Isolation of elastin and collagen polypeptides from long cattle tendons as raw material for the cosmetic industry.

Long cattle tendons were enzymatically disposed of lipoid and accompanying nitrogenous substances. Collagenous hydrolysate of average molecular mass M(a) = 0.830 +/- 1.206 kDa, suitable for application in skin and hair-care preparations, was obtained through hydrolysis by commercial protease (Bacillus subtilis) under mild conditions. Elastin, hydrolysable with greater difficulty, was subsequently hydrolysed by commercial endopeptidase (Bacillus licheniformis), under more drastic conditions, to a product of average molecular mass M(a) = 0.448 +/- 1.514 kDa. Purity of both hydrolysates was assessed by hydroxyproline and amide nitrogen contents. Aminosaccharides and glycosamino glycans in hydrolysates were not detected.