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 406110
Title Mode of action of Chrysosporium lucknowense C1 a-l-arabinohydrolases
Author(s) Kuhnel, S.; Westphal, Y.; Hinz, S.W.A.; Schols, H.A.; Gruppen, H.
Source Bioresource Technology 102 (2011)2. - ISSN 0960-8524 - p. 1636 - 1643.
Department(s) Food Chemistry Group
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) glycoside hydrolase family - aspergillus-niger - geobacillus-stearothermophilus - streptomyces-avermitilis - l-arabinofuranosidases - degradation - substrate - arabinan - oligosaccharides - fermentation
Abstract The mode of action of four Chrysosporium lucknowense C1 a-l-arabinohydrolases was determined to enable controlled and effective degradation of arabinan. The active site of endoarabinanase Abn1 has at least six subsites, of which the subsites -1 to +2 have to be occupied for hydrolysis. Abn1 was able to hydrolyze a branched arabinohexaose with a double substituted arabinose at subsite -2. The exo acting enzymes Abn2, Abn4 and Abf3 release arabinobiose (Abn2) and arabinose (Abn4 and Abf3) from the non-reducing end of reduced arabinose oligomers. Abn2 binds the two arabinose units only at the subsites -1 and -2. Abf3 prefers small oligomers over large oligomers. It is able to hydrolyze all linkages present in beet arabinan, including the linkages of double substituted residues. Abn4 is more active towards polymeric substrate and releases arabinose monomers from single substituted arabinose residues. Depending on the combination of the enzymes, the C1 arabinohydrolases can be used to effectively release branched arabinose oligomers and/or arabinose monomers.
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