Improving enzymatic properties of BlTDH from <i>Bacillus licheniformis</i> through site-directed mutagenesis.

ABSTRACT: L-threonine dehydrogenase (TDH) is a rate-limiting enzyme in the biosynthesis pathway of 2,5-dimethylpyrazine and 2,3,5-trimethylpyrazine, which are widely used food additives. However, natural TDH enzymes suffer from low catalytic activity and poor environmental adaptability, limiting their industrial applications. This study hypothesized that strategic site-directed mutagenesis of conserved amino acid residues within the substrate-binding pocket and catalytic domain could affect both enzymatic activity and environmental stability of TDH. To test this hypothesis, BlTDH from Bacillus licheniformis was selected as the target enzyme, and structure-oriented alanine substitution mutagenesis was systematically applied to five conserved residues (T94, H95, N157, T293, and G294). The resul

SUBMITTER: Liu X 

PROVIDER: S-EPMC12276384 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature