CHARACTERIZATION OF YELLOWFIN TUNA PEPSIN AND ITS APPLICATION FOR EXTRACTION COLLAGEN PEPTIDE FROM TILAPIA SKIN

Collagen peptides are small bioactive peptides obtained by enzymatically hydrolysis of collagen, in other words, the breaking down of the molecular bonds between individual collagen strands to peptides. Collagen peptides are highly bioavailable. They act as building blocks, renewing bodily tissues, such as skin, bones and joints. It has been proposed that collagen peptides may act as a messenger to the cells and trigger the synthesis and reorganization of new collagen fibers, thereby supporting our tissue structure. The objective of this study was to characterize yellowfin tuna pepsin and its application for extraction collagen peptide from tilapia skin. Enzyme pepsin was extracted from stomach of yellowfin tuna with phosphate buffer (pH 7.0) at 4 °C for 3 h then mixed with 2 M acetic acid at 1:1(w/v) for 30 minute. The characterization of crude enzyme was determined. The characterization of tuna pepsin was similarly to commercial porcine pepsin. pH optimum and stability of yellowfin tuna pepsin were 2 and 2-4, respectively. Temperature optimum and stability of yellowfin tuna pepsin were 50 °C and 10 - 30 °C, respectively. This enzyme respond to calcium chloride and copper sulfate. Yellowfin tuna (3.51±0.29 unit/ml) and porcine pepsin (3.52±1.09 unit/ml) were applied for collagen peptide extraction at 55 °C for 0, 1, 2 and 3 h. Degree of hydrolysis (%DH) of tuna pepsin was similarly to commercial porcine pepsin. Both enzyme completely extracted collagen peptide within 1 h. Collagen peptide shown antioxidant properties (DPPH, ABTS and FRAPS). Yellowfin tuna pepsin can apply in food supplement production as well to commercial porcine pepsin.