Structure-Based Engineering to Improve Thermostability of <i>At</i>Bgl1A β‑Glucosidase.

ABSTRACT: β-Glucosidases are essential enzymes in cellulose degradation and hold significant promise for industrial applications, particularly in biorefinery processes. This study focused on the structural and functional characterization of AtBgl1A, a glycoside hydrolase family 1 β-glucosidase from , and its rational engineering to enhance thermostability. AtBgl1A exhibited over 400-fold higher specificity for laminaribiose than cellobiose, supporting its physiological role in laminaribiose metabolism. The crystal structure of the wild-type AtBgl1A was determined at 2.37-Å resolution, and served as a guide for the design of thermostabilizing mutations. Among variants, the A17S/S39T/T105V triple mutant showed the most significant improvement in thermostability, with a 145 min inc

SUBMITTER: Pitchayatanakorn P 

PROVIDER: S-EPMC12223823 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature