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

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)137-142
Number of pages6
JournalJournal of Biotechnology
Volume151
Issue number1
DOIs
Publication statusPublished - 10 Jan 2011

Keywords

  • Acetylxylan esterase
  • Hemicellulolytic carbohydrate esterases
  • Substrate specificity

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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