Electrostatic interaction optimization improves catalytic rates and thermotolerance on xylanases.

ABSTRACT: Understanding the aspects that contribute to improving proteins' biochemical properties is of high relevance for protein engineering. Properties such as the catalytic rate, thermal stability, and thermal resistance are crucial for applying enzymes in the industry. Different interactions can influence those biochemical properties of an enzyme. Among them, the surface charge-charge interactions have been a target of particular attention. In this study, we employ the Tanford-Kirkwood solvent accessibility model using the Monte Carlo algorithm (TKSA-MC) to predict possible interactions that could improve stability and catalytic rate of a WT xylanase (XynA^WT) and its M6 xylanase (XynA^M6) mutant. The modeling prediction indicates that mutating from a lysine in position 99 t

SUBMITTER: de Godoi Contessoto V 

PROVIDER: S-EPMC8390807 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature