Gama rays mediated improvement of catalytic efficiency and thermostability of glucoamylase by replacing active site leucine to isoleucene from super koji (Aspergillus oryzae).

ABSTRACT: Glucoamylase is considered as an essential enzyme in food industry. However, lowere catalytic efficiency and weak thermostability confine its application in food industry. Therefore, the current study was aimed to improve catalytic efficiency and thermostability of glucoamylase by replacing active site leucine to isoleucene from Super Koji (Aspergillus oryzae) using gama rays mediated point mutation. High catalytic efficiency and thermostability of glucoamylase from mutant Aspergillus oryzae M-60(5) (screened from 51 mutants) was achieved due to a point mutation, i.e., Leu203 → lle in active site. The SDS-PAGE molecular mass of parent and mutant glucoamylase was 63.1 kDa, while mutant glucoamylase showed; productivity =  9.7 U ml‒1, kinetic constants kcat = 118 (1.62 fold), (kcat/Km) = 189

SUBMITTER: Saqib A 

PROVIDER: S-EPMC12007714 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature