Characterization and mode of action of two acetyl xylan esterases from Chrysosporium lucknowense C1 active towards acetylated xylans.
作者： L. Pouvreau , M.C. Jonathan , M.A. Kabel , S.W.A. Hinz , H. Gruppen
DOI: 10.1016/J.ENZMICTEC.2011.05.010
关键词:
摘要: Abstract Two novel acetyl xylan esterases, Axe2 and Axe3, from Chrysosporium lucknowense (C1), belonging to the carbohydrate esterase families 5 1, respectively, were purified biochemically characterized. Axe3 are able hydrolyze groups both simple acetylated xylo-oligosaccharides complex non-soluble acetylglucuronoxylan. Both enzymes performed optimally at pH 7.0 40 °C. has a clear preference for (AcXOS) with high degree of substitution does not show such preference. large AcXOS (DP 9–12) when compared smaller (especially DP 4–7) while size oligomer is irrelevant. Even though there difference in substrate affinity towards xylooligosaccharides Eucalyptus wood, final hydrolysis products same Axe3: containing one group located non-reducing xylose residue remain as examined using MALDI-TOF MS, CE-LIF application an endo-xylanase (GH 10).
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