Improving the catalytic thermostability of Bacillus altitudinis W3 ω-transaminase by proline substitutions.

ABSTRACT: As a green biocatalyst, transaminase with high thermostability can be better employed to synthesize many pharmaceutical intermediates in industry. To improve the thermostability of (R)-selective amine transaminase from Bacillus altitudinis W3, related mutation sites were determined by multiple amino acid sequence alignment between wild-type ω-transaminase and four potential thermophilic ω-transaminases, followed by replacement of the related amino acid residues with proline by site-directed mutagenesis. Three stabilized mutants (D192P, T237P, and D192P/T237P) showing the highest stability were obtained and used for further analysis. Comparison with the wild-type enzyme revealed that the double mutant D192P/T237P exhibited the largest shift in thermostability, with a 2.5-fold

SUBMITTER: Xie Z 

PROVIDER: S-EPMC7324462 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature