Active Site Studies to Explain Kinetics of Lipases in Organic Solvents Using Molecular Dynamics Simulations.

ABSTRACT: This study investigates the intricate dynamics underlying lipase performance in organic solvents using comprehensive molecular dynamics (MD) simulations, supported by enzyme kinetics data. The study reveals that a single criterion can neither predict nor explain lipase activity in organic solvents, indicating the need for a comprehensive approach. Three lipases were included in this study: Candida antarctica lipase B (CALB), Rhizomucor miehei lipase (RML), and Thermomyces lanuginosus lipase (TLL). The lipases were investigated in acetonitrile, methyl tert-butyl ether, and hexane with increasing water activity. Computational investigations reveal that CALB's activity is negatively correlated to water cluster formations on its surface. In contrast, TLL's and RML's

SUBMITTER: Tjornelund HD 

PROVIDER: S-EPMC11726617 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature