ArticlePDF Available

Abstract and Figures

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.
Content may be subject to copyright.
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.
7. References
[1] Baziwane D., He Q.: Gelatin: the paramount food additive. Food Rev. Int. 19,
423-435, (2003).
[2] Bella J., Brodsky B., Berman H.M.: Hydration structure of a collagen peptide.
Structure. 9, 893-906, (1995).
[3] Bello A.E., Oesser S.: Collagen hydrolysate for the treatment of osteoarthritis and other
joint disorders: a review of the literature. Cur. Med. Res. Opin. 22(11), 2221-2232, (2006).
[4] Bornstein P.: Covalent cross-links in collagen: a personal account of their
discovery. Matrix Biol. 22, 385-391, (2003).
[5] Brodsky B., Ramshaw J.A.M.: The collagen triple-helix structure. Matrix Biol.
15, 545-554, (1997) .
[6] Clemente A.: Enzymatic protein hydrolysates in human nutrition. Trends Food
Sci.Techn. 11, 254-262, (2000).
[7] Dioguardi F.S.: Nutrition and skin. Collagen integrity: a dominant role for amino
acids. Clin. Dermatol. 26, 636-640, (2008).
[8] Gelse K., Pöschl E., Aigner T.: Collagens-structure, function, and biosynthesis.
Adv. Drug Deliv. Rev. 55, 1531-1546, (2003).
[9] Giménez B., Alemán A., Montero P., mez-Guillén M.C.: Antioxidant and
functional propertioes of gelatin hydrolysates obtained from skin of sole and squid.
Food Chem. 114, 976-983, (2009).
[10] Hays N.P., Kim H., Wells A.M., Kajkenova O., Evans W.J.: Effects of whey and
fortified collagen hydrolysate protein supplements on nitrogen balance and body
composition in older women. J. Amer. Diet. Assoc. 109, 1082-1087, (2009).
[11] Karim A.A., Bhat R.: Gelatin alternatives for the food industry: recent developments,
challenges and prospects. Trends Food Sci. Techn. 19, 644-656, (2008).
[12] Karim A.A., Bhat R.: Fish gelatin: properties, challenges, and prospects as an
alternative to mammalian gelatins. Food Hydroc. 23, 563-576, (2009).
[13] Kim S.K., Kim Y.T., Byun H.G.: Purification and characterization of
antioxidative peptides from bovine skin. J. Bioch. Mol. Biol. 34, 219-224, (2001).
[14] Korhonen H., Pihlanto-Leppälä A., Rantamäki P., Tupasela T.: Impact of
processing on bioactive proteins and peptides. Trends Food Sci. Techn. 9, 307-319, (1998).
[15] Li B., Chen F., Wu Y., Wang X., Ji B.: Isolation and identification of
antioxidative peptides from porcine collagen hydrolysat by conescutive
xhromatography and electrospray ionization-mass spectrometry. Food Chem. 102,
1135-1143, (2007).
K. Dybka, P. Walczak 92
[16] Mendis N. Rajapakse N., Kim S.K.: Antioxidant properties of a radical-
scavening peptide purified from enzymatically prepared fish skin gelatin
hydrolysate. J. Agric. Food Chem. 53, 581-587, (2005).
[17] Minakowski W., Weidner S.: Biochemia krgowców. PWN. Warszawa 2005.
[18] Moskowitz R.W.: Role of collagen hydrolysate in bone and joint disease. Semin.
Arthritis Rheum. 30, 87-99, (2000).
[19] Myllyharju J., Kivirikko K.I.: Collagens, modifying enzymes and their
mutations in humans, flies and worms. Trends Genet. 20, 33-43, (2004).
[20] Oesser S., Seifert J., Adam M., Babel W.: Oral administration of
C labeled
collagen hydrolysate leads to an accumulation of a radioactivity in cartilage of
mice (C57/BL). J. Nutr. 129, 1891-1895, (1999).
[21] Pytrus-Sdłak B.: Kosmetyka ozdobna i pielgnacja twarzy. Medpharm Polska.
Wrocław 2007.
[22] Ricard-Blum S., Ruggiero F.: The collagen superfamily: from the extracellular
matrix to the cell membrane. Path. Biol. 53, 430-442, (2005).
[23] Silvestre M.P.C.: Review of methods for the analysis of protein hydrolysates.
Food Chem. 60, 263-271, (1997).
[24] widerski F., Czerwonka M., Waszkiewicz-Robak B.: Hydrolizat kolagenu
nowoczesny suplement diety. Przem. Spo. 4, 42-44, (2009).
[25] Wrzeniewska-Wal J.: Suplementy diety w nowej ustawie o bezpieczestwie
ywnoci. Przem. Spo. 6, 49-51, (2007).
[26] Zague V.: A new view concerning the effects of collagen hydrolysate intake on
skin properties. Arch. Derm. Res. 300, 479-483, (2008).
[27] Zhang Z., Li G., Shi B.: Physicochemical properties of collagen, gelatin and
collagen hydrolysate derived from bovine limed split wastes. J. Soc. Leath. Techn.
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
... 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. ...
Full-text available
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.
... [3], pig skin (46%), bovine hide (29.4%), and pork and cattle bones (23.1%) [4], which showed stronger application prospects. Collagen hydrolysates are mainly used as functional substances in the processing of beverages [5], meat products [6], and diet-supplement products [7], among others. Among them, deer-tendon collagen hydrolysates (DTCHs) exhibited a strong ability to improve osteoporosis by increasing the proliferative activities and extracellular matrix synthesis of MC3T3-E1 cells [8]. ...
Full-text available
Deer tendon, a deer processing byproduct, is an excellent protein source for the preparation of peptides for improving osteoporosis by its high protein content and high nutritional value. The optimal process of collagen acid extraction was implemented and the results showed that the acid concentration was 7%, the material–liquid ratio was 1:25, and the soaking time was 48 h. DTCHs could promote MC3T3-E1 cell proliferation and increase alkaline phosphatase activities in vitro. In addition, compared with the model group, the DTCHs treatment groups with an oral dosage of 350, 750, and 1500 mg/kg rat/day could significantly improve the shape, weight, bone mechanics, and alkaline phosphatase activities of tail-suspended mice. Bone microstructure and mineralization also recovered significantly in vivo. This result is expected to provide the structural and biological information for DTCHs-based functional foods.
... Collagen is a protein that has been used in multiple industrial applications, including the food industry, mainly in the meat industry, due to its biological compatibility and low allergenicity due to its ability to bind water [15]. Collagen and its fractions (gelatin) play an essential role in the human diet, having a considerable content of essential amino acids, which also prevent joint diseases [16]. Furthermore, these products constitute a source of animal protein due to the significant amounts of nutritional fibers [17,18]. ...
Full-text available
(1) Background: Phosphates are used in the food industry to improve water retention and product quality. However, when consumed in excess, they can be harmful to health. Instead, bovine skin gelatin hydrolysates present health benefits such as being a rejuvenating agent, stimulating collagen production, and improving food quality, in addition to being a source of protein. The effect of the addition of bovine skin gelatin hydrolysates on the texture and color of thermally processed chicken meat (boiled type) and antioxidant activity was evaluated. (2) Methods: Hydrolysates were prepared with subtilisin with the degree of hydrolysis being 6.57 and 13.14%, which were obtained from our previous study. (3) Results: The hydrolysates improved the firmness of the meat matrix compared to the control. Additionally, the hydrolysate with a 13.14% degree of hydrolysis reached the same firmness (p > 0.05) as the commercial ingredient sodium tripolyphosphate at its maximum limit allowed in the food industry when it was applied at 5% (w/w meat) in the meat matrix, improving firmness over the control by 63%. Furthermore, both hydrolysates reached a similar color difference to sodium tripolyphosphate at its maximum allowed limit when applied at a concentration of 2% (w/w meat). Additionally, it was found that these hydrolysates obtained the same antioxidant activity as sodium tripolyphosphate, capturing free radicals at 10%. (4) Conclusion: The findings of this study suggest that bovine skin gelatin hydrolysates can be applied as an ingredient with functional properties, being an alternative to phosphates to improve the quality of meat products.
... Незбалансовані та неповні дієти можуть бути причиною багатьох захворювань, що залежать від харчування. Якщо ми піклуємося про здоровий спосіб життя, то необхідно включати до звичайного раціону їжу, багату ессенціальними (незамінними) речовинами, мікро-та макронутрієнтами [2]. ...
Full-text available
Background. An important problem of modern society is to provide the population with food products that guarantee a higher standard of living and health. The field of HoReCa (hotel and restaurant business) does not sell enough healthy food products, therefore it is important to develop health-promoting food products. Among the wide range of food products, whipped dessert products are in great demand among consumers. The work is devoted to the development of formulation for aerated desserts, namely mousses of protective action, which have pronounced ergogenic properties that can increase efficiency, accelerate recovery, protect the body from stress. When developing the composition of mousses, we paid considerable attention to the study of the nutrient composition of the raw material, its changes during the technological processes of product development. The devepoled mousse formula includes the food additive collagen hydrolyzate the functional property of which is the renewal of intra-articular fluid and the construction of cartilage. Also, the collagen hydrolyzate promotes collagen production and can also be used to prevent the development of degenerative conditions of the musculoskeletal system. Objective. We aimed to design formulations for the production of protective mousses with the optimal ratio of basic nutrients and by supplementation with an additional component – collagen hydrolyzate – to increase the nutritional and biological value of finished products, as well as to expand the range of health food products, in particular aerated desserts. Methods. We optimized the mousses formulation taking into account the recommendations for the daily human need for the main macronutrients using mathematical modeling employing MS Excel. The qualitative and quantitative composition of microbiota during storage were analysed in accordance with DSTU 4503:2005 "Cheese products. General technical conditions". The organoleptic evaluation was performed using the sensory method on indicators according to DSTU 3718:2007 "Food concentrates. Sweet dishes, jellies, mousses, puddings, milk concentrates. General technical conditions". High-performance liquid chromatography was used to determine the micronutrient content. Results. We analysed such indicators of mousses as amino acid score and macronutrient content. The study of the amino acid composition showed that the consumption of 100 g of mousses "Cream-cheese" and "Strawberry" satisfies the daily human need in valine by 12.97% and 5.93% respectively. The developed products have a high content of all essential for the human body micronutrients, namely sulfur, calcium, phosphorus and potassium. We found that the shelf-life of mousses is 5 days at the temperature of 5 ± 1 °C in a glass container. Such microorganisms as bacteria of the Escherichia coli group, Staphylococcus aureus, Salmonella spp. were not detected during the entire shelf-life, that meets the requirements of regulatory documents and indicates the sanitary cleanliness and safety of the products. We have experimentally established the rational amount of collagen hydrolyzate food additive that is 3% by weight of the prescription composition of the product. Conclusions. We developed the mousse formulations comprised the supplement of a food additive of collagen hydrolyzate, which made it possible to obtain products balanced in biological value and with improved consumer properties, taking into account the norms for a person's daily need for basic macronutrients. We obtained products of high consumer quality and biological value by supplementation the recipe composition with a collagen hydrolyzate.
... 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. ...
Full-text available
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.
Biopolymers are natural polymers manufactured chemically or generated from biological materials. Biopolymers are a renewable and biodegradable resource. They can be found in various applications in food, manufacturing, packaging, and biomedical engineering industries. Biopolymers are attractive materials due to biocompatibility, biodegradability, natural abundance, and specific properties such as non-toxicity. Biopolymers can be classed on a variety of scales, including origin, the number of monomeric units, the basis of degradability, and heat response. Biopolymers have a wide range of uses due to their unique characteristics and topologies. Biopolymers are reinforced with diverse elements to improve their intended characteristics and practical applications. There is a conjugation of biopolymer with thermoplastic materials. Thermoplastic or thermoset plastic is a form of plastic polymer material that can be molded at a high temperature and solidifies upon cooling. Polylactic acid, polycarbonate, polyethylene, polypropylene, polyvinyl alcohol, and polyester are among the many thermoplastics. These thermoplastics were combined with biopolymers to increase their physical, mechanical, and thermal qualities. The works that investigated the conjugation of thermoplastic materials to biopolymers were discussed in this chapter.
Due to the increasing shortage of food protein in the world, the most effective and complete use of proteinaceous substrates is an urgent task. The most promising way to utilize secondary protein-containing raw materials is to increase its nutritional value through enzymatic hydrolysis. The use of protein hydrolysates obtained from protein-containing by-products has great potential in various areas of the food industry, as well as in the production of foods for medical and special dietary uses. The aim of the research was to propose optimal methods for processing protein substrates to obtain hydrolysates with desired properties, taking into account the characteristics of the main types of proteinaceous by-products and the specificity of proteases used. Material and methods. We used the data contained in PubMed, WoS, Scopus, and eLIBRARY.RU databases, which meet the requirements of scientific reliability and completeness. Results. Collagen-containing wastes from the meat, poultry and fish processing industries, whey, soy protein and gluten are the main types of protein-containing by-products successfully used to produce food and functional hydrolysates. The molecular structure, basic biological and physico-chemical properties of collagen, whey proteins, various protein fractions of wheat gluten and soy protein are described. The expediency of enzymatic treatment of protein-containing by-products using proteases is shown to reduce antigenicity and eliminate anti-nutritional properties, improve nutritional, functional, organoleptic and bioactive properties for subsequent use in food production, including those for medical and special dietary uses. Information is presented on the classification of proteolytic enzymes, their main properties, and the effectiveness of their use in the processing of various types of proteinaceous by-products. Conclusion. Based on the literature data analysis, the most promising methods for obtaining food protein hydrolysates from secondary protein-containing raw materials are proposed, including pretreatment of substrates and the selection of proteolytic enzymes with a certain specificity.
Full-text available
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.
Nutritional strategies to improve connective tissue collagen synthesis have garnered significant interest, although the scientific validity of these interventions lags behind their hype. This study was designed to determine the effects of three forms of collagen on N-terminal peptide of procollagen and serum amino acid levels. A total of 10 recreationally active males completed a randomized double-blinded crossover design study consuming either placebo or 15 g of vitamin C-enriched gelatin or hydrolyzed collagen (HC), or gummy containing equal parts of gelatin and HC. Supplements were consumed 1 hr before 6 min of jump rope. Blood samples were collected immediately prior to supplement consumption and 4 hr after jump rope. A subset of blood samples (n = 4) was collected for amino acid analysis 1 hr after ingestion. Consumption of an equivalent dose of each supplement increased amino acids in the circulation similarly across all interventions. N-terminal peptide of procollagen levels tended to increase ∼20% from baseline in the gelatin and HC interventions but not the placebo or gummy. These results suggest that vitamin C-enriched gelatin and HC supplementation may improve collagen synthesis when taken 1 hr prior to exercise. However, large variability was observed, which precluded significance for any treatment.
Full-text available
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.
Full-text available
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.