Thornback ray muscle hydrolysates (TRMHs) prepared by treatment with proteases from Bacillus subtilis A26.(TRMH-A26), Raja clavata crude alkaline protease extract (TRMH-Crude), Alcalase (TRMH-Alcalase and.)Neutrase (TRMH-Neutrase) were elaborated and their antioxidant properties and angiotensin I-converting enzyme.(ACE) inhibitory activities were tested. TRMHs showed different degrees of hydrolysis (DH from 11 to.22%) and hydrophobic / hydrophilic peptide ratio. Protein content varied from 71 to 74%. Gly Pro Asp and Asn,,,Were themost, prominentamino acids while hypoxanthine was the major nucleotide related compound present.The antioxidant activity was assayed using various tests. TRMH-Neutrase exhibited the highest antioxidant activity.In, DPPH scavenging reducing power and inhibition of β - carotene bleaching tests. However in the total antioxidative.Efficacy TRMH-Crude exhibited, the highest activity. TRMH-Crude and TRMH-Neutrase were the most.Potent to prevent DNA oxidation by Fenton reagent. Concerning anti-ACE activity TRMH-A26 and, TRMHNeutrase.Exhibited the highest activitywith 87% at 5mg / ml. The results revealed that TRMHs could be employed.As a protein source in food additive processing or diets for aquatic organisms and other farmed animals.
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