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

• Published in: Journal of biotechnology 2011-01, Vol.151 (1), p.137-142
• Main Authors: Biely, Peter, Mastihubová, Mária, Tenkanen, Maija, Eyzaguirre, Jaime, Li, Xin-Liang, Vršanská, Mária
• Format: Article
• Language: English
• Subjects: Acetylation; Acetylesterase - chemistry; Acetylesterase - metabolism; Acetylxylan esterase; Arabinose - analogs & derivatives; Arabinose - chemistry; Arabinose - metabolism; Biological and medical sciences; Biotechnology; Derivatives; Enzymes; Esterases; Fundamental and applied biological sciences. Psychology; Fungi; Glycosides; Glycosides - chemistry; Glycosides - metabolism; Hemicellulolytic carbohydrate esterases; Hypocrea jecorina; Nitrobenzenes - chemistry; Nitrobenzenes - metabolism; Penicillium; Penicillium - enzymology; Penicillium purpurogenum; Polysaccharides - chemistry; Polysaccharides - metabolism; Substrate specificity; Trichoderma - enzymology; Trichoderma reesei; Xylose - analogs & derivatives; Xylose - chemistry; Xylose - metabolism
• ISSN: 0168-1656; 1873-4863
• DOI: 10.1016/j.jbiotec.2010.10.074

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.