|This article relies on references to primary sources. (December 2013)|
||This article possibly contains original research. (December 2013)|
Hydrolyzed collagen is a form of collagen. It is also called collagen hydrolysate, collagen peptide, gelatine, gelatine hydrolysate and hydrolyzed gelatine. Hydrolyzed collagen contains a different type of collagen depending upon its source. Hydrolyzed collagen derived from gelatin has primarily collagen type I and III while hydrolyzed collagen made from chicken sternal cartilage contains type II collagen and also coexisting glycosaminoglycans (GAGs) such as hyaluronic acid and chondroitin sulfate.
Hydrolyzed collagen is produced from collagen found in the bones, skin, and connective tissue of animals such as cattle, chicken, fish, horses, pigs, and rabbits. The process of hydrolysis involves breaking down the molecular bonds between individual collagen strands using heat and either acid or alkali solutions. Typically, with skin sourced collagen, hides are put in a lime slurry pit for up to 3 months, loosening collagen bonds; the hides are then washed to remove lime, and the collagen extracted in boiling water. The extracted collagen is evaporator concentrated, desiccated with drum driers, and pulverized.
There are different types of hydrolysis, some are done with either an acid solution (gelatin) or fruit enzymes process. In contrast, hydrolyzed collagen type II sourced from chicken sternal cartilage employs an enzymatic process to break down polypeptide chains to produce low molecular weight collagen type II peptides.
Amino acid content
The amino acid content of hydrolyzed collagen type I/III or type II is the same as that its collagen source. Hydrolyzed collagen contains both non-essential and essential amino acids, predominantly glycine, proline and hydroxyproline, which together represent around 50% of the total amino acid content, but lacks or contains very low levels of amino acids such as tryptophan and asparagine.
|Other essential amino acids||16%|
|Other non-essential amino acids||12%|
Glycine and proline concentration is as much as 20 times higher than other food sources of protein. Hydrolyzed collagen contains 8 out of 9 essential amino-acids, including glycine and arginine—two amino-acid precursors necessary for the biosynthesis of creatine. It contains no tryptophan and is deficient in isoleucine, threonine, and methionine.
The bioavailability of hydrolyzed collagen was demonstrated in a 1999 study; mice orally administered 14C hydrolyzed collagen digested and absorbed more than 90% within 6 hours, with measurable accumulation in cartilage and skin. A 2005 study found hydrolyzed collagen absorbed as small peptides in the blood.
A preclinical study investigated the effects of oral ingestion of hydrolyzed collagen, along with vitamin C and glucosamine, suggested that the moisture content of skin, its viscoelastic properties, and smoothness benefit.
A published study reports that the oral intake of hydrolyzed collagen type II (BioCell Collagen) reduces facial aging signs. A human study enrolling 26 female subjects demonstrated that BioCell Collagen was well tolerated with no serious adverse event and led to a significant reduction of skin dryness and wrinkles from baseline.  An increase in collagen and blood circulation was also observed. More studies are needed to confirm the observation.
The mechanism of action of ingested hydrolyzed collagen on skin may be the increased density of collagen fibrils and the fibroblasts' density (the fibroblasts being the main cells of the dermis, and those producing collagen). It may be that that the peptides of ingested hydrolyzed collagen have chemotactic properties on fibroblasts or an influence on growth of fibroblasts.
Joint & Bone Health
A published study reports that the oral intake of hydrolyzed collagen type II (BioCell Collagen) reduces joint discomfort. A randomized controlled trial (RCT) enrolling 80 subjects demonstrated that BioCell Collagen was well tolerated with no serious adverse event and led to a significant improvement of chronic joint discomfort. More studies need to be performed to confirm the observation.
Other clinical trials have yielded mixed results. Four studies reported benefit with no side effects; however, the studies were not extensive, and all recommended further controlled study. One study found that oral collagen only improved symptoms in a minority of patients and reported nausea as a side effect. Another study reported no improvement in disease activity in patients with rheumatoid arthritis. Another study found that collagen treatment may actually cause an exacerbation of rheumatoid arthritis symptoms.
Several studies have shown that a daily intake of hydrolyzed collagen increases bone mass density. It seems that hydrolyzed collagen peptides stimulated differentiation and osteoblasts activity- the cells that build bone- over that of osteoclasts (cells that destroy bone).
It has been claimed that hydrolyzed collagen may promote lean muscle mass through and the burning of fat rather than carbohydrates and proteins, toning and thickening skin, joint rebuilding, arterial strengthening, increased energy, organ rebuilding, alleviate osteoporosis, as well as lessening the symptoms of arthritis, high blood pressure, bladder weakness, chronic fatigue, shallow breathing, autoimmune, skin problems, and splitting nails.
Hydrolyzed collagen, like gelatin, is made from animal by-products, including skin, bones, and connective tissue. It is possible that consumption of hydrolyzed collagen risks contraction of Transmissible spongiform encephalopathy.
The U.S. Food and Drug Administration (FDA), with support from the TSE (Transmissible spongiform encephalopathy) Advisory Committee, has since 1997 been monitoring the potential risk of transmitting animal diseases, especially bovine spongiform encephalopathy (BSE). The FDA study concluded: "...steps such as heat, alkaline treatment, and filtration could be effective in reducing the level of contaminating TSE agents; however, scientific evidence is insufficient at this time to demonstrate that these treatments would effectively remove the BSE infectious agent if present in the source material."
In Cosmetics, hydrolyzed collagen may be found in topical creams, acting as a product texture conditioner, and moisturizer.
- "What is Hydrolyzed Collagen?". Rousselot. Retrieved 31 July 2009.
- Bensaid, A.; Tomé, D., L’Heureux-Bourdon, D., Even, P., Gietzen, D., Morens, C., Gaudichon, C., Larue-Achagiotis, C. and Fromentin, G. (2003). "A high-protein diet enhances satiety without conditioned taste aversion in the rat". Physiology and behavior 78 (2): 311–320. doi:10.1016/S0031-9384(02)00977-0. PMID 12576130.
- Fricke, O.; Baecker, N., Heer, M., Tutlewski, B. and Schoenau, E. (2008). "The effect of L-arginine administration on muscle force and power in postmenopausal women". Clinical physiology and functional imaging 28 (5): 307–311. doi:10.1111/j.1475-097X.2008.00809.x. PMID 18510549.
- Oesser, S.; Adam, M., Babel, W. and Seifert, J. (1999). "Oral administration of 14C labelled gelatine hydrolysate leads to an accumulation of radioactivity in cartilage of mice (C57/BL)". Journal of nutrition 129 (10): 1891–1895. PMID 10498764.
- Iwai, K.; Hasegawa, T., Taguchi, Y., Morimatsu, F., Sato, K., Nakamura, Y., Higashi, A., Kido, Y., Nakabo, Y. and Ohtsuki, K. (2005). "Identification of food-derived collagen peptides in human blood after oral ingestion of gelatine hydrolysates". Journal of Agricultural and Food Chemistry 53 (16): 6531–6536. doi:10.1021/jf050206p. PMID 16076145.
- Matsumoto, H.; Ohara, H., Ito, K., Nakamura, Y. and Takahashi, S. (2006). "Clinical effects of fish type I collagen hydrolysate on skin properties". ITE Letters 7 (4): 386–390.
- Schwartz, S. and Park, J. 2012. Ingestion of BioCell Collagen, a novel hydrolyzed chicken sternal cartilage extract; enhanced blood microcirculation and reduced facial aging signs. Clin. Interv. Aging. 7:267-73. doi: 10.2147/CIA.S32836. PMID 22956862.
- Matsuda, N.; Koyama, Y., Hosaka, Y., Ueda, H., Watanabe, T., Araya, T., Irie, S. and Takehana K. (2006). "Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis". Journal of nutrition vitaminology 52 (3): 211–215. doi:10.3177/jnsv.52.211.
- Postlethwaite, A.E.; Seyer, J.M. and Kang, A.H. (1978). "Chemotactic attraction of human fibroblasts to type I, II, and III collagens and collagen-derived peptides". Proc Natl Acad Sci USA 75 (2): 871–875. doi:10.1073/pnas.75.2.871. PMC 411359. PMID 204938.
- Shigemura, Y.; K Iwai, F Morimatsu, T Iwamoto, T Mori, C Oda, T Taira, EY Park, Y Nakamura and K Sato (2009). "Effect of prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin". Journal of Agricultural and Food Chemistry 57 (2): 444–449. doi:10.1021/jf802785h. PMID 19128041.
- Moskowitz, R. (2000). "Role of collagen hydrolysate in bone and joint disease". Seminars in arthritis and rheumatism 30 (2): 87–99. doi:10.1053/sarh.2000.9622. PMID 11071580.
- Ruiz-Benito, P.; Camacho-Zambrano, M.M., Carrillo-Arcentales, J.N., Mestanza-Peralta, M.A., Vallejo-Flores, C.A., Vargas-Lopez, S.V., Villacis-Tamayo, R.A. and Zurita-Gavilanes, L.A. (2009). "A randomized controlled trial on the efficacy and safety of a food ingredient, collagen hydrolysate, for improving joint comfort". International journal of food science and nutrition 12: 1–15.
- Schauss, A., Stenehjem, J., Park, J., Endres, J., and Clewell, A. 2012. Effect of the novel low molecular weight hydrolyzed chicken sternal cartilage extract, BioCell Collagen, on improving osteoarthritis-related symptoms: a randomized, double-blind, placebo-controlled trial. Journal of Agricultural and Food Chemistry 60(16):4096-101. PMID 22486722.
- Barnett ML, Kremer JM, St Clair EW, Clegg DO, Furst D, Weisman M, Fletcher MJ, Chasan-Taber S, Finger E, Morales A, Le CH, Trentham DE: Treatment of rheumatoid arthritis with oral type II collagen. Results of a multicenter, double-blind, placebo-controlled trial. Arthritis Rheum 1998 Feb;41(2):290-7.
- Ausar SF, Beltramo DM, Castagna LF, Quintana S, Silvera E, Kalayan G, Revigliono M, Landa CA, Bianco ID: Treatment of rheumatoid arthritis by oral administration of bovine tracheal type II collagen. Rheumatol Int. 2001 May;20(4):138-44.
- Trentham DE, Dynesius-Trentham RA, Orav EJ, Combitchi D, Lorenzo C, Sewell KL, Hafler DA, Weiner HL: Effects of oral administration of type II collagen on rheumatoid arthritis. Science 1993 Sep 24;261(5129):1727-30.
- Bagchi D, Misner B, Bagchi M, Kothari SC, Downs BW, Fafard RD, Preuss HG: Effects of orally administered undenatured type II collagen against arthritic inflammatory disease: a mechanistic exploration. Int J Clin Pharmacol Res. 2002;22(3-4):101-10.
- Sieper J, Kary S, Sorensen H, Alten R, Eggens U, Huge W, Hiepe F, Kuhne A, Listing J, Ulbrich N, Braun J, Zink A, Mitchison NA: Oral type II collagen treatment in early rheumatoid arthritis. A double-blind, placebo-controlled, randomized trial. Arthritis Rheum. 1996 Jan;39(1):41-51.
- McKown KM, Carbone LD, Kaplan SB, Aelion JA, Lohr KM, Cremer MA, Bustillo J, Gonzalez M, Kaeley G, Steere EL, Somes GW, Myers LK, Seyer JM, Kang AH, Postlethwaite AE: Lack of efficacy of oral bovine type II collagen added to existing therapy in rheumatoid arthritis. Arthritis Rheum. 1999 Jun;42(6):1304-8
- Cazzola M, Antivalle M, Sarzi-Puttini P, Dell’Acqua D, Panni B, Caruso I: Oral type II collagen in the treatment of rheumatoid arthritis. A six-month double blind placebo-controlled study. Clin Exp Rheumatol. 2000 Sep-Oct; 18(5):571-7.
- Oesser, S.; Seifert, J. (2003). "Stimulation of type II collagen biosynthesis and secretion in bovine chondrocytes cultured with degraded collagen". Cell tissue research 311 (3): 393–399. doi:10.1007/s00441-003-0702-8. PMID 12658447.
- Nomura, Y.; Oohashi, K., Watanabe, M. and Kasugai (2005). "Increase in bone mineral density through oral administration of shark gelatine to ovariectomized rats". S Nutrition 21 (11-12): 1120–1126. doi:10.1016/j.nut.2005.03.007. PMID 16308135.
- "What Is Hydrolyzed Collagen?". Livestrong.com Blog. Retrieved 8 June 2011.
- U.S. Food and Drug Administration. "The Sourcing and Processing of Gelatin to Reduce the Potential Risk Posed by Bovine Spongiform Encephalopathy (BSE) in FDA-Regulated Products for Human Use".