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Substrate and posit...
Substrate and positional specificity of feruloyl esterases for monoferuloylated and monoacetylated 4-nitrophenyl glycosides
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- Puchar, Vladimir (författare)
- Slovak Academy of Sciences, Bratislava
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- Vršanská, Mária (författare)
- Slovak Academy of Sciences, Bratislava
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- Mastihubová, Mária (författare)
- Slovak Academy of Sciences, Bratislava
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- Topakas, Evangelos (författare)
- National Technical University of Athens
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- Vafiadi, Christina (författare)
- National Technical University of Athens
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- Faulds, Craig B. (författare)
- Institute of Food Research
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- Tenkanen, Maija (författare)
- University of Helsinki
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Christakopoulos, Paul (författare)
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- Biely, Peter (författare)
- Slovak Academy of Sciences, Bratislava
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(creator_code:org_t)
- Elsevier BV, 2007
- 2007
- Engelska.
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Ingår i: Journal of Biotechnology. - : Elsevier BV. - 0168-1656 .- 1873-4863. ; 127:2, s. 235-243
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 4-Nitrophenyl glycosides of 2-, 3-, and 5-O-(E)-feruloyl- and 2- and 5-O-acetyl-α-l-arabinofuranosides and of 2-, 3-, and 4-O-(E)-feruloyl- and 2-, 3- and 4-O-acetyl-β-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-α-l-arabinofuranoside. On the contrary, type-B and -C feruloyl esterases, represented by FoFaeI from F. oxysporum and TsFaeC from Talaromyces stipitatus, acted on almost all ferulates with exception of 4- and 3-O-feruloyl-β-d-xylopyranoside. 5-O-Feruloyl-α-l-arabinofuranoside was the best substrate for both TsFaeC and FoFaeI, although catalytic efficiency of the latter enzyme toward 2-O-feruloyl-α-l-arabinofuranoside was comparable. In comparison with acetates, the corresponding ferulates served as poor substrates for the carbohydrate esterase family 1 feruloyl esterase from Aspergillus oryzae. The enzyme hydrolyzed all α-l-arabinofuranoside and β-d-xylopyranoside acetates. It behaved as a non-specific acetyl esterase rather than a feruloyl esterase, with a preference for 2-O-acetyl-β-d-xylopyranoside.
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