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Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of β-d-xylopyranose and α-l-arabinofuranose

Paper ID Volume ID Publish Year Pages File Format Full-Text
23943 43483 2011 6 PDF Available
Title
Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of β-d-xylopyranose and α-l-arabinofuranose
Abstract

Measurements of esterase activity by enzyme-coupled assays on monoacetates of 4-nitrophenyl β-d-xylopyranoside and 4-nitrophenyl α-l-arabinofuranoside showed that acetylxylan esterases of families 1, 4 and 5 produced by Trichoderma reesei and Penicillium purpurogenum have a strong preference for deacetylation of position 2 in xylopyranosides. The acetylxylan esterases exhibit only weak activity on acetylated arabinofuranosides, with 2-acetate as the best substrate. Acetyl esterases of family 16 produced by the same two fungi deacetylate in xylopyranosides preferentially positions 3 and 4. Their specific activity on arabinofuranosides is also much lower than on xylopyranosides, however, substantially greater than that in the case of typical acetylxylan esterases.

Keywords
AcXE, acetylxylan esterase; AcE, acetyl esterase; CE, carbohydrate esteraseHemicellulolytic carbohydrate esterases; Acetylxylan esterase; Substrate specificity
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Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of β-d-xylopyranose and α-l-arabinofuranose
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 151, Issue 1, 10 January 2011, Pages 137–142
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Don't Miss Today's Special Offer
Price was $35.95
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