What are collagen peptides?
What are collagens?
Collagen accounts for 25–35% of all vertebrate body proteins. Collagen is vital to maintain the healthy structure and strength of connective tissue, such as skin, blood vessels, cartilage, and bones. Collagens interact with cells via several receptor families and control their proliferation, differentiation, and migration. It is formed by the three primary amino acid glycine (GLY) (33%), proline (PRO), and hydroxyproline (HYP) (22%) in three separate polypeptide chain that winds around each other to produce a triplex helix. Therefore, collagen is shaped into long bars and packaged into tight fibers to do its job of build-up cartilage, bone, and skin to maintain body form. The helical region of collagen comprises the repeat of GLY–X–Y, where PRO can be in the X or Y position, and HYP occurs only in the Y position. Therefore, GLY-PRO–Y, GLY–X–HYP, and GLY–PRO–HYP are essential for the stabilization of the collagen structure. HYP is a derivative formed by hydroxylation of the amino acid PRO which requires vitamin C as a co-factor. Vitamin C deficiency decreases the conversion of PRO to HYP, which leads to reduced collagen stability. Thus HYP is a significant component of the protein collagen and plays a crucial role in the balance of the collagen triple helix and its use as a criterion to determine the amount of collagen. The collagen family comprises 29 types that have been identified. MaxGrainta chooses collagen type I from the freshwater fish skin of Tilapia (Oreophromis spp) Japan. Collagen type I is the most abundant found in skin, bone, teeth, tendon, vascular ligature, ligaments, and organs. The three main reasons we choose to use collagen from freshwater Tilapia as raw materials instead of collagen from cows and pigs are; first, cows are carriers of mad cow disease, and swine is a carrier of swine flu. The second reason is for people who are allergic to seafood, and the third reason is religion.
What are collagen peptides?
Heat-denatured collagen forms a substance called soluble gelatin. Enzymatic hydrolysate at a specific incubation temperature of gelatin is more soluble than gelatin. Then it is called to as collagen hydrolysate or collagen peptide. Collagen peptides are a bioavailable form of collagens. Enzymatic hydrolysis treatment breaks the bonds in the polypeptide chain to get a large number of peptides. The molecular weight of collagen peptides earned from hydrolysis is small (0.3–8 KDa) compared to that of its native collagen (285–300 KDa). This treatment affects not only the size of the peptides but also physicochemical and biological properties. The lower molecular weight shows very low viscosity, highly soluble in water, and allows collagen peptides to be readily digestible and easily absorbed in the digestive tract. Due to the rich content of specific amino acids and critical di-peptides of hydroxyproline-proline and hydroxyproline-glycine to enhance skin, joint, and bone health. These typical features, coupled with the unique GLY-X-Y motif, confer collagen peptides with all-around functionalities and applications as food supplements and ingredients in the form of powders and drinks.