Enhancement in the Catalytic Properties of CotA Laccase from Bacillus pumilus via High-Throughput Screening Using Malachite Green as a Pressure.

ABSTRACT: Bacterial laccase exhibits substantial application potential in various fields. In this study, we constructed a mutation library of CotA laccase from Bacillus pumilus using error-prone PCR, and we performed four rounds of enrichment screening under malachite green (MG) pressure. The results demonstrated that the proportions of the four selected mutant strains were significantly increased. The enzyme activities of the four final mutants PW2, PW5, PW4G, and PW6 were 94.34, 75.74, 100.66, and 87.04 U/mg, respectively, representing a significant increase of approximately 2- to 3-fold compared to the wild-type CotA laccase. Notably, PW4 exhibited significantly improved thermal stability at 90 °C and pH tolerance at pH 12.0. Homology modeling analysis revealed that alterations in the amin

SUBMITTER: Li X 

PROVIDER: S-EPMC11858407 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature