Computational design of α-amylase from Bacillus licheniformis to increase its activity and stability at high temperatures.

ABSTRACT: The thermostable α-amylase derived from Bacillus licheniformis (BLA) has multiple advantages, including enhancing the mass transfer rate and by reducing microbial contamination in starch hydrolysis. Nonetheless, the application of BLA is constrained by the accessibility and stability of enzymes capable of achieving high conversion rates at elevated temperatures. Moreover, the thermotolerance of BLA requires further enhancement. Here, we developed a computational strategy for constructing small and smart mutant libraries to identify variants with enhanced thermostability. Initially, molecular dynamics (MD) simulations were employed to identify the regions with high flexibility. Subsequently, FoldX, a computational design predictor, was used to design mutants by rigidifying highly fle

SUBMITTER: Fan S 

PROVIDER: S-EPMC10883975 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature