Enhancing Cold Adaptation of Bidomain Amylases by High-Throughput Computational Engineering.

ABSTRACT: Cold-adapted bidomain enzymes have the potential to foster industrial sustainability by reducing energy consumption and greenhouse gas emissions. Despite their allure, these benefits are unattainable, as the molecular basis of cold adaptation remains elusive, and there are no strategies to guide the acquisition of this behavior. To uncover principles of cold adaptation, we selected the cold-adapted Saccharophagus degradans amylase (sdA) and mesophilic Pseudomonas saccharophila amylase (psA) as model systems. Through molecular dynamics (MD) simulations and biochemical assays, we found that sdA exhibits significantly greater interdomain separation between its catalytic domain (CD) and carbohydrate-binding module (CBM) at low temperatures. Therefore, we introduce the domain separation index m

SUBMITTER: Ding N 

PROVIDER: S-EPMC12258674 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature