Comparison of mesophilic and thermophilic feruloyl esterases: characterization of their substrate specificity for methyl phenylalkanoates.

Topakas, E; Christakopoulos, P; Faulds, CB

dc.contributor.author	Topakas, E	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Faulds, CB	en
dc.date.accessioned	2014-03-01T01:22:00Z
dc.date.available	2014-03-01T01:22:00Z
dc.date.issued	2005	en
dc.identifier.issn	0168-1656	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/16434
dc.subject	feruloyl esterase	en
dc.subject	esterase	en
dc.subject	kinetic studies	en
dc.subject	ferulic acid	en
dc.subject	diferulic acid	en
dc.subject	agro-industrial co-products	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	carboxylesterase	en
dc.subject.other	carboxylic acid	en
dc.subject.other	article	en
dc.subject.other	binding site	en
dc.subject.other	chemical structure	en
dc.subject.other	chemistry	en
dc.subject.other	comparative study	en
dc.subject.other	drug antagonism	en
dc.subject.other	enzyme specificity	en
dc.subject.other	enzymology	en
dc.subject.other	Fusarium	en
dc.subject.other	kinetics	en
dc.subject.other	metabolism	en
dc.subject.other	molecular probe	en
dc.subject.other	Sporothrix	en
dc.subject.other	temperature	en
dc.subject.other	Binding Sites	en
dc.subject.other	Carboxylic Acids	en
dc.subject.other	Carboxylic Ester Hydrolases	en
dc.subject.other	Fusarium	en
dc.subject.other	Kinetics	en
dc.subject.other	Molecular Probes	en
dc.subject.other	Molecular Structure	en
dc.subject.other	Sporothrix	en
dc.subject.other	Substrate Specificity	en
dc.subject.other	Temperature	en
dc.title	Comparison of mesophilic and thermophilic feruloyl esterases: characterization of their substrate specificity for methyl phenylalkanoates.	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.jbiotec.2004.10.001	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.jbiotec.2004.10.001	en
heal.language	English	en
heal.publicationDate	2005	en
heal.abstract	The active sites of feruloyl esterases from mesophilic and thermophilic sources were probed using methyl esters of phenylalkanoic acids. Only 13 out of 26 substrates tested were significant substrates for all the enzymes. Lengthening or shortening the aliphatic side chain while maintaining the same aromatic substitutions completely abolished activity for both enzymes, which demonstrates the importance of the correct distance between the aromatic group and the ester bond. Maintaining the phenylpropanoate structure but altering the substitutions of the aromatic ring demonstrated that the type-A esterase from the mesophilic fungus Fusarium oxysporum (FoFaeA) showed a preference for methoxylated substrates, in contrast to the type-B esterase from the same source (FoFaeB) and the thermophilic type-B (StFaeB) and type-C (StFaeC) from Sporotrichum thermophile, which preferred hydroxylated substrates. All four esterases hydrolyzed short chain aliphatic acid (C-2-C-4) esters of p-nitrophenol, but not the C-12 ester of laurate. All the feruloyl esterases were able to release ferulic acid from the plant cell wall material in conjunction with a xylanase, but only the type-A esterase FoFaeA was effective in releasing the 5,5' form of diferulic acid. The thermophilic type-B esterase had a lower catalytic efficiency than its mesophilic counterpart, but released more ferulic acid from plant cell walls. (C) 2004 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.2004.10.001	en
dc.identifier.isi	ISI:000226459000003	en
dc.identifier.volume	115	en
dc.identifier.issue	4	en
dc.identifier.spage	355	en
dc.identifier.epage	366	en