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Action of Xylan Deacetylating Enzymes on Monoacetyl Derivatives of 4-nitrophenyl Glycosides of β-D-xylopyranose and α-L-arabinofuranose

Action of Xylan Deacetylating Enzymes on Monoacetyl Derivatives of 4-nitrophenyl Glycosides of β-D-xylopyranose and α-L-arabinofuranose

Peter Biely, Mária Mastihubová, Maija Tenkanen, Jaime Eyzaguirre, Xin-Liang Li, Mária Vršanská

J Biotechnol. 2011 Jan 10;151(1):137-42.

PMID: 21029756

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP2001969	4-Nitrophenyl β-D-xylopyranoside		2001-96-9	Price

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