Computer-Aided Design to Improve the Thermal Stability of Rhizomucor miehei Lipase.

ABSTRACT: Lipase, a green biocatalyst, finds extensive application in the food sector. Enhancing the thermal stability of lipase presents both challenges and opportunities within the food industry. This research employed multiple rounds of cross-screening using tools like FoldX and I-Mutant 3.0 to strategically design mutations for Rhizomucor miehei lipase (RML), resulting in eight unique single-point mutation designs. E230I, N120M, and N264M have been confirmed experimentally to be potential combination mutation candidates. The resulting triple mutant N120M/E230I/N264M showed a higher thermal stability, with an optimum temperature of 55 °C, 10 °C higher than that of the wild-type RML. The half-life was extended from 46 to 462 min at 50 °C. Furthermore, the catalytic activity of N120M/E230I/N

SUBMITTER: Teng R 

PROVIDER: S-EPMC11727178 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature