Functional expression and characterization of a novel aminopeptidase B from Aspergillus niger in Pichia pastoris.

ABSTRACT: A novel aminopeptidase B (APB-AN) was identified from Aspergillus niger CGMCC 3.1454 for the first time and was cloned and expressed in Pichia pastoris. The mature enzyme of approximately 100 kDa was purified for characterization. The optimum pH and temperature of the recombinant APB-AN were determined to be 7.0 and 40 °C, respectively. The enzyme was stable below 40 °C and at pH values from 5.0 to 8.0. The K _m and V _max values were determined to be 0.61 mmol/L and 11.45 mmol/L/min, respectively, using Arg-pNA as the substrate. APB-AN was inhibited by Cu²⁺ and Fe²⁺ and activated by Co²⁺ and Na⁺. Most metal chelators (Ca²⁺, Mg²⁺ and Mn²⁺) and aminopeptidase i

SUBMITTER: Song P 

PROVIDER: S-EPMC8257800 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature