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Xylosyl transfer to cellobiose catalysed by an endo-(1→4)-β-d-xylanase of Cryptococcus albidus

✍ Scribed by Peter Biely; Mária Vršanská

Publisher: Elsevier Science
Year: 1983
Tongue: English
Weight: 614 KB
Volume: 123
Category: Article
ISSN: 0008-6215
DOI: 10.1016/0008-6215(83)88384-0

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✦ Synopsis

In transglycosylation reactions catalysed by an endo-(l-4)P-D-xylanase of the yeast Crypkxoccus albidus, cellobiose is a relatively good acceptor of xylosyl residues. Three transfer products isolated from a reaction mixture containing phenyl P-D-xylopyranoside, cellobiose, and the enzyme were established by i3Cn.m.r. spectroscopy to be 6'-0-/3-D-xylopyranosylcellobiose, 6'-0P-D-xylobiosylccllobiose, and 6'-0P-D-xylotriosylcellobiose. When these compounds were treated with the enzyme, the 6-0-P-D-xylosidic linkage was hydrolysed slowly in comparison to the rate of hydrolysis of (1-4)~B-D-xylosidic linkages.

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Hydrolysis of (1→3)- and (1→2)-β-d-xylos

Hydrolysis of (1→3)- and (1→2)-β-d-xylosidic linkages by an endo-(1→4)-β-d-xylanase of Cryptococcus albidus

✍ Mária Vršanská; Ján Hirsch; Pavol Kováč; Peter Biely 📂 Article 📅 1990 🏛 Elsevier Science 🌐 English ⚖ 494 KB

The substrate specificity of an endo-(1----4)-beta-D-xylanase of the yeast Cryptococcus albidus was investigated using a series of methyl beta-D-xylotriosides. In addition to (1----4) linkages, the enzyme could cleave (1----3) and (1----2) linkages adjacent to a (1----4) linkage and further from the