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Mode of action of endo-β-1,4-xylanases of families 10 and 11 on acidic xylooligosaccharides

Paper ID Volume ID Publish Year Pages File Format Full-Text
25762 43597 2006 8 PDF Available
Title
Mode of action of endo-β-1,4-xylanases of families 10 and 11 on acidic xylooligosaccharides
Abstract

Mode of action of endo-β-1,4-xylanases (EXs) of glycoside hydrolase families 10 (GH-10) and 11 (GH-11) was examined on various acidic xylooligosaccharides. As expected, none of the enzymes of GH-10 cleaved aldotetraouronic acid (MeGlcA3Xyl3), which is the shortest acidic product of the action of these EXs on glucuronoxylan. Surprisingly, aldopentaouronic acid (MeGlcA3Xyl4) was also not attacked. Only aldohexaouronic acid (MeGlcA3Xyl5) served as a substrate and was cleaved to xylobiose and aldotetraouronic acid. These results suggested that binding of xylopyranosyl residue in the −2 subsite is prerequisite for cleavage of the linkage adjacent to the xylopyranosyl unit carrying MeGlcA. EXs of family GH-11 cleaved neither aldotetraouronic acid, nor aldopentaouronic acid, which is in agreement with their action on glucuronoxylan. Aldohexaouronic acid was cleaved to aldopentaouronic acid and xylobiose without any production of xylose, suggesting that a xylosyl transfer reaction is involved in the degradation of the substrate by EXs of GH-11.

Keywords
Endo-β-1,4-xylanase; Xylooligosaccharides; Cleavage; Degradation
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Mode of action of endo-β-1,4-xylanases of families 10 and 11 on acidic xylooligosaccharides
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 121, Issue 3, 10 February 2006, Pages 338–345
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
Online Support
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