Thermostability mechanisms of β-agarase by analyzing its structure through molecular dynamics simulation.

ABSTRACT: Agarase is a natural catalyst with a good prospect in the industry. However, most of the currently discovered β-agarases are unsuitable for relatively high-temperature and high-pressure conditions required by industrial production. In this study, molecular dynamics simulations were first used to investigate the dynamic changes of folding and unfolding of mesophile and thermophile β-agarases (i.e., 1URX and 3WZ1) to explore the thermostability mechanism at three high temperatures (300 K, 400 K, and 500 K). Results showed that the sequence identity of 3WZ1 and 1URX reaches 48.8%. 1URX has a higher thermal sensitivity and less thermostability than 3WZ1 as more thermostable regions and hydrogen bonds exist in 3WZ1 compared with 1URX. The structures of 1URX and 3WZ1 become unstable with increas

SUBMITTER: Liu L 

PROVIDER: S-EPMC9076770 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature