ISOLATION AND CHARACTERIZATION OF COLLAGEN FROM SALMON (Salmo salar) SKIN USING PAPAIN ENZYME

Abstract

Salmon skin is a fish byproduct that is rich in collagen. There are several methods to extract collagen from the skin, one of which involves combining chemical (acid) and enzymatic (protease) processes. Papain soluble collagen (PaSC) refers to the collagen that is obtained through the use of papain. This collagen can be classified as halal. The objective of this study was to ascertain the optimal duration and concentration for extracting collagen from salmon skin, taking into account both the yield of collagen and its chemical properties. The skin was obtained by treating it with a mixture of acetic acid (0.5 M) and papain enzyme (500, 1,000, and 1,500 U/mg/g skin) for 1, 2, and 3 hours. The parameters examined encompassed heavy metal content, collagen yield, amino acid composition, functional group analysis, and molecular weight determination. The maximum collagen solubility was achieved by combining acetic acid at a concentration of 0.5 M with papain enzyme at a concentration of 1,000 U/mg/g skin for a duration of 2 hours. The percentage of PaSC extracted from salmon skin was 15.38% (dry basis). The dominant amino acids in PaSC were proline, glycine, and arginine. The molecular weight distribution range of the collagen was approximately 20–142 kDa. According to the FTIR spectrum, the PaSC extraction did not alter the triple helix structure.