Structural characterization of the family GH115 α-glucuronidase from Amphibacillus xylanus yields insight into its coordinated action with α-arabinofuranosidases

The coordinated action of carbohydrate-active enzymes has mainly been evaluated for the purpose complete saccharification plant biomass (lignocellulose) to sugars. By contrast, accessory hemicellulases on xylan debranching and recovery is less well characterized. Here, activity two family GH115 α-glucuronidases (SdeAgu115A from Saccharophagus degradans, AxyAgu115A Amphibacillus xylanus) spruce arabinoglucuronoxylan (AGX) was in combination with an α-arabinofuranosidase families GH51 (AniAbf51A, aka E-AFASE Aspergillus niger) GH62 (SthAbf62A Streptomyces thermoviolaceus). α-arabinofuranosidases boosted (methyl)-glucuronic acid release by SdeAgu115A approximately 50 % 30 %, respectively. impact comparatively low, motivating its structural characterization. crystal structure revealed increased length flexibility active site loop compared SdeAgu115A. This difference could explain ability accommodate more highly substituted arabinoglucuronoxylan, inform enzyme selections improved AGX use.