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The coordinated action of glucuronoyl esterase and α-glucuronidase promotes the disassembly of lignin-carbohydrate complexes.
Raji, Olanrewaju; Arnling Bååth, Jenny; Vuong, Thu V; Larsbrink, Johan; Olsson, Lisbeth; Master, Emma R.
Afiliação
  • Raji O; Department of Chemical Engineering and Applied Science, University of Toronto, ON, Canada.
  • Arnling Bååth J; Department of Biology and Biological Engineering, Wallenberg Wood Science Center, Chalmers University of Technology, Gothenburg, Sweden.
  • Vuong TV; Department of Chemical Engineering and Applied Science, University of Toronto, ON, Canada.
  • Larsbrink J; Department of Biology and Biological Engineering, Wallenberg Wood Science Center, Chalmers University of Technology, Gothenburg, Sweden.
  • Olsson L; Department of Biology and Biological Engineering, Wallenberg Wood Science Center, Chalmers University of Technology, Gothenburg, Sweden.
  • Master ER; Department of Chemical Engineering and Applied Science, University of Toronto, ON, Canada.
FEBS Lett ; 595(3): 351-359, 2021 02.
Article em En | MEDLINE | ID: mdl-33277689
ABSTRACT
Glucuronoxylans represent a significant fraction of woody biomass, and its decomposition is complicated by the presence of lignin-carbohydrate complexes (LCCs). Herein, LCCs from birchwood were used to investigate the potential coordinated action of a glucuronoyl esterase (TtCE15A) and two α-glucuronidases (SdeAgu115A and AxyAgu115A). When supplementing α-glucuronidase with equimolar quantities of TtCE15A, total MeGlcpA released after 72 h by SdeAgu115A and AxyAgu115A increased from 52% to 67%, and 61% to 95%, respectively. Based on the combined TtCE15A and AxyAgu115A activities, ~ 34% of MeGlcpA in the extracted birchwood glucuronoxylan was occupied as LCCs. Notably, insoluble LCC fractions reduced soluble α-glucuronidase concentrations by up to 70%, whereas reduction in soluble TtCE15A was less than 30%, indicating different tendencies to adsorb onto the LCC substrate.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeos / Proteínas de Bactérias / Xilanos / Esterases / Glicosídeo Hidrolases / Lignina Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeos / Proteínas de Bactérias / Xilanos / Esterases / Glicosídeo Hidrolases / Lignina Idioma: En Ano de publicação: 2021 Tipo de documento: Article