The study was carried out to evaluate the antioxidant activity and α-amylase activity inhibitory potential of Sarotherodon galillaeus muscle protein hydrolysates. Sarotherodon galillaeus muscle protein isolate was hydrolysed with three digestive proteases namely trypsin, chymotrypsin and pepsin. Degree of hydrolysis was determined. The antioxidative potential of the hydrolysates was investigated using DPPH radical scavenging, ferric reducing power, hydrogen peroxide scavenging and metal chelating activity. The ability of the hydrolysates to inhibit the activity of sugar-hydrolysing enzyme was also evaluated. Highest degree of hydrolysis was obtained with pepsin (55.86%) followed by trypsin (47.11%) and chymotrypsin (42.36%) after 6 hrs of hydrolysis. The half maximal inhibitory concentration (IC50) of hydrolysates produced by trypsin, chymotrypsin and pepsin for DPPH radical scavenging activity were 1.26 ± 0.95, 0.98 ± 0.07 and 1.18 ± 0.34 mg/ml respectively. Trypsin-produced hydrolysates displayed highest metal chelating activity and ferric reducing power while hydrolysates obtained with pepsin showed highest hydrogen peroxide scavenging activity. Amylase activity inhibitory potential of all the hydrolysates was low with pepsin-produced hydrolysates shown highest inhibitory effect of 18.46 ± 1.51%. The hydrolysates showed antioxidative potential that can be used in prevention of food oxidation.
Sarotherodon galillaeus, Hydrolysate, Amylase, Antioxidant, Degree of Hydrolysis
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