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Structural characte...
Structural characterization of the family GH115 α-glucuronidase from Amphibacillus xylanus yields insight into its coordinated action with α-arabinofuranosidases
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- Yan, Ruoyu (author)
- University of Toronto
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- Wang, Weijun (author)
- University of Toronto
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- Vuong, Thu V. (author)
- University of Toronto
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- Xiu, Yang (author)
- University of Toronto
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- Skarina, Tatiana (author)
- University of Toronto
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- Di Leo, Rosa (author)
- University of Toronto
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- Gatenholm, Paul, 1956 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Toriz Gonzalez, Guillermo, 1968 (author)
- Universidad de Guadalajara,University of Guadalajara
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- Tenkanen, Maija (author)
- Helsingin Yliopisto,University of Helsinki
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- Stogios, Peter J. (author)
- University of Toronto
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- Master, Emma (author)
- Aalto-Yliopisto,Aalto University,University of Toronto
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(creator_code:org_t)
- Elsevier BV, 2021
- 2021
- English.
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In: New Biotechnology. - : Elsevier BV. - 1876-4347 .- 1871-6784. ; 62, s. 49-56
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Abstract
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)
- NATURVETENSKAP -- Kemi -- Organisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Organic Chemistry (hsv//eng)
Keyword
- GH115
- α-Arabinofuranosidase
- α-Glucuronidase
- GH62
- Arabinoglucuronoxylan
- GH51
- Hemicellulases
Publication and Content Type
- art (subject category)
- ref (subject category)
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- By the author/editor
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Yan, Ruoyu
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Wang, Weijun
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Vuong, Thu V.
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Xiu, Yang
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Skarina, Tatiana
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Di Leo, Rosa
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show more...
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Gatenholm, Paul, ...
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Toriz Gonzalez, ...
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Tenkanen, Maija
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Stogios, Peter J ...
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Master, Emma
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Structural Biolo ...
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- ENGINEERING AND TECHNOLOGY
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ENGINEERING AND ...
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and Industrial Biote ...
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and Biocatalysis and ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Chemical Science ...
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and Organic Chemistr ...
- Articles in the publication
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New Biotechnolog ...
- By the university
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Chalmers University of Technology