Antioxidant activity of trypsin and pepsin-hydrolyzed fish collagen

Abstract

Collagen is a type of structural protein that constructs skin, teeth, bones, and muscles. Collagen hydrolysate is a product resulting from the hydrolysis of polypeptides that can be carried out enzymatically and chemically. This study aimed to obtain collagen hydrolysate using different enzymes and to determine its antioxidant content. The stages of the research carried out were characterization of collagen, hydrolysis of collagen with different enzymes, and characterization of collagen hydrolysate. The collagen used has a protein content of 95.75% considered as high protein content. The amino acid content of collagen was dominated by glutamic acid, which was 7.06%. Meanwhile, the pepsin-hydrolyzed collagen contained 7.81% of glutamic acid, and pepsin-hydrolyzed and trypsin-hydrolyzed collagen was 6.13% and 6.76%, respectively. TT the highest degree of hydrolysis was obtained from papain enzyme treatment 54.98%.