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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.
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No. 1058 Food Chemistry and Biotechnology, Vol. 73 2009
Institute of Fermentation Technology and Microbiology
Technical University of Lodz
Review: Professor Marianna Turkiewicz, Ph.D., D.Sc
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.
1. Introduction
Modern lifestyle characterized with permanent lack of time results in
consumption of a highly processed food which does not have any beneficial
effect on our health. Inbalanced and incomplete diets can be a reason of many
diet depended diseases. If we care about healthy lifestyle, we have to include
nutrient-rich food to our normal diet. Diet supplements are such kind of health
beneficial substances which contain concentrated source of nutrients or other
components causing positive physiological effects. Diet supplements are
produced in the form of powder, capsules, powder in sachets, liquid in bottles
with droppers or in other forms suitable for proper dosage. It is well recognized
that diet supplements are not medicines and their use is not regulated by the
pharmaceutical law [25].
K. Dybka, P. Walczak 84
2. Collagens characteristic
Collagen proteins are the most abundant in the human and animal body.
They are the major proteins of connective tissue, skin, tendons, cartilage,
ligaments, cornea, teeth, nails and hair [8]. Proteins of collagen family represent
a group of varied extracellular matrix molecules linked by the occurrence of the
collagen triple-helical domain as a common structural element [5]. In vertebrates
organisms, at least 27 types of collagen with 42 distinct polypeptide chains has
been reported [19]. According to similarieties in their structure and
supramolecular organization, they are classified into fibril-forming, fibril-
associated collagens with interruptions in triple helix (FACITs), network-forming
collagens, anchoring fibrils or transmembrane collagens [22]. The different
collagen types are characterized by considerable complexity and diversity in their
structure, their splice variants, the presence of additional, non-helical domains
and their function. All members of the collagen family have one characteristic
feature a right-handed triple helix composed of -chains (Fig. 1). Triple-helix
can be formed by three identical chains (homotrimers) as in types II, III, VII,
VIII, X, XIII, XV, XVII, XXIII, XXV collagen and by two or three different
chains (heterotrimers) as in types I, IV, V, VI, IX, and XI collagen [19, 22]. Each
of the three collagen -chains coils into a left-handed helix which assemble to
rope-like figure bordered by the C- and N-propeptides [8].
Fig. 1. Molecular structure of fibrillar collagens
Collagens consist of a high amount of glycine (about 33% amino acid
residues), proline (12-14%), 4-hydroksyproline (<14%) and 4-hydroksylysine
(1.5%) [17]. Tryptophan and cysteine were not noticed [21]. Collagens are
known to share a repeating pattern Gly-X-Y in which the X and Y positions are
frequently occupied by proline (Pro) and 4-hydroksyproline (Hyp) residues
Collagen hydrolysates as a new diet supplement 85
[2, 7, 17]. Research have reported that the content of Hyp plays an especially
important role in stabilizing the triple-helical conformation in collagen and in
peptides with collagen-like domains [2, 4]. Hydroksyproline residues stabilize
triple helical conformation by sharing direct hydrogen bonds[2]. The most
common motif in fibril-forming collagens is repeating sequence Gly-X-Y
resulting in triple helical domains of 300 nm in length which corresponds to
about 1000 amino acids [8]. The three residues in the repeating triplet occupy
distinct positions within the supercoiled helix. The central possition of Gly
residues makes this residue not suitable for interacting with other residues.
Interactions caused by proximity between neighboring chain are related with less
solvent accessibility of Y position residues. In contrast to Gly and Y positions in
triplet motif, the greatest exposure for interactions, shows the X position [5].
Bella et al. [2] suggested that the water molecules aggregate as a shell to the
carbonyl and hydroxyprolyl groups resulting diverse conformation with a
specific motifs of water bridges bonding oxygen atoms within a single chain or
between different chains of triple helix.
3. Biosynthesis and degradation of collagen
Permanent collagens exchange processes in our body takes place during the
whole human life. Old fibrils are replace by new one all the time. When we are
young, collagen production and degradation are in dynamic balance, but during
maturation of tissues, degradation is being more intenssive. UV radiation,
smoking cigarettes, stress and unhealthy diet lead to the degradation of natural
collagen structure and to earlier senility.
3.1. Biosynthesis of collagens
The biosynthesis of fibril-forming collagen is a multisteps and complicated
process which takes place in intracellular and extracellular spaces.
It begins with transcription of the genes and ends with assemble of a triple helix
collagen fibrils into fibers with their final distinctive functions in tissues (Fig. 2).
Cell type, growth factors and cytokines are considered as particularly agents in
the system of transcriptional regulation during collagen biosynthesis. It is well
konown that the major group of collagen genes assemble into a complex of 3 to
117 exons and introns, characterised with more than 50 exons encoding the
mRNAs of fibrillar collagens. It was reported that other mRNA species could be
found. They are related with mulitple initiation sites of transcription or
alternative splicing of exons. The process of mRNA translation into synthesized
polypeptide chains (preprocollagen) takes part in membrane-bound ribosomes.
K. Dybka, P. Walczak 86
Fig. 2. The main steps in biosynthesis of fibril-forming collagens
In the endoplasmic reticulum preprocollagen is involved in several
posttranslational modifications. Three vitamin C-depended enzymes, prolyl
3-hydroxylase, prolyl 4-hydroxylase and lysyl hydroxylase catalyze hydroxylation
Collagen hydrolysates as a new diet supplement 87
of proline and lysine residues. Presence of 4-hydroxyproline is critical for
hydrogen bonding within molecule [8, 19]. Hydroksylysine residues are recognized
as bonding agents within fibril chains. The 3-hydroxyproline function has not been
reported, yet. Other action is glycosylation of some of hydroksylysine residues and
asparagine residues in C and/or N propeptides. After the association of C
propeptides and formation of disulfide bonds, three chains form molecule
called procollagen, this precursor of collagen is secreted and released into the
extracellular space in transport vesicles of Golgi apparatus.
Then procollagen trimers are processed in different ways which depend on
the collagen type. The C-propeptides and N-propeptides are removed by specific
metalloproteases. Following the procollegen modifications, the tropocollagen
fibrils are assembled. It was found that some of fibril-forming collagens (e.g. I,
II, III, V, XI) associate spontaneously into fibrillar structures during in vitro test.
It has been compared to the crystalization process. Several models described self-
assembly structure encoded in collagens and formation mechanism of periodic
fibrils. Fully formed fibers are stabilized by hydrophobic and electrostatic
interactions between collagen monomers and covalent cross-links joining
differently orientated fibrils in tissues [8, 28].
3.2. Degradation of collagen
Collagen is a very stable protein in normal healthy conditions. Collagen
degradation may proceed in different ways, but generally it is belived that there
are two possibilities intracellular and extracellular. The main cause of intercellular
degradation process are proteolytic enzymes, particularlly cathepsins. Cathepsins
are various proteolytic enzymes found in animal tissue that catalyze the
hydrolysis of proteins into polypeptides in acid environment. In the extracellular
way there are several stages including depolymerisation which effects with
deterioration of molecular structures; activity of collagen-specific enzymes
tissue collagenases; heat-disintegration at body temperature of products of
collagenases degradation, which lose triple helices structure and become
available for non specific proteinases. Collagenases can be synthesized by many
cells of human body (e.g. fibroblasts, neutrophils, and tumor cells [28].
4. Collagen hydrolysates production
The main source of collagen peptides are bovine hide, bone, pigskin or
fishbones and fish skin. Marine sources are an alternative to bovine or porcine
and they are not associated with the prions related to risk of Bovine Spongiform
Encefalopathy (BSE) [12]. Collagen hydrolysates are manufactured in controlled
hydrolysis process to obtain soluble peptides. The raw material is washed,
K. Dybka, P. Walczak 88
homogenized and demineralized with diluted mineral acid or alkaline. The raw
material is extracted in several stages with warm water. Further enzymatic
degradation of gelatin results in a final product which is collagen hydrolysate
[18, 24, 26]. Clemente [6] has presented enzymatic hydrolysis as the most
appropriate method for preparation of tailor-made peptides. Collagen
hydrolysates vary from each other with respect of peptides molecular weight,
mostly their molecular weight range from 2 to 6 kDa [18, 26]. Its molecular
weight is less than the average molecular weight of peptones. After purification,
the product is concentrated and dried. The most common post-dried procedures
are related to the control of molecular size and the elimination or reduction of
bitterness in the resulting hydrolysates. The most efficient procedure to remove
residual high-molecular weight peptides and proteins or to reduce the antigen
content of hypoallergenic formulas, is ultrafiltration [6].
Several analysis may be done for the quality control of these products: the
osmolarity, analysis of the hydrolysis degree, the molecular weight distribution,
the total nitrogen, amino acid composition and the presence of toxic compounds
(e.g. biogenic amines or pathogens). Protein hydrolysate qualitative analysis use
different techniques based on spectrophotometric, chromatographic and
electrophoretic methods (UV-spectrophotometry, HPLC, SDS-PAGE) [23].
5. Properties and applications of collagen hydrolysates
Gelatin and collagen hydrolysates have been reported to have beneficial
biological functions. Hydrolyzed gelatin products have been designated as
generally recognized as safe (GRAS) food products or food additives by the
Food and Drug Administration (FDA) [1, 18]. Despite the fact that collagen
hydrolysate has been generally regarded as having a low biological value,
because it does not contain all of the essential amino acids, its a reputable
nutritional component often used to supplement other proteins because of its
superb digestibility and high consumer tolerance [26].
5.1. Beneficial role of collagen hydrolysate in health
According to the opinion of many researchers, beneficial effects of oral
administration of collagen hydrolysates results of crossing the intestinal barrier,
by a dietary bioactive peptides, which reach the blood circulation and become
available for metabolic processes [26]. Collagen hydrolysates are used in medical
applications, such as high-energy supplements, geriatric products and enteric,
therapeutic or weight-control diets. Applification of protein hydrolysates in
treatment of patients with specific disorders of digestion, absorption and amino
acid metabolism. Tests also included clinical cure of patients with malnutrition
Collagen hydrolysates as a new diet supplement 89
attached with trauma, burns, cancer and hepatic encephalopaties [6]. Collagen
hydrolysates are good source of amino acids for people suffering from anorexia,
anaemia and for vegetarians (because of absence of meat in their diet). Diet
supplements conataining collagen hydrolysates are considered as improvement
agents in tendon or joint regeneration in physically active athlets with activity-
related joint pain [18, 26].
Orally consumed collagen hydrolysate has been shown to be absorbed
intestinally and to accumulate in cartilage. Speciffically, collagen hydrolysate
ingestion stimulates a significant increase in the synthesis of extracellular matrix
macromolecules by chondrocytes [3]. According to medical data clinical
investigations suggest that ingestion of collagen hydrolysates reduces pain in
patients suffering from osteoarthritis and osteoporosis. It is considered that about
15% of world population suffer from joint pain-related diseases. In Poland an
increasing problem become joint-related diseases connectet with other high risk
disorders agents which are abundant. Increasing risks agents are senility (over 50%
of elderly people suffer from rheumatism), gender (a high amount of patients are
women, particularlly after menopause), body weight (huge body weight is
a reason of joint overload and results in joint pain), constantly excessive sport
activity, joint injury (e.g. dislocations), metabolic diseases (e.g. diabetes) [24].
Collagen hydrolysates are involved in cartilage matrix synthesis [26]. Over
almost two decades scientists have studied a relationships between therapeutic
trials in joint diseases and collagen, gelatin or collagen hydrolysates. In numerous
studies researchers accepted dose of 10 g of collagen hydrolysates daily as a safe
and well tolerated by patients. Additionaly clinical tests have proved that this
level of daily ingested proteins can reduce the pain in comparison with placebo
group patients [18].
Several scientific reports have presented good bioavailability of hydrolyzed
collagen, after oral administration by animals and human beings. Oesser et al. [20]
discovered that about 95% of orally applied collagen hydrolysate was absorbed
within the first 12 h. Wu et al. [26] described the high safety of eating collagen
hydrolysates in an animal model (1.66 g/kg of body weight per day). Studies
related with preparations consisting gelatin derivated peptides showed good
tolerance and little side effects including a sensation of unpleasant taste, a feeling
of heaviness in the stomach, and a bloated feeling or pyrosis after oral
administration [20].
According to opinion of Zague [26] some studies described chemotactic
activity of short peptides (Pro-Hyp and Pro-Hyp-Gly) to human fibroblast,
peripheral blood neutrophils and monocytes in the cell culture. Collagen-
degradation peptides might attract these cells and result in repair of damaged
tissue. It is believed that collagen hydrolysates can not be absorbed from skin and
the basis of the skin effectiveness of collagen hydrolysate depends on a gradual
improvement of water absorption to skin as a result of possitive effect of the oral
K. Dybka, P. Walczak 90
administration of supplement. A beneficial effects has been also observed for
skin-related organs and for hair and nail quality.
Antihypertensive and antioxidative activities of bioactive peptides isolated
from collagen hydrolysates have been discovered [26]. Collagen and gelatin
digests contain angiotensin-converting enzyme (ACE) inhibitory peptides. ACE
play an important role in blood pressure regulation and inhibition of this enzyme
can cause an antihypertensive effect [14, 15, 16]. Protein supplements (e.g.
collagen hydrolysates) may be useful to enhance nitrogen retention [10].
5.2. Industrial application of collagen hydrolysates
Gelatin and hydrolyzed collagen are utilized in food industry in confectionery
(to improve texture, chewiness and foam stabilization), dairy (as stabilisation
and texturization agents), bakery (to provide stabilization, emulsification and
gelling), low-fat spreads (to provide fat reduction, creaminess and mouthfeel), in
meat-processing (to provide water-binding e.g. in reconstituted hams), in wine
and fruit juices production (fining agent) [1, 12, 13, 27]. Collagen hydrolysates,
like all protein hydrolysates show technological advantages such as good
solubility, heat stability and relatively high resistance to precipitation by many
agents, such as metal ions or pH [6]. Protein hydrolysates have an excellent
solubility at high degree of hydrolysis, which is a substantially useful
characteristic for many food applications and influences other functional features
such as emulsifying and foaming properties [9, 15].
Collagen hydrolysate has a high water-binding capacity and can be used as
an essential product low-calorie carbohydrates or low fat food production.
In the pharmaceutical industry gelatin and collagen hydrolysates are used to
manufacture capsules, implants and intravenous infusions [11, 12].
6. Conclusions
Collagens are the most abundant group of organic macro-molecules in
human and animal body. Because of their tensile strength, they perform
numerous important structural functions within the body, especially in connective
tissues. Collagen proteins are essential in connective tissues of such organs as
heart, intestines, lungs or parenchymal organs like liver and kidneys; as protein
matrix of the skeleton and its related structures (e.g. bones, teeth, tendons,
cartilage and ligaments); in fibrous matrix of skin and blood vessels [6, 7, 18, 26]. Its
excellent properties are result of their amino acid composition and molecular
structure. Collagens are also involved in the management of cellular mediators.
Collagen protein (in the form of collagen hydrolysate) has been shown to
improve skin hydration, reduce wrinkles and decrease pain and functionality
Collagen hydrolysates as a new diet supplement 91
disorders in joint diseases. In addition, collagen hydrolysate seems to be a relatively
inexpensive and widespread available protein source.
Collagen hydrolysate and gelatin can be used in food, cosmetics or
pharmaceutical industry as a natural additive revealing an antioxidant properties
with competitive foaming and emulsifying functionalities [9,15]. Finally, such
properties like excellent biodegradability, low immunogenicity and the
possibilities for large-scale production make them interesting compounds for
a wideespread industrial use in food industry, cosmetics industry or medicine.
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[21] Pytrus-Sdłak B.: Kosmetyka ozdobna i pielgnacja twarzy. Medpharm Polska.
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nowoczesny suplement diety. Przem. Spo. 4, 42-44, (2009).
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ywnoci. Przem. Spo. 6, 49-51, (2007).
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Chem. 90, 23-28, (2005).
[28]; 4.08.2009
W artykule dokonano przegldu literatury dotyczcej właciwoci hydrolizatów
kolagenu stosowanych jako suplementy diety. Aktywno biologiczna i oddziaływanie
prozdrowotne hydrolizatów białek kolagenowych zostały udowodnione naukowo,
zwłaszcza w leczeniu chorób zwyrodnieniowych koci i stawów oraz poprawie
kondycji skóry, włosów i paznokci. Wysoka tolerancja pacjentów na spoywane
hydrolizaty kolagenu w długim czasie powoduje, i s one atrakcyjnym, prozdro-
wotnym suplementem diety.
Instytut Technologii Fermentacji i Mikrobiologii
Politechnika Łódzka
... Collagen proteins are the most abundant in the human and animal body vital proteins of connective tissue, skin, tendons, cartilage, ligaments, cornea, teeth, nails and hair [2,10,11]. The main sources of collagen peptides are bovine hide, bone, pigskin and marine sources [10,11]. ...
... Collagen proteins are the most abundant in the human and animal body vital proteins of connective tissue, skin, tendons, cartilage, ligaments, cornea, teeth, nails and hair [2,10,11]. The main sources of collagen peptides are bovine hide, bone, pigskin and marine sources [10,11]. Collagen hydrolysates are processed via hydrolysis until soluble peptide was achieved [10]. ...
... The main sources of collagen peptides are bovine hide, bone, pigskin and marine sources [10,11]. Collagen hydrolysates are processed via hydrolysis until soluble peptide was achieved [10]. In the food industry, many studies have been conducted to study the physicochemical, microbiological and sensory property of meat product incorporated with collagen. ...
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Pork and bovine collagen incorporated into meat products showed promising functional properties as food ingredients but has the halal issue. This study investigated the effect of incorporating fish collagen hydrolysate (FCH) as a fat replacer in buffalo patties in terms of proximate values, texture and colour properties. There were five different formulations including a control (10% fat, 0% FCH), A (7.5% fat, 2.5% FCH), B (5% fat, 5% FCH), C (2.5% fat, 7.5% FCH), and D (0% fat, 10% FCH). There were no significant differences (p>0.05) between all formulations in terms of cooking yield, shrinkage, water-holding capacity, and pH value. The sensory test showed no significant difference (p>0.05) between all formulations in terms of colour, appearance, juiciness, aroma, and overall acceptability, while sample D with 10% FCH had significantly lower (p<0.05) acceptability in flavour and texture as compared to other formulations. Formulations with higher FCH had higher protein and ash yet lower moisture content. The fat content (w/w) significantly increased (p<0.05) from 3.44% in the control sample to 4.80% in formulation A and 4.49% in formulation B. However, the fat content in formulation C (2.46%) and D (3.11%) were significantly (p<0.05) lower than the control sample. All formulations had no significant difference (p>0.05) in terms of textural properties, except formulation B and formulation C which exhibited significantly (p<0.05) highest (0.39) and lowest (0.17) cohesiveness, respectively. Raw beef patties with higher FCH content were darker as compared to patties with lower FCH content. There were no significant differences (p>0.05) in yellowness and redness of buffalo patties with or without FCH incorporation before and after cooking. In conclusion, FCH has the potential to be used as a fat replacer in the production of low-fat patties.
... The development and utilization of both biomaterials and bio-energy are methods to resolve these problems. Collagen, which exists in the connective tissue of animals, is the most abundant protein in various vertebrates and invertebrates (Dybka and Walczak, 2009). Almost one-third of mammalian proteins are collagens. ...
... What's more collagen peptides are safe and low allergenicity. Some collagen peptides have been designated as Generally Recognized As Safe (GRAS) food products or food additives in USA (Dybka and Walczak, 2009). Then collagen peptides are potential and functional food resources. ...
... However, they still contain almost all of the natural amino acids and are rich in glycine, praline and so forth. Collagen peptides or hydrolysates provide amino acids for people with anorexia, anaemia and for vegetarians whose diet is lack of meat (Dybka and Walczak, 2009) and collagen peptides can be used in combination with other amino acids, such as tryptophan to overcome its low content of some essential amino acids. Due to presented, collagen peptides are still a good source of our foods. ...
... Animal-derived refers to proteins directly originating from animal sources such as meat, fish, poultry, eggs and dairy (and the constituents whey and casein protein) [7], which are also regarded as "complete" proteins (i.e., they provide sufficient amounts of all essential amino acids (EAA) to meet human requirements) [8]. Plant-derived refers to proteins obtained from plant sources (e.g., wheat, soy) [9] and collagenderived refers to proteins derived from gelatin and/or collagen hydrolysates [8,10]. Notably, gelatin/collagen hydrolysates-derived proteins do originate from animal sources (e.g., bone, pigskin, fish skin [10]), however, they are not regarded as "complete" proteins, hence our rationale for distinguishing them from animal-derived protein sources for the purpose of this review. ...
... Plant-derived refers to proteins obtained from plant sources (e.g., wheat, soy) [9] and collagenderived refers to proteins derived from gelatin and/or collagen hydrolysates [8,10]. Notably, gelatin/collagen hydrolysates-derived proteins do originate from animal sources (e.g., bone, pigskin, fish skin [10]), however, they are not regarded as "complete" proteins, hence our rationale for distinguishing them from animal-derived protein sources for the purpose of this review. Finally, blended protein sources refer to different sources/types of protein combined together to form one nutritional load. ...
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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.
... Collagen can be transformed into 66 gelatin, which is consumed as a food source, via heat treatment. Gelatin hydrolysates generated 67 using edible enzymes are natural additives and approved by the Food and Drug Administration 68 (FDA) ( Dybka and Walczak, 2009). In fact, gelatin hydrolysates containing soluble peptides 69 are manufactured using proteolytic enzymes via controlled hydrolysis. ...
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The protective effect of pig skin gelatin water extracts (PSW) and the low molecular weight hydrolysates of PSW generated via enzymatic hydrolysis with Flavourzyme® 1000L (LPSW) against scopolamine-induced impairment of cognitive function in mice was determined. Seventy male ICR mice weighing 20-25 g were randomly assigned to seven groups: Control (CON); scopolamine (SCO, 1 mg/kg B.W., intraperitoneally (i.p.); tetrahydroaminoacridine 10 [THA 10, tacrine; 10 mg/kg B.W. per oral (p.o.) with SCO (i.p.)]; PSW 10 (10 mg/kg B.W. (p.o.) with SCO (i.p.); PSW 40 (40 mg/kg B.W. (p.o.) with SCO (i.p.); LPSW 100 (100 mg/kg B.W. (p.o.) with SCO (i.p.); LPSW 400 (400 mg/kg B.W. (p.o.) with SCO (i.p.). All treatment groups, except CON, received scopolamine on the day of the experiment. The oxygen radical absorbance capacity of LPSW 400 at 1 mg/mL was 154.14 μM Trolox equivalent. Administration of PSW and LPSW for 15 weeks did not significantly affect on physical performance of mice. LPSW 400 significantly increased spontaneous alternation, reaching the level observed for THA and CON. The latency time of animals receiving LPSW 400 was higher than that of mice treated with SCO alone in the passive avoidance test, whereas it was shorter in the water maze test. LPSW 400 increased acetylcholine (ACh) content and decreased ACh esterase activity (p<0.05). LPSW 100 and LPSW 400 reduced monoamine oxidase-B activity. These results indicated that LPSW at 400 mg/kg B.W. is a potentially strong antioxidant and contains novel components for the functional food industry.
... The market demand for the hydrolysed collagen has increased over the past decades due to it has broad application in different types of industries such as food and beverages, pharmaceutical, nutraceutical and cosmetics industries (Dybka & Walczak, 2009). The broad range of applications of the hydrolysed collagen is contributed by the ability to dissolve in water and excellent emulsifying properties compare to native collagen which is not soluble in water due to higher molecular weight. ...
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This study was carried out to evaluate the effects of different enzymatic treatments on the physicochemical and functional properties of hydrolysed collagen extracted from the skin of milkfish (Chanoschanos). Alcalase (A) and bromelain (B) treatment with different hydrolysis time (30, 60 and 90 min) were performed to extract the hydrolysed collagens. Bromelain treatment was found to be more effective in enhancing the degree of extractability of hydrolysed collagen, however, the extent of collagen hydrolysis was observed to be more efficient with alcalase treatment. The highest protein content was obtained for A90 (61.73±0.07 %). All samples had relatively low moisture content (<10 %) with pH values in neutral range. Different hydrolysis time for both enzymes resulted in varying emulsion properties and water holding capacity of hydrolysed collagens. However, no significance differences (p>0.05) was observed on the effect of different enzymatic treatments on the stability of emulsion formed. Hydrolysed collagens produced by bromelain hydrolysis were observed to have higher capability to scavenge free radicals, thus higher antioxidative properties (~80 % DPPH radical scavenging activity). Hence, modification of enzymatic hydrolysis treatment could resulted in varying properties of hydrolysed collagen, which can be tailor-made for specific application as functional food ingredient. Keywords: hydrolysed collagen, milkfish skin, physicochemical and functional properties.
... Przypuszcza się, iż doustne przyjmowanie hydrolizatów kolagenu jako suplementu diety wpływa na syntezę makrocząsteczek macierzy zewnątrzkomórkowej, w tym białek kolagenowych. Naukowo udowodniono właściwości prozdrowotne oraz aktywność biologiczną hydrolizatów kolagenu przede wszystkim w leczeniu chorób stawów i kości oraz wpływ na poprawę wyglądu i kondycji skóry, paznokci i włosów [31]. Dzięki rozwojowi nauki w najbliższej przyszłości powinniśmy poznać szczegółowe zależności między właściwościami a budową kolagenów. ...
Collagens are a family of fibrous proteins which are a major component of the extracellular matrix (ECM) in animal organisms. These proteins are found in most tissues and organs (bones, cartilages, skin, ligaments, tendons, corneas). The main functions of collagens include the maintenance of structural integrity, elasticity and tensile strength of the connective tissue. Macromolecules from the collagen family are characterized by a unique structure rich in e.g. glycine, proline and hydroxyproline. The collagen structure consists of three left-handed polypeptide chains which are coiled around each other forming a right-handed rope-like super helix. This structure is stabilized by the presence of interstrand hydrogen bonds. To date, 29 types of collagen have been isolated and described. They differ from each other in structure, functions, and body distribution. Research development has allowed us to understand the structure and properties of native collagens which has resulted in the production of artificial collagen fibrils used in nanotechnology and biomedicine. Collagen materials are considered to be the most useful biomaterials in medicine because of their properties such as non-toxicity, low antigenicity, high biocompatibility and biodegradability. KEY WORDS collagen, biomaterials, regenerative medicine, tissue engineering, atelocollagen Kolageny to rodzina białek fibrylarnych, będąca głównym składnikiem macierzy zewnątrzkomórkowej organizmów zwierzęcych. Białka te występują w większości tkanek i narządów, w kościach, chrząstkach, skórze, więzadłach, ścięgnach, rogówce. Podstawowym ich zadaniem jest utrzymanie integralności strukturalnej i sprężystości tkanki łącznej oraz jej wytrzymałości na rozciąganie. Kolageny charakteryzują się unikatową strukturą bogatą w aminokwasy, takie jak glicyna i prolina oraz hydroksyprolina. Głównym elementem struktury kolagenów są 3 lewoskrętne polipeptydowe łańcuchy, nawijające się wokół siebie i tworzące prawoskrętną konformację liny superhelisowej, która utrzymywana jest dzięki obecności wiązań wodorowych. Dotychczas udało się wyizolować i opisać 29 typów kolagenów charakteryzujących się odmienną strukturą, funkcją oraz występowaniem w organizmie. Rozwój technik badawczych umożliwił poznanie struktury i właściwości naturalnych białek kolagenowych, co z kolei zaowocowało produkcją syntetycznych włókien kolagenowych, wykorzystywanych w nanotechnologii czy biomedycynie. Materiały kolagenowe zaliczane są do najbardziej użytecznych biomateriałów ze względu na takie właściwości, jak minimalna toksyczność, niska antygenowość, wysoka biozgodność oraz biodegradowalność. S Ł O WA K L U C Z O WE kolagen, biomateriały, medycyna regeneracyjna, inżynieria tkankowa, atelokolagen
... Collagen peptides are derived from an enzymatic hydrolysis of collagen, consisting mainly of the amino acids glycine (Gly), proline (Pro), and hydroxyproline (Hyp) (Clemente 2000;Dybka and Walczak 2009;Oesser and Seifert 2003;Walrand et al. 2008;Watanabe-Kamiyama et al. 2010). The amino acids sequence and the molecular weight distribution of the peptides depends on the raw materials source and the specific production process (Iwai et al. 2005;Ohara et al. 2007;Saito et al. 2001). ...
The aim of the study was to evaluate the use of specific collagen peptides in reducing pain in athletes with functional knee problems during sport. 139 athletic subjects with functional knee pain ingested 5 g of bioactive collagen peptides (BCP) or a placebo per day for 12 weeks. The primary outcome of the study was a change in pain intensity during activity was evaluated by the participants and the attending physicians using a visual analogue scale (VAS). As secondary endpoints, pain intensity under resting conditions, the range of motion (ROM) of the knee joint, and the use of additional therapeutic options were assessed. The results revealed a statistically significantly improvement in activity-related pain intensity in the verum group compared with placebo. (ΔVAS<sub>BCP</sub> = 19.5 ± 2.4; ΔVAS<sub>Placebo</sub> = 13.9 ± 2.1; p = 0.046). The results were confirmed by the physician's assessment. (ΔVAS<sub>BCP</sub> = 16.7 ± 1.8; ΔVAS<sub>Placebo</sub> = 12.2 ± 1.8; p = 0.021). Pain under resting conditions was also improved but no significance compared with placebo was detected (ΔVAS<sub>BCP</sub> = 10.2 ± 18.4; ΔVAS<sub>Placebo</sub> = 7.4 ± 15.2; p = 0.209). Due to the high joint mobility at baseline, no significant changes of this parameter could be detected. The use of additional treatment options was significantly reduced after BCP intake. The study demonstrated that the supplementation of specific collagen peptides in young adults with functional knee problems led to a statistically significant improvement of activity-related joint pain.
... 5,10,11 Collagen is a well-known protein for its excellent ability for cell affinity because of the Arg-Gly-Asp (RGD) sequence contained in the molecule that is recognized as binding site of cell adhesion. [12][13][14] Collagen-derived proteins, including type A gelatin, type B gelatin, and collagen hydrolysate, are of high interests as these proteins possess high solubility in water and cost effectiveness, in comparison to other proteins, such as fibrin and laminin, besides the recognition of cell adhesion site. 15 Thus, the three proteins were reasonably selected as test samples. ...
In this study, polycaprolactone (PCL) film, a high potential material used in biomedical applications, was treated by air plasma prior to a conjugation by carbodiimide cross-linking with various types of proteins, including type A gelatin, type B gelatin, and collagen hydrolysate. The properties of modified PCL films were characterized by X-ray photoelectron spectroscopy (XPS), contact angle measurement, and atomic force microscopy. The XPS results showed that oxygen and nitrogen atoms were successfully introduced on the air plasma-treated PCL surface. Primary amine was found on the air plasma-treated PCL films. All proteins were shown to be successfully cross-linked on air plasma-treated PCL films. The wettability and roughness of protein-conjugated PCL films were significantly increased compared to those of neat PCL film. In vitro biocompatibility test using L929 mouse fibroblast showed that the attachment percentage and spreading area of attached cells on all protein-conjugated PCL films were markedly increased. Comparing among modified PCL films, no significant difference on the attachment of L929 on modified PCL films was noticed. However, the spreading areas of cells after 24 hours of culture on type A gelatin- and type B gelatin-modified PCL surfaces were higher than that on collagen hydrolysate-modified surface, possibly related to the lower percentage of amide bond on collagen hydrolysate-conjugated surface compared to those on both gelatin-conjugated PCL ones. This indicated that the two-step modification of PCL film via air plasma and carbodiimide cross-linking with collagen-derived proteins could enhance the biocompatibility of PCL films. © 2016 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 2016.
... Tomar 10 gramos diarios de CH estimula y facilita la síntesis de colágeno tisular y, por lo tanto, ayuda a potenciar la regeneración de los tejidos colaginosos, previniendo y tratando las enfermedades degenerativas que afectan a los mismos (artrosis y osteoporosis) y también el deterioro dérmico. Todo ello viene respaldado por los resultados de los estudios expuestos anteriormente y por recopilaciones de los mismos 24,30,44,49 . ...
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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.
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In recent decades, food waste management has become a key priority of industrial and food companies, state authorities and consumers as well. The paper describes the biotechnological processing of mechanically deboned chicken meat (MDCM) by-product, rich in collagen, into gelatins. A factorial design at two levels was used to study three selected process conditions (enzyme conditioning time, gelatin extraction temperature and gelatin extraction time). The efficiency of the technological process of valorization of MDCM by-product into gelatins was evaluated by % conversion of the by-product into gelatins and some qualitative parameters of gelatins (gel strength, viscosity and ash content). Under optimal processing conditions (48–72 h of enzyme conditioning time, 73–78 °C gelatin extraction temperature and 100–150 min gelatin extraction time), MDCM by-product can be processed with 30–32% efficiency into gelatins with a gel strength of 140 Bloom, a viscosity of 2.5 mPa.s and an ash content of 5.0% (which can be reduced by deionization using ion-exchange resins). MDCM is a promising food by-product for valorization into gelatins, which have potential applications in food-, pharmaceutical- and cosmetic fields. The presented technology contributes not only to food sustainability but also to the model of a circular economy.
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To identify the antioxidative peptides in the gelatin hydrolysate of bovine skin, the gelatin was hydrolyzed with serial digestions in the order of Alcalase, pronase E, and collagenase using a three-step recycling membrane reactor. The second enzymatic hydrolysate (hydrolyzed with pronase E) was composed of peptides ranging from 1.5 to 4.5 kDa, and showed the highest antioxidative activity, as determined by the thiobarbituric acid method. Three different peptides were purified from the second hydrolysate using consecutive chromatographic methods. This included gel filtration on a Sephadex G-25 column, ion-exchange chromatography on a SP-Sephadex C-25 column, and high-performance liquid chromatography on an octadecylsilane chloride column. The isolated peptides were composed of 9 or 10 amino acid residues. They are: Gly-Glu-Hyp-Gly-Pro-Hyp-Gly-Ala-Hyp (PI), Gly-ProHyp-Gly-Pro-Hyp-Gly-Pro-Hyp-Gly (PII), and Gly-ProHyp-Gly-Pro-Hyp-Gly-Pro-Hyp (PIII), as characterized by Edman degradation and fast-atom bombardment mass spectrometry. The antioxidative activities of the purified peptides were measured using the thiobarbituric acid method, and the cell viability with a methylthiazol tetrazolium assay The results showed that PII had potent antioxidative activity on peroxidation of linoleic acid. Moreover, the cell viability of cultured liver cells was significantly enhanced by the addition of the peptide. These results suggest that the purified peptide, PII, from the gelatin hydrolysate of bovine skin is a natural antioxidant, which has potent antioxidative activity.
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Protein hydrolysates constitute an alternative to intact proteins and elemental formulas in the development of special formulations designed to provide nutritional support to patients with different needs. The production of extensive protein hydrolysates by sequential action of endopeptidases and exoproteases coupled with the development of post-hydrolysis procedures is considered the most effective way to obtain protein hydrolysates with defined characteristics. This paper reviews the development and use of protein hydrolysates for dietary treatment of patients with phenylketonuria, food allergy and chronic liver failure.
Collagen, gelatin and collagen hydrolysate were prepared from bovine limed split wastes by different preparative processes. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis showed that the molecular weight distribution of collagen was very narrow (about 200 and 100kDa for β and α chains respectively) compared with those of gelatin (less than 300kDa and wide distribution) and collagen hydrolysate (less than 50kDa and wide distribution). The isoelectric points of collagen, gelatin and collagen hydrolysate were 8.26, 4.88 and 4.54 respectively determined by Zeta potential titration. Circular dichroism (CD) spectra revealed that there were two peaks, a positive peak around 221nm and a negative peak around 192nm for collagen, which are the characteristics of collagen triple helix. However, gelatin and collagen hydrolysate lacked any positive peaks around 220nm, suggesting random coils. The denaturation temperature of collagen was about 37.5°C determined by the viscosity method, the helix-coil transitions for gelatin and collagen hydrolysate were not present in the heating process. Collagen reaggregated to fibrils at 35°C monitored at 313nm. In contrast, gelatin and collagen hydrolysate lost the ability of fibril formation. Collagen was more resistant to trypsin hydrolysis compared with gelatin and collagen hydrolysate. In addition, the collagen membrane exhibited superior features such as higher enthalpy, greater network structure and better physical/mechanical properties compared with those of the gelatin membrane. Therefore, collagen isolated from limed split wastes can be a high value product due to its special characteristics and has many potential future applications in biomaterials, functional additives, cosmetics and pharmaceutical industries.
Of all the hydrocolloids in use today, surely none has proven as popular with the general public and found favor in as wide a range of food products as gelatin. A sparkling, clear dessert jelly has become the archetypal gel and the clean melt‐in‐the‐mouth texture is a characteristic that has yet to be duplicated by any polysaccharide. Despite its apparently unfashionable status, more gelatin is sold to the food industry than any other gelling agent. It is relatively cheap to produce in quantity, and there is a ready supply of suitable raw material. The traditional sources of gelatin include bovine and pig skins and demineralized bones and hooves. However, recent studies have shown that there are viable new sources of gelatin such as marine fish skins and bones. Researchers have further sought to develop gelatin derivatives or modified gelatins like coldwater soluble gelatin, hydrolyzed gelatin and esterified gelatin.
Gelatin is regarded as a special and unique hydrocolloid, serving multiple functions with a wide range of applications. The main sources of gelatin include pigskin, cattle bones and cattle hide. Gelatin replacement has been a major issue in recent years due to the emerging and lucrative vegetarian, halal and kosher markets. It has recently gained increased interest, especially within Europe, with the emergence of bovine spongiform encephalopathy (BSE) in the 1980s. In this paper, we will discuss the unique properties of gelatin, the rationale for developing gelatin alternatives, the progress to date of research in development of gelatin alternatives, possible approaches for developing gelatin alternatives, and future directions for research in this area.
The porcine skin collagen was hydrolyzed by different protease treatments to obtain antioxidative peptides. The hydrolysate of collagen by cocktail mixture of protease bovine pancreas, protease Streptomyces and protease Bacillus spp. exhibited the highest antioxidant activities on 1,1-diphenyl-2-picrylhydrazyl (DPPH) radicals, metal chelating and in a linoleic acid peroxidation system induced by Fe2+. And degree of hydrolysis highly affected the antioxidant properties of the hydrolysates. Four different peptides showing strong antioxidant activity were isolated from the hydrolysate using consecutive chromatographic methods including gel filtration chromatography, ion-exchange chromatography and high-performance liquid chromatography. The molecular masses and amino acid sequences of the purified antioxidant peptides were determined using electrospray ionization (ESI) mass spectrometry. One of the antioxidative peptides, Gln-Gly-Ala-Arg, was then synthesized and the antioxidant activities measured using the aforementioned methods. The results confirmed the antioxidant activity of this peptide, and adds further support to its feasibility as a provider of natural antioxidants from porcine skin collagen protein.
Recent advances, principally through the study of peptide models, have led to an enhanced understanding of the structure and function of the collagen triple helix. In particular, the first crystal structure has clearly shown the highly ordered hydration network critical for stabilizing both the molecular conformation and the interactions between triple helices. The sequence dependent nature of the conformational features is also under active investigation by NMR and other techniques. The triple-helix motif has now been identified in proteins other than collagens, and it has been established as being important in many specific biological interactions as well as being a structural element. The nature of recognition and the degree of specificity for interactions involving triple helices may differ from globular proteins. Triple helix binding domains consist of linear sequences along the helix, making them amenable to characterization by simple model peptides. The application of structural techniques to such model peptides can serve to clarify the interactions involved in triple-helix recognition and binding and can help explain the varying impact of different structural alterations found in mutant collagens in diseased states.
Proteins are fundamental and integral food components, both nutritionally and functionally. Nutritionally, they are a source of energy and amino acids, which are essential for growth and maintenance. Functionally, they affect the physicochemical and sensory properties of various proteinaceous foods. In addition, many dietary proteins possess specific biological properties which make these components potential ingredients of functional or health-promoting foods. These proteins may also affect the technological functionality of the intended end-products. On the other hand, it is essential to apply or develop technologies which retain or even enhance the activity of bioactive components in food systems. This review article focuses on the effects of processing on the properties of bioactive proteins derived from various sources. A special emphasis is given to milk proteins as their physiological and technological functionality has been studied extensively.
Protein hydrolysates have been used for nutritional or technological purposes. Various methods are used for the quality control of these preparations. This paper reviews those used for the determination of the hydrolysis degree, the characterization according to the peptide size, the evaluation of the molecular weight distribution, and the estimation of the amino acid and peptide contents. The potential and limitations of different techniques are also described.
Food and pharmaceutical industries all over the world are witnessing an increasing demand for collagen and gelatin. Mammalian gelatins (porcine and bovine), being the most popular and widely used, are subject to major constraints and skepticism among consumers due to socio-cultural and health-related concerns. Fish gelatin (especially from warm-water fish) reportedly possesses similar characteristics to porcine gelatin and may thus be considered as an alternative to mammalian gelatin for use in food products. Production and utilization of fish gelatin not only satisfies the needs of consumers, but also serves as a means to utilize some of the byproducts of the fishing industry. This review focuses on the unique features, advantages, constraints, and challenges involved in the production and utilization of fish gelatin in order to provide a comprehensive look and deeper insight on this important food ingredient, as well as prospects for its future commercial exploitation and directions for future studies.