Structural characterization of the family GH115 α-glucuronidase from Amphibacillus xylanus yields insight into its coordinated action with α-arabinofuranosidases
Journal article, 2021

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

GH115

α-Arabinofuranosidase

α-Glucuronidase

GH62

Arabinoglucuronoxylan

GH51

Hemicellulases

Author

Ruoyu Yan

University of Toronto

Weijun Wang

University of Toronto

Thu V. Vuong

University of Toronto

Yang Xiu

University of Toronto

Tatiana Skarina

University of Toronto

Rosa Di Leo

University of Toronto

Paul Gatenholm

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry, Paul Gatenholm Group

Guillermo Toriz Gonzalez

University of Guadalajara

Maija Tenkanen

University of Helsinki

Peter J. Stogios

University of Toronto

Emma Master

Aalto University

University of Toronto

New Biotechnology

1871-6784 (ISSN)

Vol. 62 49-56

Subject Categories

Structural Biology

Biocatalysis and Enzyme Technology

Organic Chemistry

DOI

10.1016/j.nbt.2021.01.005

PubMed

33486119

More information

Latest update

2/11/2021