Substrate and positional specificity of feruloyl esterases for monoferuloylated and monoacetylated 4-nitrophenyl glycosides

Puchart, V; Vrsanska, M; Mastihubova, M; Topakas, E; Vafiadi, C; Faulds, CB; Tenkanen, M; Christakopoulos, P; Biely, P

dc.contributor.author	Puchart, V	en
dc.contributor.author	Vrsanska, M	en
dc.contributor.author	Mastihubova, M	en
dc.contributor.author	Topakas, E	en
dc.contributor.author	Vafiadi, C	en
dc.contributor.author	Faulds, CB	en
dc.contributor.author	Tenkanen, M	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Biely, P	en
dc.date.accessioned	2014-03-01T01:27:20Z
dc.date.available	2014-03-01T01:27:20Z
dc.date.issued	2007	en
dc.identifier.issn	0168-1656	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/18404
dc.subject	α-l-Arabinofuranoside and β-d-xylopyranoside acetates and ferulates	en
dc.subject	Feruloyl/acetyl esterase	en
dc.subject	Substrate and positional specificity	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	Alcohols	en
dc.subject.other	Catalyst selectivity	en
dc.subject.other	Enzymes	en
dc.subject.other	Sugars	en
dc.subject.other	Yeast	en
dc.subject.other	Acetyl esterase	en
dc.subject.other	Aspergillus niger	en
dc.subject.other	Aspergillus oryzae	en
dc.subject.other	Deferuloylation	en
dc.subject.other	Feruloyl esterase	en
dc.subject.other	Hydroxyl groups	en
dc.subject.other	Positional specificity	en
dc.subject.other	Enzyme kinetics	en
dc.subject.other	4 nitrophenyl 2 o acetyl alpha levo arabinofuranoside	en
dc.subject.other	4 nitrophenyl 2 o acetyl beta dextro xylopyranoside	en
dc.subject.other	4 nitrophenyl 2 o feruloyl alpha levo arabinofuranoside	en
dc.subject.other	4 nitrophenyl 2 o feruloyl beta dextro xylopyranoside	en
dc.subject.other	4 nitrophenyl 3 o acetyl beta dextro xylopyranoside	en
dc.subject.other	4 nitrophenyl 3 o feruloyl alpha levo arabinofuranoside	en
dc.subject.other	4 nitrophenyl 3 o feruloyl beta dextro xylopyranoside	en
dc.subject.other	4 nitrophenyl 4 o acetyl beta dextro xylopyranoside	en
dc.subject.other	4 nitrophenyl 4 o feruloyl beta dextro xylopyranoside	en
dc.subject.other	4 nitrophenyl 5 o acetyl alpha levo arabinofuranoside	en
dc.subject.other	4 nitrophenyl 5 o feruloyl alpha levo arabinofuranoside	en
dc.subject.other	acetic acid derivative	en
dc.subject.other	alpha levo arabinofuranoside acetate	en
dc.subject.other	beta dextro xylopyranoside acetate	en
dc.subject.other	esterase	en
dc.subject.other	feruloyl esterase	en
dc.subject.other	feruloyl esterase a	en
dc.subject.other	feruloyl esterase b	en
dc.subject.other	feruloyl esterase c	en
dc.subject.other	glycoside	en
dc.subject.other	unclassified drug	en
dc.subject.other	article	en
dc.subject.other	Aspergillus niger	en
dc.subject.other	Aspergillus oryzae	en
dc.subject.other	catalysis	en
dc.subject.other	chemical modification	en
dc.subject.other	chemical reaction kinetics	en
dc.subject.other	controlled study	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme specificity	en
dc.subject.other	enzyme substrate	en
dc.subject.other	Fusarium oxysporum	en
dc.subject.other	hydrolysis	en
dc.subject.other	nonhuman	en
dc.subject.other	priority journal	en
dc.subject.other	Acetylation	en
dc.subject.other	Acetylesterase	en
dc.subject.other	Arabinose	en
dc.subject.other	Aspergillus niger	en
dc.subject.other	Carboxylic Ester Hydrolases	en
dc.subject.other	Fungi	en
dc.subject.other	Fusarium	en
dc.subject.other	Glycoside Hydrolases	en
dc.subject.other	Glycosides	en
dc.subject.other	Hydrolysis	en
dc.subject.other	Kinetics	en
dc.subject.other	Substrate Specificity	en
dc.subject.other	Talaromyces	en
dc.subject.other	Aspergillus niger	en
dc.subject.other	Aspergillus oryzae	en
dc.subject.other	Fusarium oxysporum	en
dc.subject.other	Talaromyces stipitatus	en
dc.title	Substrate and positional specificity of feruloyl esterases for monoferuloylated and monoacetylated 4-nitrophenyl glycosides	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.jbiotec.2006.06.020	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.jbiotec.2006.06.020	en
heal.language	English	en
heal.publicationDate	2007	en
heal.abstract	4-Nitrophenyl glycosides of 2-, 3-, and 5-O-(E)-feruloyl- and 2- and 5-O-acetyl-alpha-L-arabinofuranosides and of 2, 3-, and 4-O-(E)-fer-uloyl- and 2, 3- and 4-0-acetyl-beta-D-xylopyranosides, compounds mimicking natural substrates, were used to investigate substrate and positional specificity of type-A, -B, and -C feruloyl esterases. All the feruloyl esterases behave as true feruloyl esterases showing negligible activity on sugar acetates. Type-A enzymes, represented by AnFaeA from Aspergillus niger and FoFaeII from Fusarium oxysporum, are specialized for deferuloylation of primary hydroxyl groups, with a very strong preference for hydrolyzing 5-O-feruloyl-alpha-L-arabinofuranoside. On the contrary, type-B and -C feruloyl esterases, represented by FoFaeI from E oxysporum and TsFaeC from Talaromyces stipitatus, acted on almost all ferulates with exception of 4- and 3-O-feruloyl-beta-D-xylopyranoside. 5-O-Feruloyl-alpha-L-arabinofuranoside was the best substrate for both TsFaeC and FoFaeI, although catalytic efficiency of the latter enzyme toward 2-O-fer-uloyl-alpha-L-arabinofuranoside was comparable. In comparison with acetates, the corresponding ferulates served as poor substrates for the carbohydrate esterase family I feruloyl esterase from Aspergillus oryzae. The enzyme hydrolyzed all alpha-L-arabinofurano side and beta-D-xylopyranoside acetates. It behaved as a non-specific acetyl esterase rather than a feruloyl esterase, with a preference for 2-O-acetyl-beta-D-xylopyranoside. (c) 2006 Elsevier B.V. All rights reserved.	en
heal.publisher	ELSEVIER SCIENCE BV	en
heal.journalName	Journal of Biotechnology	en
dc.identifier.doi	10.1016/j.jbiotec.2006.06.020	en
dc.identifier.isi	ISI:000243657600007	en
dc.identifier.volume	127	en
dc.identifier.issue	2	en
dc.identifier.spage	235	en
dc.identifier.epage	243	en