairs [10], improve nail disorders such as brittle nails [11], increase the size of collagen fibrils in Achilles tendon [12], induce fibroblast density, and enhance formation of collagen fibrils in dermis etcetera [13]. Traditionally, collagens are derived from livestock sources, such as bovine hide and bones as well as swine skin [14]. ...
Fish-scale collagen peptides (FSCPs) were prepared using a given combination of proteases to hydrolyze tilapia (Oreochromis sp.) scales. FSCPs were determined to stimulate fibroblast cells proliferation and procollagen synthesis in a time- and dose-dependent manner. The transdermal penetration capabilities of the fractionationed FSCPs were evaluated using the Franz-type diffusion cell model. The heavier FSCPs, 3500 and 4500 Da, showed higher cumulative penetration capability as opposed to the lighter FSCPs, 2000 and 1300 Da. In addition, the heavier seemed to preserve favorable coiled structures comparing to the lighter that presents mainly as linear under confocal scanning laser microscopy. FSCPs, particularly the heavier, were concluded to efficiently penetrate stratum corneum to epidermis and dermis, activate fibroblasts, and accelerate collagen synthesis. The heavier outweighs the lighter in transdermal penetration likely as a result of preserving the given desired structure feature.
... On the other hand, gelatin lacks tryptophan, an essential amino acid, and the amount of other essential amino acids is small (2). Nevertheless, it has been reported that the ingestion of gelatin has beneficial effects on osteoarthritis (3), nail defects (4,5), hair growth (6), and the rate of metabo lism (7). In this study, we investigated the effect of inges tion of gelatin and casein on BMD of mice. ...
Malnutrition, particularly protein undernutrition, contributes to the occurrence of osteoporotic fracture by lowering bone mass. In this study, the effects of dietary protein on bone mineral density and body weight in protein undernutrition were compared between gelatin and milk casein. When mice were fed for 10 wk with a low protein diet containing 10(%) casein or 6% casein +4% gelatin, there was no significant difference in the final body weight between the 6% casein+4% gelatin group and the 10% casein group. In contrast, bone mineral content and bone mineral density of the femur were significantly higher in the 6% casein+4% gelatin group than in the 10% casein group. Bone mineral content and bone mineral density did not differ significantly in 14% protein groups between 14% casein and 6% casein +80% gelatin. These results suggest that gelatin has differential effects on bone mineral density and body weight in protein undernutrition.
... For example, lower bone mineral density in protein malnutrition and joint disease are improved by ingestion of CP ( 12 , 13 ). It has also been reported that hair thickness increased after prolonged ingestion of CP ( 14 ) and that nail disorders, such as brittle nails, were improved by CP intake ( 15 ). Recently, we reported that ingestion of CP increases the size of collagen fibrils in the rabbit Achilles tendon in a dose-dependent and protein-specific manner ( 16 ). ...
In order to investigate the effects of collagen peptide ingestion on fibroblasts and the extracellular matrix in the dermis, collagen peptide was administered orally to pigs at 0.2 g/kg body weight/d for 62 d, and its effects were compared with those of lactalbumin and water controls. Fibroblast density, and diameter and density of collagen fibrils were significantly larger in the collagen peptide group than in the lactalbumin and water control groups. The two major components of dermal glycosaminoglycans, hyaluronic acid and dermatan sulfate, which are present in the inter-fibrillar space, did not differ significantly among the three groups. However, the ratio of dermatan sulfate, which is derived from fibril-bound decorin, was largest in the collagen peptide group. These results suggest that ingestion of collagen peptide induces increased fibroblast density and enhances formation of collagen fibrils in the dermis in a protein-specific manner.
Collagen and elastin are extracellular matrix protein and their hydrolysates prepared form marine materials are used as functional food ingredients. The beneficial effects on human skin and joint conditions after oral ingestion have been reported. To elucidate the mechanisms for the beneficial effects, we attempted to detect the food-derived peptides in human blood after oral ingestion of the hydrolysate. Pro-Hyp and Pro-Gly were identified as major food-derived peptides in human blood after ingestion of collagen and elastin hydrolysate respectively. We have demonstrated that the bioactivities of those peptides on human skin fibroblast. Thus, it has been speculated that the food-derived peptides in human blood may play significant role in the beneficial effect after the ingestion of the hydrolysates. We also found the dose-dependent increase of food-derived collagen peptides in human blood that may causes individual differences on the beneficial effects. For effective utilization and value addition of marine products, it is important to understand the more detailed mechanism for the beneficial effects and potential bioactivity of marine food-derived peptides.
Sono commercializzati numerosi prodotti anticaduta. Tuttavia, pochissimi hanno un⬢attivita dimostrata. Una diagnosi accurata delle cause della caduta e sempre necessaria prima di consigliare o prescrivere un prodotto anticaduta. La conoscenza della fisiopatologia della perdita dei capelli e del ciclo del capello e un prerequisito per comprendere i criteri di qualita richiesti per gli studi clinici che, da soli, consentono una valutazione obiettiva delle presunte proprieta dei prodotti anticaduta. Secondo questi criteri, viene presentata un⬢analisi critica della letteratura medica concernente i principi attivi anticaduta attualmente presenti sul mercato.
Objective: Effects of fish-derived collagen peptide (FCP) on skin properties were investigated. Methods: Placebo-controlled double-blind trial was conducted in Japanese women (35-65 years of age) with dry and saggy face skin. They ingested 5 g of placebo or FCP for 8 weeks, and skin properties and subjective feeling of skin conditions were examined before and after ingestion for 4 and 8 weeks. Results: Decrease of wrinkle number was significantly larger (P = 0.034) in the FCP group than in the placebo group at 8 weeks by sub-group analysis. In women with dry face skin, texture improved significantly (P=0.010) in the FCP group than in the placebo group, and number of red areas showed tendency of improvement (P=0.054) at 8 weeks in the FCP group compared to the placebo group. Inter-group significant difference (P = 0.008) was observed for subjective feeling of skin conditions at 8 weeks. Conclusions: Ingestion of FCP improves skin properties and subjective feeling of skin conditions.
Fish gelatin is a versatile ingredient, offering novel and viable properties and meeting the demands of the global halal/kosher market. Unlike the invariable composition of land-based mammalian gelatin, fish gelatin can be extracted from the skins, bones and scales of cold- or warm-water fish, providing a lot of variation in composition, particularly with respect to amino acid content, and allowing diverse applications in the food and pharmaceutical industries. Fish gelatins are available in both gelling and nongelling forms. The most important challenges of fish gelatin are its fishy odor and poor rheological properties, limiting its utility to a few products. Development of improved processes for eliminating the odor and enhancing the desirable functional and rheological properties by incorporating co-enhancers would certainly make fish gelatin a versatile ingredient for both the food and the pharmaceutical industry.
BACKGROUND:
Recent studies show that enzymatically hydrolyzed collagen, the collagen peptide is absorbed and distributed to joint tissues and has analgesic and anti-inflammatory properties. A double blind placebo controlled randomized trial with collagen peptides isolated from pork (PCP) and bovine bone (BCP) sources was carried out to study the effectiveness of orally supplemented collagen peptide to control the progression of osteoarthritis in patients diagnosed with knee osteoarthritis. Improvement in treatment was assessed with reduction in Western Ontario McMaster Universities (WOMAC), visual analogue scale (VAS) and Quality of Life (QOL) scores from baseline to 13 weeks (Visit 7). Safety and tolerability were also evaluated.
RESULTS:
There was significant reduction from base line to Visit 7 in the primary end points of WOMAC and VAS scores and in the secondary end point of QOL score in subjects with PCP and BCP groups, while in subjects with placebo group the end point indices remained unaltered. Furthermore, all the score levels of WOMAC, VAS and QOL decreased significantly (p < 0.01) in study group compared to placebo group in Visit 7.
CONCLUSION:
The study demonstrated that the collagen peptides are potential therapeutic agents as nutritional supplements for the management of osteoarthritis and maintain joint health.
This paper relates the comparison of three methods applied to characterize the molecular weight of hydrolyzed collagen (HC). The high-pressure size-exclusion chromatography (HPSEC) performed on hydrophilic macroporous copolymer beads with an aqueous denaturing eluent allows the determination of the molecular weights distribution and of the weight—and number-average molecular weights. The viscosity measured in standard conditions and the number-average molecular weight determined by formol titration are correlated respectively with the weight-average molecular weight (log scale) and the number-average molecular weight determined by HPSEC.
Dietary supplements (vitamins, polyphenols, micronutrients and proteins) have demonstrated beneficial effects on skin health. The classical route of administration of active compounds is by topical application and manufactures have substantial experience of formulating ingredients in this field. However, the use of functional foods or nutraceuticals for improving skin condition is increasing. The preclinical efficacy assays and bioavailability trials provide a basis from which to establish appropriate collagen hydrolysate (CH) intakes that might impact skin health outcomes. This commentary deals essentially with the general aspects of CH, bioavailability and findings of preclinical studies concerning the effects of CH intake on skin. To comprehensively study the different benefits of CH on skin, controlled clinical trials are needed in addition to the previous pre-clinical and bioavailability assays. Gaps in knowledge are identified and suggestions are made for future research.
To review the current status of collagen hydrolysate in the treatment of osteoarthritis and osteoporosis.
Review of past and current literature relative to collagen hydrolysate metabolism, and assessment of clinical investigations of therapeutic trials in osteoarthritis and osteoporosis.
Hydrolyzed gelatin products have long been used in pharmaceuticals and foods; these products are generally recognized as safe food products by regulatory agencies. Pharmaceutical-grade collagen hydrolysate (PCH) is obtained by hydrolysis of pharmaceutical gelatin. Clinical studies suggest that the ingestion of 10 g PCH daily reduces pain in patients with osteoarthritis of the knee or hip; blood concentration of hydroxyproline is increased. Clinical use is associated with minimal adverse effects, mainly gastrointestinal, characterized by fullness or unpleasant taste. In a multicenter, randomized, doubleblind, placebo-controlled trial performed in clinics in the United States, United Kingdom, and Germany, results showed no statistically significant differences for the total study group (all sites) for differences of mean pain score for pain. There was, however, a significant treatment advantage of PCH over placebo in German sites. In addition, increased efficacy for PCH as compared to placebo was observed in the overall study population amongst patients with more severe symptomatology at study onset. Preferential accumulation of 14C-labeled gelatin hydrolysate in cartilage as compared with administration of 14C-labeled proline has been reported. This preferential uptake by cartilage suggests that PCH may have a salutary effect on cartilage metabolism. Given the important role for collagen in bone structure, the effect of PCH on bone metabolism in osteoporotic persons has been evaluated. Studies of the effects of calcitonin with and without a collagen hydrolysate-rich diet suggested that calcitonin plus PCH had a greater effect in inhibiting bone collagen breakdown than calcitonin alone, as characterized by a fall in levels of urinary pyridinoline cross-links. PCH appeared to have an additive effect relative to use of calcitonin alone.
Collagen hydrolysate is of interest as a therapeutic agent of potential utility in the treatment of osteoarthritis and osteoporosis. Its high level of safety makes it attractive as an agent for long-term use in these chronic disorders.
In order to investigate whether the oral ingestion of collagen peptide affects the extracellular matrix of tendon, two doses (0.2 g/kg and 1.0 g/kg body weight) were orally administered daily for 56 d to a rabbit, and both the size of collagen fibrils and the amount of glycosaminoglycans in the Achilles tendon were measured in comparison with those in a rabbit fed with a control protein, lactalbumin, or water alone. Ingestion of collagen peptide or lactalbumin induced a significant increase in collagen fibril diameter and a decrease in fibril density except for a high dose of lactalbumin compared with the water control. A histogram pattern of fibril diameter in a high dose of collagen peptide showed a peak at 160-180 nm, which was not observed in other groups. However the percentage of diameters over 200 nm was the lowest in this group but highest in the low-dose group of collagen peptide. The mean fibril diameter and mass average diameter of a high dose of collagen peptide were significantly smaller than those in a low dose. The amount of dermatan sulphate increased in the high-dose groups, while the amount of hyaluronic acid decreased in rabbits fed with collagen peptide or lactalbumin at either dose. These results suggest that the ingestion of collagen peptide affects the size of collagen fibrils and composition of glycosaminoglycans in the Achilles tendon and thus may improve the mechanical properties of the Achilles tendon.
ResearchGate has not been able to resolve any references for this publication.