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 435198
Title Two GH10 endo-xylanases from Myceliophthora thermophila C1 with and without cellulose binding module act differently towards soluble and insoluble xylans
Author(s) Gool, M.P. van; Muiswinkel, G.C.J. van; Hinz, S.W.A.; Schols, H.A.; Sinitsyn, A.P.; Gruppen, H.
Source Bioresource Technology 119 (2012). - ISSN 0960-8524 - p. 123 - 132.
Department(s) Food Chemistry Group
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) chrysosporium-lucknowense - hydrolase family - substrate - arabinoxylans - hydrolysis - efficiency - residues - domains - bran
Abstract Xylanases are mostly classified as belonging to glycoside hydrolase (GH) family 10 and 11, which differ in catalytic properties and structures. However, within one family, differences may also be present. The influence of solubility and molecular structure of substrates towards the efficiency of two GH10 xylanases from Myceliophthora thermophila C1 was investigated. The xylanases differed in degradation of high and low substituted substrate and the substitution pattern was an important factor influencing their efficiency. Alkali-labile interactions, as well as the presence of cellulose within the complex cell wall structure hindered efficient hydrolysis for both xylanases. The presence of a carbohydrate binding module did not enhance the degradation of the substrates. The differences in degradation could be related to the protein structure of the two xylanases. The study shows that the classification of enzymes does not predict their performance towards various substrates.
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