Abstract
The sarcoplasmic protein was extracted from the muscle of grass carp, a Chinese freshwater carp, and was hydrolyzed with five proteases to produce antioxidant peptides. Papain hydrolysate was found to have the greatest activity against lipid peroxidation. Response surface methodology (RSM) was applied to optimize the hydrolysis conditions (including enzyme to substrate ratio, time and temperature). The minimum EC 50 value (317.25 μg/mL) which signified the maximum antioxidant activity was obtained at an enzyme to substrate ratio of 0.79%, an incubation time of 5.69 h and an incubation temperature of 52.15 °C, which was in agreement with the predicted value (313.99 μg/mL) estimated by RSM within a 95% confidence interval. Also, it was found that moderate denaturation of the sarcoplasmic protein and a modest increase in the degree of hydrolysis promoted the antioxidant activities of the hydrolysates. Oligopeptides (< 3 kDa) contributed more to the antioxidant activity than polypeptides.
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