Enzymatic treatments of collagen from barramundi (Lates Calcarifer) skin for production of bioactive peptides hydrolysates

Abstract

The utilization of barramundi skin, a by-product of the fish processing industry, as a prospective source of alternative collagen has been explored. To further broaden the prospect of barramundi collagen, its hydrolysate form (CH) was investigated using different enzymatic hydrolysis (alcalase and papain) at various concentration (1%, 2% and 3%). Degree of hydrolysis (DH) of the resulting hydrolysates were determined. The CH were then subjected to physico-chemical characterization including assessment of protein content, FTIR spectra, morphology, solubility and antioxidant properties. Among these, alcalase at a concentration of 1% exhibited notable efficacy, yielding a hydrolysate with DH of 56.5 %, 61.44% ABTS radical scavenging activity and 85% solubility across the pH range studied. Furthermore, both alcalase and papain-derived collagen hydrolysates demonstrated the capacity to disrupt the triple helix structure of crude collagen as observed through FTIR spectroscopy and scanning electron microscopy analysis. These results place collagen obtained from barramundi skin as a potential biotechnological alternative to produce highly potential bioactive peptide-containing hydrolysates.