FISHERIES RESEARCH INSTITUTE,MOA,TAIWAN

The objectives of this research was to study the functional activity peptides from neritic squid (Loligo edulis) sarcoplasmic protein hydrolysate. The neritic squid sarcoplasmic protein was hydrolyzed with papain, bromelin, protease Type XIV, protease Type XXIII at 37 oC for 0, 6, 12, 18, 24 hr and companied with the control group. The antioxidative activities of protein hydrolysates were measured by four methods inculding the Trolox equivalent antioxidant capacity, scavenging effect of DPPH (α, α-diphanyl-β-picrylhydrazyl) radical, reducing power and chelating Cu2+ effect. The hydrolysate obtained by treating with 0.02% protease Type XIV for 18 hr, showed the better Trolox equivalent antioxidant capacity (value = 1.14 ± 0.01mM) than others . As treating with 0.02% papain for 12 hr, the scavenging effect of DPPH radical and reducing power reached the higher value, 80.78 ± 0.69% and 0.27 ± 0.01 respectively, than others conditions. The highest values of chelating Cu2+ effect, 12.76 ± 0.81% was obtained by treating with 0.02% protease Type XIV for 12 hr.