The feruloyl esterase system of Talaromyces stipitatus: Determining the hydrolytic and synthetic specificity of TsFaeC

Vafiadi, C; Topakas, E; Christakopoulos, P; Faulds, CB

dc.contributor.author	Vafiadi, C	en
dc.contributor.author	Topakas, E	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Faulds, CB	en
dc.date.accessioned	2014-03-01T01:25:15Z
dc.date.available	2014-03-01T01:25:15Z
dc.date.issued	2006	en
dc.identifier.issn	0168-1656	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/17618
dc.subject	Alkyl ferulates	en
dc.subject	Feruloyl esterase	en
dc.subject	Kinetic studies	en
dc.subject	Phenylalkanoates	en
dc.subject	Surfactantless microemulsions	en
dc.subject	Transesterification	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	Aromatic compounds	en
dc.subject.other	Catalyst activity	en
dc.subject.other	Esterification	en
dc.subject.other	Esters	en
dc.subject.other	Hydrolysis	en
dc.subject.other	Microemulsions	en
dc.subject.other	Alkyl ferulates	en
dc.subject.other	Feruloyl esterase	en
dc.subject.other	Phenylalkanoates	en
dc.subject.other	Surfactantless microemulsions	en
dc.subject.other	Enzyme kinetics	en
dc.subject.other	alkyl group	en
dc.subject.other	arabinose	en
dc.subject.other	benzoic acid	en
dc.subject.other	butanol	en
dc.subject.other	cinnamic acid	en
dc.subject.other	ester derivative	en
dc.subject.other	ferulic acid	en
dc.subject.other	hexane	en
dc.subject.other	hydroxyl group	en
dc.subject.other	methyl group	en
dc.subject.other	propionic acid derivative	en
dc.subject.other	water	en
dc.subject.other	article	en
dc.subject.other	catalysis	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme substrate	en
dc.subject.other	enzyme synthesis	en
dc.subject.other	hydrolysis	en
dc.subject.other	mental concentration	en
dc.subject.other	nonhuman	en
dc.subject.other	priority journal	en
dc.subject.other	synthesis	en
dc.subject.other	Talaromyces	en
dc.subject.other	Binding Sites	en
dc.subject.other	Carboxylic Ester Hydrolases	en
dc.subject.other	Catalysis	en
dc.subject.other	Coumaric Acids	en
dc.subject.other	Enzyme Stability	en
dc.subject.other	Hydrolysis	en
dc.subject.other	Kinetics	en
dc.subject.other	Molecular Structure	en
dc.subject.other	Recombinant Proteins	en
dc.subject.other	Substrate Specificity	en
dc.subject.other	Talaromyces	en
dc.subject.other	Temperature	en
dc.subject.other	Talaromyces stipitatus	en
dc.title	The feruloyl esterase system of Talaromyces stipitatus: Determining the hydrolytic and synthetic specificity of TsFaeC	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.jbiotec.2006.02.009	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.jbiotec.2006.02.009	en
heal.language	English	en
heal.publicationDate	2006	en
heal.abstract	The active site of the recombinant Talaromyces stipitatus type-C feruloyl esterase (TsFaeC) was probed using a series of C-1-C-4 alkyl ferulates and methyl esters of phenylalkanoic and cinnamic acids. The enzyme was active on 23 of the 34 substrates tested. Lengthening or shortening the aliphatic side chain while maintaining the same aromatic substitutions completely abolished the enzyme activity. Maintaining the phenylpropenoate structure but altering the substitutions of the aromatic ring demonstrated the importance of hydroxyl groups on meta and/or para position of the benzoic ring. The highest catalytic efficiency of TsFaeC for methyl cinnamates was shown on methyl 3,4-dihydroxy cinnamate and on its hydro form (3,4-dihydroxy-phenyl-propionate). Maintaining the ferulate structure but altering the esterified alkyl group, the comparison of k(cat) and k(cat)/K-m values showed that the enzyme hydrolysed faster and more efficiently than ethyl ferulate. Alkyl ferulates were applied also for substrate selectivity mapping of feruloyl esterase to catalyze feruloyl group transfer to L-arabinose, using as a reaction system a ternary water-organic mixture consisting of n-hexane, t-butanol and water. The reaction parameters affecting the feruloylation rate and the conversion of the enzymatic synthesis, such as the composition of the reaction media, temperature, substrate and enzyme concentration have been investigated. (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.2006.02.009	en
dc.identifier.isi	ISI:000240208800006	en
dc.identifier.volume	125	en
dc.identifier.issue	2	en
dc.identifier.spage	210	en
dc.identifier.epage	221	en