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Forskningsartikel - Refereegranskat, 2004

Hydrolysis of Nothogenia erinacea xylan by xylanases from families 10 and 11

Nerinckx W, Broberg A, Duus JO, Ntarima P, Parolis LAS, Parolis H, Claeyssens M


The structures of several enzymatic hydrolysis products of Nothogenia erinacea seaweed xylan, a linear homopolymer with mixed ss-(1 --> 3)/ss-(1 --> 4) linkages, were analysed by physicochemical and biochemical techniques. With the glycoside hydrolase family 10 ss-(1 --> 4)-xylanase from Cryptococcus adeliae, hydrolysis proceeds to a final mixture of products containing a mixed linkage-type triose as a major compound, whereas with the family I I xylanase from Thermomyces lanuginosus this is a mixed linkage tetraose. The Cryptococcus xylanase is shown to be capable of also catalysing the hydrolysis of ss-(1 --> 3) linkages, that is this of a mixed type tetraose intermediary formed, in accordance with the broader substrate specificity of family 10 enzymes. From a partial degradation experiment with the T lanuginosus xylanase, a series of higher mixed oligosaccharides were isolated and identified. The observed oligosaccharide intermediates and splicing pattern indicate an irregular ss-(1 --> 3)/ss-(1 --> 4) linkage distribution within the linear D-xylose polymer. Similar results were obtained with rhodymenan, the seaweed xylan from Palmares palmata . (C) 2004 Elsevier Ltd. All rights reserved

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Carbohydrate Research
2004, Volym: 339, nummer: 6, sidor: 1047-1060