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Biochemical properties and antioxidant activity of myofibrillar protein hydrolysates obtained from patin (Pangasius sutchi)


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Antioxidant activities of myofibrillar protein hydrolysates (MPH) prepared from patin (Pangasius sutchi) using papain and Alcalase® 2.4 L with different degrees of hydrolysis (DH) were investigated. With a DH of 65.83%, the hydrolysate prepared with papain exhibited the maximum of 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging activity (71.14%) with a reducing power of 0.310. At a concentration of 1 mg mL−1, the papain-MPH exhibited a Trolox equivalent antioxidant capacity (TEAC) of 70.50 ± 1.22 μmol g−1 protein. With a DH of 83.6%, the Alcalase-MPH had the highest metal-chelating activity. Low molecular weight peptides showed higher antioxidant activities than high molecular weight peptides. Both papain-MPH and Alcalase-MPH contained high amounts of the essential amino acids (48.71% and 48.10%, respectively) with glutamic acid, aspartic acid and lysine as the dominant amino acids. These results suggest that the protein hydrolysates derived from patin may be used as an antioxidative ingredient in both functional food and nutraceutical applications.