On the specificity and mode of action of a xylanase from trametes hirsuta (wulf.) pilát
✍ Scribed by Marta Kubačková; Štefan Karácsonyi; Ladislav Bilisics; Rudolf Toman
- Publisher
- Elsevier Science
- Year
- 1979
- Tongue
- English
- Weight
- 673 KB
- Volume
- 76
- Category
- Article
- ISSN
- 0008-6215
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✦ Synopsis
The mode of action of the extracellular endo-(1 leads to 4)-beta-D-xylanase produced by Trametes hirsuta on a (4-0-methyl-D-glucurono)-D-xylan and a modified, essentially neutral D-xylan from white willow (Salix alba L.) has been studied. Xylotetraose and xylohexaose, together with aldotetraouronic and aldohexaouronic acids, were the main products. The acidic oligosaccharides had a 4-O-methyl-D-glucopyranosyluronic acid group attached to the non-reducing D-xylosyl end-group. The action pattern of the xylanase corresponds to that of a typical endo-enzyme that acts more readily in the middle of chain, and the specific region of its action appears to involve five D-xylosyl residues. The products of the enzymic treatment of the D-xylan have revealed a regular distribution of the 4-O-methyl-D-glucopyranosyluronic acid groups attached to the D-xylan backbone.