Hydrolysis of Nothogenia erinacea xylan by xylanases from families 10 and 11
| Autor: | Anders Broberg, Wim Nerinckx, Jens Ø. Duus, Lesley A.S. Parolis, Patricia Ntarima, Marc Claeyssens, Haralambos Parolis |
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| Rok vydání: | 2004 |
| Předmět: |
Magnetic Resonance Spectroscopy
Time Factors Molecular Sequence Data Oligosaccharides Xylose Biochemistry Substrate Specificity Analytical Chemistry chemistry.chemical_compound Hydrolysis Ascomycota Polysaccharides Enzymatic hydrolysis Glycoside hydrolase family 10 Trifluoroacetic Acid Organic chemistry chemistry.chemical_classification Endo-1 4-beta Xylanases Organic Chemistry General Medicine Oligosaccharide Seaweed Xylan Cryptococcus Enzyme Carbohydrate Sequence chemistry Rhodophyta Xylanase Xylans Protons |
| Zdroj: | Carbohydrate Research. 339:1047-1060 |
| ISSN: | 0008-6215 |
| DOI: | 10.1016/j.carres.2004.02.017 |
| Popis: | The structures of several enzymatic hydrolysis products of Nothogenia erinacea seaweed xylan, a linear homopolymer with mixed β-(1 → 3)/β-(1 → 4) linkages, were analysed by physicochemical and biochemical techniques. With the glycoside hydrolase family 10 β-(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 11 xylanase from Thermomyces lanuginosus this is a mixed linkage tetraose. The Cryptococcus xylanase is shown to be capable of also catalysing the hydrolysis of β-(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 β-(1 → 3)/β-(1 → 4) linkage distribution within the linear d -xylose polymer. Similar results were obtained with rhodymenan, the seaweed xylan from Palmares palmata . |
| Databáze: | OpenAIRE |
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