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

Vladimir Puchart, Maria Vrsanska, Maria Mastihubova, Evangelos Topakas, Christina Vafiadi, Craig B Faulds, Maija Tenkanen, Paul Christakopoulos, Peter Biely

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review


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.
TidskriftJournal of Biotechnology
Sidor (från-till)235-243
Antal sidor9
StatusPublicerad - 2007
MoE-publikationstypA1 Tidskriftsartikel-refererad

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