Abstract
An aminopeptidase that derived from Streptomyces canus T20 (ScAP) was successfully expressed and characterized in Escherichia coli BL21 (DE3) for first time. The specific activity was 6000 U/mg, which is highest in Streptomyces aminopeptidases. Its optimal conditions were 60 °C and pH 8.0, respectively. ScAP exhibited excellent thermal and alkaline pH stability, retained 80.0% maximal activity at 50 °C for 200 h or at pH 9.0 for 24 h. Its activity observed to be complete inhibited by 0.1 mM EDTA and enhanced by Ca2+ and Co2+ to 115.4% and 104.0% respectively. ScAP also has exhibited high specificity towards rice protein on preparation of small peptides. The yield of small rice peptides achieved 66.5%, which is highest by far. Besides, ScAP have significant debittering effect on rice peptides. Results showed that bitter intensity score decreased by 49.0% with optimum condition (0.048% ScAP at 50 °C for 6 h). Therefore, ScAP as dual functional aminopeptidase of hydrolytic and debittering might have a potential application in the production of high yield and low bitterness of small rice peptides.
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