Enhancing catalytic efficiency of Bacillus subtilis laccase BsCotA through active site pocket design.

ABSTRACT: BsCotA laccase is a promising candidate for industrial application due to its excellent thermal stability. In this research, our objective was to enhance the catalytic efficiency of BsCotA by modifying the active site pocket. We utilized a strategy combining the diversity design of the active site pocket with molecular docking screening, which resulted in selecting five variants for characterization. All five variants proved functional, with four demonstrating improved turnover rates. The most effective variants exhibited a remarkable 7.7-fold increase in catalytic efficiency, evolved from 1.54 × 10⁵ M^-1 s^-1 to 1.18 × 10⁶ M^-1 s^-1, without any stability loss. To investigate the underlying molecular mechanisms, we conducted a

SUBMITTER: Hou Y 

PROVIDER: S-EPMC11377520 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature