Glucuronoxylan 3-O-acetylated on uronic acid-substituted xylopyranosyl residues and its hydrolysis by GH10, GH11 and GH30 endoxylanases.

Autor: Puchart V; Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, SK 845 38 Bratislava, Slovak Republic. Electronic address: vladimir.puchart@savba.sk., Mørkeberg Krogh KBR; Novozymes A/S, Bagsvaerd, Denmark. Electronic address: KBK@novozymes.com., Biely P; Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, SK 845 38 Bratislava, Slovak Republic. Electronic address: peter.biely@savba.sk.
Jazyk: angličtina
Zdroj: Carbohydrate polymers [Carbohydr Polym] 2019 Feb 01; Vol. 205, pp. 217-224. Date of Electronic Publication: 2018 Oct 16.
DOI: 10.1016/j.carbpol.2018.10.043
Abstrakt: Glucuronoxylan selectively 3-O-acetylated on uronic acid-substituted xylopyranosyl residues was prepared by deacetylation of steam explosion-extracted aspenwood acetylglucuronoxylan by the CE6 acetylxylan esterase from Orpinomyces sp. The 3-O-acetylation of MeGlcA-substituted xylopyranosyl residues did not influence the mode of action of GH10, 11 and 30 xylanases, resulting in similar aldouronic acids as are found in alkali-extracted glucuronoxylan hydrolysates. In all three hydrolysates of the selectively acetylated glucuronoxylan, however, 3-O-acetylated aldouronic acids predominated over non-acetylated ones, suggesting that in native aspenwood xylan almost all MeGlcA-substituted Xylp residues are 3-O-acetylated. The results contribute to current knowledge of the mode of action of xylanases and also point to a possibility to produce novel types of xylooligosaccharides. The 3-O-acetylated aldouronic acids, along with the specifically 3-O-acetylated glucuronoxylan, may serve as model substrates for searching for a novel type of esterase able to liberate this MeGlcA-shielded acetyl group. Such esterases are important to improve significantly saccharification yields.
(Copyright © 2018 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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