Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally ( Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type

Abstract

Antioxidative activity and functional properties of protein hydrolysates from yellow stripe trevally ( Selaroides leptolepis) meat, hydrolyzed by Alcalase 2.4L (HA) and Flavourzyme 500L (HF) with different degrees of hydrolysis (DH) were investigated. As the DH increased, DPPH radical-scavenging activity and reducing power of HA decreased ( p < 0.05) but no differences were observed for HF ( p > 0.05). Metal chelating activity of both HA and HF increased with increasing DH ( p < 0.05). HF generally had a higher ( p < 0.05) chelating activity than had HA at the same DH tested. At low DH (5%), HA exhibited a better DPPH radical-scavenging activity while, at high DH (25%), HF had a higher ( p < 0.05) reducing power. For the functional properties, hydrolysis by both enzymes increased protein solubility to above 85% over a wide pH range (2–12). When the DH increased, the interfacial activities (emulsion activity index, emulsion stability index, foaming capacity, foam stability) of hydrolysates decreased ( p < 0.05), possibly caused by the shorter peptide chain length. At the same DH, the functionalities of protein hydrolysate depended on the enzyme used. The results reveal that antioxidative activity and functionalities of protein hydrolysates from yellow stripe trevally meat were determined by the DH and by the enzyme type employed.