Modification of the active centre of nattokinase to enhance its thermostability using a strategy based on molecular dynamics simulation, steered dynamics simulation, and conservative prediction.

ABSTRACT:

Introduction

The poor thermostability of nattokinase represents a significant limitation in its potential applications. Additionally, there is a notable absence of studies focused on modifying residues within the active site region of nattokinase with the aim of enhancing its catalytic properties. Furthermore, the direct utilisation of directed evolution often yields unfavourable outcomes, with a considerable workload being a common consequence.

Methods

In order to solve the above problems, a new method based on molecular dynamics simulation, steered dynamics simulation and conservative analysis with site-directed mutagenesis was proposed to screen nattokinase mutants with improved thermal stability. Molecular dynamics simulation was used to explain the mechanism of catalyti

SUBMITTER: Li Y 

PROVIDER: S-EPMC11602293 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature