Format

Send to

Choose Destination
See comment in PubMed Commons below
J Biotechnol. 2011 Jan 10;151(1):137-42. doi: 10.1016/j.jbiotec.2010.10.074. Epub 2010 Oct 26.

Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of β-D-xylopyranose and α-L-arabinofuranose.

Author information

  • 1Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84538 Bratislava, Slovakia. chempbsa@savba.sk

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.

© 2010 Elsevier B.V. All rights reserved.

[PubMed - indexed for MEDLINE]

LinkOut - more resources

Full Text Sources

Other Literature Sources

PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk