Structural and biochemical basis for activity of Aspergillus nidulans α-1,3-glucanases from glycoside hydrolase family 71.

ABSTRACT: The microbial polysaccharide α-1,3-glucan is an important component of fungal cell walls and dental plaque biofilms, contributing to microbial virulence and biofilm resilience. Glycoside hydrolase family 71 (GH71) includes α-1,3-glucan degrading enzymes which could be exploited for biotechnological applications; however, the family is presently poorly understood. To increase our understanding of GH71, we have performed a phylogenetic analysis of the family and detailed biochemical analysis of two of the five GH71 enzymes encoded by Aspergillus nidulans (AnGH71B and -C). Both are active on soluble α-1,3-glucooligosaccharides but surprisingly only minimally on water-insoluble α-1,3-glucan. Assays on intact and milled A. nidulans biomass indicate that the enzymes act on fungal cell wall glyco

SUBMITTER: Mazurkewich S 

PROVIDER: S-EPMC12394665 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature