Biochemical analyses of a new GH18 chitinase from <i>Beauveria bassiana</i> KW1 and its synergy with a commercial protease on silkworm exuviae hydrolysis.

ABSTRACT: This study aimed to investigate the biochemical characteristics of a new GH18 chitinase (BbChi3250) derived from Beauveria bassiana KW1, which was isolated from Bombyx batryticatus. BbChi3250 occurs widely throughout Beauveria and Cordyceps species and has low sequence identity (≤39.58%) with already-characterized B. bassiana chitinases. Biochemical analyses revealed that BbChi3250 is an endo-chitinase and shows good activity toward ethylene glycol chitin, with a k_cat/K_m of 596.00 mL·mg^-1·s^-1. Importantly, BbChi3250 demonstrates significant synergy with protease CbPro in hydrolyzing silkworm exuviae, reflected in high degrees of synergy in releasing N-acetyl-β-D-glucosamine and tyrosi

SUBMITTER: Liu Y 

PROVIDER: S-EPMC12542771 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature