Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 476938
Title Characterization of an acetyl esterase from Myceliophthorathermophila C1 able to deacetylate xanthan
Author(s) Kool, M.M.; Schols, H.A.; Wagenknecht, M.; Hinz, S.W.A.; Moerschbacher, B.M.; Gruppen, H.
Source Carbohydrate Polymers 111 (2014). - ISSN 0144-8617 - p. 222 - 229.
DOI https://doi.org/10.1016/j.carbpol.2014.04.064
Department(s) Food Chemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2014
Keyword(s) bacterial polysaccharide xanthan - xylan esterases - carbohydrate esterases - xanthomonas-campestris - rheological properties - plant polysaccharides - enzymatic-hydrolysis - gum - transition - families
Abstract Screening of eight carbohydrate acetyl esterases for their activity towards xanthan resulted in the recogni-tion of one active esterase. AXE3, a CAZy family CE1 acetyl xylan esterase originating from Myceliophthorathermophila C1, removed 31% of all acetyl groups present in xanthan after a 48 h incubation. AXE3 activ-ity towards xanthan was only observed when xanthan molecules were in the disordered conformation.Optimal performance towards xanthan was observed at 53¿C in the complete absence of salt, a condi-tion favouring the disordered conformation. AXE3-deacetylated xanthan was hydrolyzed using cellulasesand analyzed for its repeating units using UPLC–HILIC–ELSD/ESI–MS. This showed that AXE3 specificallyremoves the acetyl groups positioned on the inner mannose and that acetyl groups positioned on theouter mannose are not removed at all. After a prolonged incubation at optimal conditions, 57% of allacetyl groups, representing 70% of all acetyl groups on the inner mannose units, were hydrolyzed.
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