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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 (författare)
- University of Toronto
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- Wang, Weijun (författare)
- University of Toronto
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- Vuong, Thu V. (författare)
- University of Toronto
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- Xiu, Yang (författare)
- University of Toronto
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- Skarina, Tatiana (författare)
- University of Toronto
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- Di Leo, Rosa (författare)
- University of Toronto
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- Gatenholm, Paul, 1956 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Toriz Gonzalez, Guillermo, 1968 (författare)
- Universidad de Guadalajara,University of Guadalajara
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- Tenkanen, Maija (författare)
- Helsingin Yliopisto,University of Helsinki
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- Stogios, Peter J. (författare)
- University of Toronto
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- Master, Emma (författare)
- Aalto-Yliopisto,Aalto University,University of Toronto
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(creator_code:org_t)
- Elsevier BV, 2021
- 2021
- Engelska.
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Ingår i: New Biotechnology. - : Elsevier BV. - 1876-4347 .- 1871-6784. ; 62, s. 49-56
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- 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)
Nyckelord
- GH115
- α-Arabinofuranosidase
- α-Glucuronidase
- GH62
- Arabinoglucuronoxylan
- GH51
- Hemicellulases
Publikations- och innehållstyp
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- ref (ämneskategori)
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Till lärosätets databas
- Av författaren/redakt...
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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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visa fler...
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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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visa färre...
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- NATURVETENSKAP
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NATURVETENSKAP
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och Biologi
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och Strukturbiologi
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- TEKNIK OCH TEKNOLOGIER
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TEKNIK OCH TEKNO ...
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och Industriell biot ...
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och Biokatalys och e ...
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- NATURVETENSKAP
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NATURVETENSKAP
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och Organisk kemi
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Chalmers tekniska högskola