Effect of Bacterial Serine Protease Mutants on Antioxidant Properites of Enzymatic Hydrolyzed Fish Protein
Article
Figures
Metrics
Preview PDF
Reference
Related
Cited by
Materials
Abstract:
In this study, hydrolysis ability of bacterial serine protease and its mutants on silver carp protein was analyzed and antioxidant activities of protein hydrolysates were evaluated. Majority of the proteases in the hydrolysis reaction within the first 40 min was severe and the degree of hydrolysis increased rapidly. Then hydrolysis curves become flat or even decline from 40 min to 120 min. Bacterial serine protease mutant 239 showed the strongest hydrolysis ability on silver carp fish protein, which the maximum hydrolysis degree was 11.51% after 2 hours, whereas mutant 33 showed less degree of hydrolysis with only final 3.08%. The results showed that the bacterial serine protease and its mutant enzymes have high antioxidant activity. Protein hydrolysates of silver carp protein from mutant 166 have a strongest antioxidant activity by the DPPH scavenging was 91.02% with weak 61.41% DPPH scavenging ability for protease mutant 169. The resulted indicated that mutant in the domain related to active center will change the hydrolysis ability of protease. The mutant in substrate specificity domains will affect antioxidant activity of protein hydrolysates.
