Hydrolysed bovine collagen, also known as collagen peptides, is a form of collagen broken down into smaller, easily digestible particles. It is derived from bovine sources, particularly skin, bone and muscle. It is commonly used as a dietary supplement to support healthy skin, bones and joints.

The name 'hydrolysed bovine collagen' describes the source and process used to obtain this product:

• Hydrolysed refers to the process of hydrolysis, a chemical reaction in which a compound is broken down by water. In the case of collagen, hydrolysis breaks down the large, complex collagen proteins into smaller peptides that are easier for the body to absorb and utilise.
• Bovine indicates that the collagen comes from animals belonging to the family Bovidae..
• collagen is the main structural protein of the body's various connective tissues.

The production process of hydrolysed bovine collagen involves different steps:

• Extraction: raw bovine materials (such as hides or bones) are first cleaned, treated with a disinfectant solution and then soaked in water to loosen and remove any attached tissue.
• Hydrolysis: the cleaned materials are then subjected to hydrolysis, using an acid or alkaline solution, to break down the collagen proteins into smaller peptides. This process can last from a few hours to a few days.
• Purification: the hydrolysed collagen solution is then filtered to remove any solids and impurities. It may also undergo further treatment to remove any unwanted tastes or odours.
• Drying: the purified collagen solution is dried to remove residual water, usually through a process such as spray or drum drying.
• Grinding: the dried collagen is ground into a fine powder to obtain the desired particle size.
• Packaging: the final powder of hydrolysed bovine collagen is packaged for distribution and use.

It is worth noting that the quality of the final product may vary depending on factors such as the quality of the raw materials used, the specific hydrolysis process employed and the conditions under which the product is dried and ground.

Medical

This study found that collagen peptides induce the proliferation of fibroblasts and keratinocytes and the expression of pro-collagen-1α, factors beneficial to skin health. The study also found that collagen peptides reduce inflammation induced by lipopolysaccharide (LPS), a component of the cell walls of gram-negative bacteria. (1).

This study evaluated the potential of a thermophilic thermolysis-like protease (TLP), A69, in the preparation of bioactive collagen peptides from bovine bone. The study found that the prepared collagen peptides had good moisture-holding capacity and antioxidant activity, suggesting potential applications in the cosmetic, food and pharmaceutical industries. (2).

References_____________________________________________________________________

(1) Brandao-Rangel, M. A. R., Oliveira, C. R., da Silva Olímpio, F. R., Aimbire, F., Mateus-Silva, J. R., Chaluppe, F. A., & Vieira, R. P. (2022). Hydrolyzed Collagen Induces an Anti-Inflammatory Response That Induces Proliferation of Skin Fibroblast and Keratinocytes. Nutrients, 14(23), 4975.

Abstract. Collagen-based products are found in different pharmaceuticals, medicine, food, and cosmetics products for a wide variety of applications. However, its use to prevent or improve the health of skin is growing dizzyingly. Therefore, this study investigated whether collagen peptides could induce fibroblast and keratinocyte proliferation and activation beyond reducing an inflammatory response induced by lipopolysaccharide (LPS). Human skin fibroblasts (CCD-1072Sk) and human keratinocytes (hKT-nh-skp-KT0026) were seeded at a concentration of 5 × 104 cells/mL. LPS (10 ng/mL) and three doses of collagen peptides (2.5 mg/mL, 5 mg/mL, 10 mg/mL) were used. The readout parameters were cell proliferation; expression of inducible nitric oxide synthase (iNOS); expression of pro-collagen-1α by fibroblasts; and secretion of interleukin-1β (IL-1β), interleukin-6 (IL-6), interleukin-8 (IL-8), tumor necrosis factor α (TNF-α), transforming growth factor β (TGF-β), and vascular endothelial growth factor (VEGF) by both cell types. The results demonstrated that all doses of collagen supplementation induced increased proliferation of both human fibroblasts (p < 0.01) and human keratinocytes (p < 0.001), while only the dose of 10 mg/mL induced an increased expression of pro-collagen-1α by fibroblasts. Similarly, only the dose of 10 mg/mL reduced LPS-induced iNOS expression in fibroblasts (p < 0.05) and keratinocytes (p < 0.01). In addition, collagen supplementation reduced the LPS-induced IL-1β (p < 0.05), IL-6 (p < 0.001), IL-8 (p < 0.01), and TNF-α (p < 0.05), and increased the TGF-β and VEGF expression in fibroblasts. Furthermore, collagen supplementation reduced the LPS-induced IL-1β (p < 0.01), IL-6 (p < 0.01), IL-8 (p < 0.01), and TNF-α (p < 0.001), and increased the TGF-β (p < 0.05) and VEGF (p < 0.05) expression in keratinocytes. In conclusion, collagen peptides were found to induce fibroblast and keratinocyte proliferation and pro-collagen-1α expression, involving increased expression of TGF-β and VEGF, as well as the suppression of an inflammatory response induced by LPS.

(2) Cheng, J. H., Zhang, X. Y., Wang, Z., Zhang, X., Liu, S. C., Song, X. Y., ... & Xu, F. (2021). Potential of thermolysin-like protease A69 in preparation of bovine collagen peptides with moisture-retention ability and antioxidative activity. Marine Drugs, 19(12), 676.

Abstract. Bovine bone is rich in collagen and is a good material for collagen peptide preparation. Although thermolysin-like proteases (TLPs) have been applied in different fields, the potential of TLPs in preparing bioactive collagen peptides has rarely been evaluated. Here, we characterized a thermophilic TLP, A69, from a hydrothermal bacterium Anoxybacillus caldiproteolyticus 1A02591, and evaluated its potential in preparing bioactive collagen peptides. A69 showed the highest activity at 60 °C and pH 7.0. We optimized the conditions for bovine bone collagen hydrolysis and set up a process with high hydrolysis efficiency (99.4%) to prepare bovine bone collagen peptides, in which bovine bone collagen was hydrolyzed at 60 °C for 2 h with an enzyme–substrate ratio of 25 U/g. The hydrolysate contained 96.5% peptides that have a broad molecular weight distribution below 10000 Da. The hydrolysate showed good moisture-retention ability and a high hydroxyl radical (•OH) scavenging ratio of 73.2%, suggesting that the prepared collagen peptides have good antioxidative activity. Altogether, these results indicate that the thermophilic TLP A69 has promising potential in the preparation of bioactive collagen peptides, which may have potentials in cosmetics, food and pharmaceutical industries. This study lays a foundation for the high-valued utilization of bovine bone collagen.