Hydrolyzed collagen

Hydrolyzed collagen is usually made from type I collagen by an enzymatic hydrolysis process. It is also called collagen hydrolysate, collagen peptide, gelatine, gelatine hydrolysate and hydrolyzed gelatine.

Contents

Characteristics and production

Hydrolyzed collagen is produced from collagen found in the bones, skin, and connective tissue of animals such as cattle, pigs, horses, and fish. The process of hydrolysis involves breaking down the molecular bonds between individual collagen strands using heat and either acid or alkali solutions.

The hydrolysis process results in reducing the collagen proteins of about 300,000 Dalton (unit) (Da) into small peptides having an average molecular weight between 2000 and 5000 Da.

Amino acid content

The amino acid content of hydrolyzed collagen is the same as collagen. Hydrolyzed collagen contains 20 amino acids, predominantly glycine, proline and hydroxyproline, which together represent around 50% of the total amino acid content. Glycine and proline concentration is 10 to 20 times higher than in other food sources of protein.[1]

Amino acids Percentage
Proline/Hydroxyproline 25%
Glycine 20%
Glutamic acid 11%
Arginine 8%
Alanine 8%
Other essential amino acids 16%
Other non-essential amino acids 12%

Digestibility

The bioavailability of hydrolyzed collagen has been demonstrated by many studies. In a study of 1999, scientists demonstrated on mice that more than 90% of orally administered 14C labelled hydrolyzed collagen is digested and absorbed in 6 hours after ingestion. An important part is accumulated in cartilage and skin.[2] In another study of 2005, scientists showed that the hydrolyzed collagen is absorbed in small peptides in the blood.[3]

Skin Health

One preclinical study investigated the effects of oral ingestion of hydrolyzed collagen, along with vitamin C and glucosamine, on the skin properties of women tending to have dry and rough skin. This study suggested that, with the ingestion of 5g per day during 6 weeks, the moisture content of the skin, its viscoelastic properties and its smoothness improved.[4]

Regarding the mechanism of action of hydrolyzed collagen on skin, it seems that orally ingested hydrolyzed collagen increases the density of collagen fibrils and the fibroblasts density (the fibroblasts being the main cells of the dermis, and the ones which produce collagen).[5] The explanation of this action may be that the peptides of ingested hydrolyzed collagen have chemotactic properties on fibroblasts [6] or an influence on growth of fibroblasts.[7]

Joint & Bone Health

Some clinical studies report that the oral ingestion of 10g of hydrolyzed collagen by day decreases the joint pain, and that patients having the most severe symptoms benefited more.[8][9]

Other clinical trials have yielded mixed results. Four studies reported positive effects with no side effects. However, the studies were not extensive and all recommended the need for further controlled studies.[10][11][12][13]

Another study found that oral collagen only improved symptoms in a minority of patients and reported nausea as a side effect.[14] Another study reported no improvement in disease activity in patients with rheumatoid arthritis.[15] Yet another study found that collagen treatment may actually cause an exacerbation of rheumatoid arthritis symptoms.[16]

Any beneficial action is probably due to the fact that hydrolyzed collagen is accumulated in cartilage [2] and stimulates the production of collagen by the chondrocytes, the cells of cartilage.[17]

On bone health, several studies have shown that a daily intake of 10g of hydrolyzed collagen for 4 to 24 weeks increases bone mass density.[18][19] It seems that hydrolyzed collagen peptides stimulated the differentiation and the activity of osteoblasts, the cells that build the bone, instead of osteoclasts, those that destroy it.

Nutrition

Hydrolyzed collagen is a good protein to use in blends with others for a weight management diet. It contains 8 out of 9 essential amino-acids, and proteins are recognized as being the most satiating macronutrient.[20] Hydrolyzed collagen is also a good ingredient for a sportive diet[citation needed]. It is important for athletes to restore their protein content after an exercise, and the consumption of hydrolyzed collagen that contains more than 97% of protein can help it.[citation needed] Hydrolyzed collagen also contains some glycine and arginine, two of the three amino-acids of the creatine, a molecule which present in the body and having an important play during the exercise, providing energy to the body. Finally, hydrolyzed collagen contains some arginine, which has been shown to be efficient to improve the athletic performance.[19]

Cosmetics

Hydrolyzed collagen is used not only in health and nutrition but also in nutraceuticals and cosmetics. > In Cosmetics, hydrolyzed collagen will be formulated into topical cream or facial masks. In both cases, while playing a texturizing role in the finished product, it will help moisturize and firm the skin. These products will be mainly found in North America and Asia. In Europe, hydrolyzed collagen will be used in more complex formula, mainly targeting the treatment of age signs, such as wrinkles or skin’s loss of elasticity.

Hydrolyzed collagen is claimed by some to protect and even help in achieving gains in lean muscle mass, to help improve the symptoms of arthritis, and to promote weight loss through the burning of fat rather than carbohydrates and proteins. Other potential benefits of hydrolyzed collagen include improvements in skin toning and thickening, joint rebuilding, arterial strengthening, increased energy and organ rebuilding. Some suggest that hydrolyzed collagen may resolve chronic problems such as osteoporosis, high blood pressure, arthritis in joints, bladder weakness, chronic fatigue, shallow breathing, autoimmune and skin problems and splitting nails.[21]

Safety concerns

Hydrolyzed collagen, like gelatin, is made from by-products of beef, pork, and fish production, including the skin, bones, and connective tissue. There have been concerns that human consumption of hydrolyzed collagen may expose the consumer to a risk of TSE (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."[22]

Uses

When submitted to strict quality controls and sensorial panels,[23] Hydrolyzed collagen may have excellent organoleptic properties[citation needed], and be taste and odor-free. Due to those properties, it is easy to use in foods and beverages, as well as in powder blends or dietary supplements. Many functional products are already available, especially in Japan. Regarding the cosmetics, hydrolyzed collagen occurs in many products: shampoos, conditioners, soaps, face cares, or even in make-up.

References

  1. ^ "What is Hydrolyzed Collagen?". Rousselot. http://www.rousselot-rhc.com/what-is-peptan.html. Retrieved 31 July 2009. 
  2. ^ a b 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. 
  3. ^ 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 agriculture and food chemistry 53 (16): 6531–6536. doi:10.1021/jf050206p. PMID 16076145. 
  4. ^ 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. 
  5. ^ 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. 
  6. ^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=411359. 
  7. ^ 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". J Agric Food Chem 57 (2): 444–449. doi:10.1021/jf802785h. PMID 19128041. 
  8. ^ 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. 
  9. ^ 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. 
  10. ^ 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.
  11. ^ 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.
  12. ^ 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.
  13. ^ 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.
  14. ^ 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.
  15. ^ 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
  16. ^ 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.
  17. ^ 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. 
  18. ^ 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. 
  19. ^ a b Wu, J.; Fujioka, M., Sugimoto, K., Mu, G. and Ishimi, Y (2004). "Increase of effectiveness of oral administration of collagen peptide on bone metabolism in growing and mature rats". Bone and mineral metabolism 22 (6): 547–553. doi:10.1007/s00774-004-0522-2. PMID 15490264. 
  20. ^ 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. 
  21. ^ "What Is Hydrolyzed Collagen?". Livestrong.com Blog. http://www.livestrong.com/article/77943-hydrolyzed-collagen/. Retrieved 8 June 2011. 
  22. ^ 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". http://www.fda.gov/RegulatoryInformation/Guidances/ucm125182.htm. 
  23. ^ "Quality Controls". Rousselot. http://www.rousselot-rhc.com/technical-and-quality-datas.html. Retrieved 31 July 2009. 

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