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 407941
Title Screening for distinct xylan degrading enzymes in complex shake flask fermentation supernatants
Author(s) Gool, M.P. van; Vansco, I.; Schols, H.A.; Toth, K.; Szakacs, G.; Gruppen, H.
Source Bioresource Technology 102 (2011)10. - ISSN 0960-8524 - p. 6039 - 6047.
Department(s) Food Chemistry Group
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) alpha-l-arabinofuranosidases - eucalyptus-globulus labill - wheat-flour arabinoxylan - xylanolytic enzymes - aspergillus - mode - arabinofuranohydrolase - oligosaccharides - purification - esterases
Abstract The efficient degradation of complex xylans needs collaboration of many xylan degrading enzymes. Assays for xylan degrading activities based on reducing sugars or PNP substrates are not indicative for the presence of enzymes able to degrade complex xylans: They do not provide insight into the possible presence of xylanase-accessory enzymes within enzyme mixtures. A new screening method is described, by which specific xylan modifying enzymes can be detected. Fermentation supernatants of 78 different fungal soil isolates grown on wheat straw were analyzed by HPLC and MS. This strategy is powerful in recognizing xylanases, arabinoxylan hydrolases, acetyl xylan esterases and glucuronidases. No fungus produced all enzymes necessary to totally degrade the substrates tested. Some fungi produce high levels of xylanase active against linear xylan, but are unable to degrade complex xylans. Other fungi producing relative low levels of xylanase secrete many useful accessory enzyme component(s).
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