Mapping the hydrolytic and synthetic selectivity of a type C feruloyl esterase (StFaeC) from Sporotrichum thermophile using alkyl ferulates

Vafiadi, C; Topakas, E; Wong, KKY; Suckling, ID; Christakopoulos, P

dc.contributor.author	Vafiadi, C	en
dc.contributor.author	Topakas, E	en
dc.contributor.author	Wong, KKY	en
dc.contributor.author	Suckling, ID	en
dc.contributor.author	Christakopoulos, P	en
dc.date.accessioned	2014-03-01T01:22:42Z
dc.date.available	2014-03-01T01:22:42Z
dc.date.issued	2005	en
dc.identifier.issn	09574166	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/16631
dc.subject	Active Site	en
dc.subject	Enzyme	en
dc.subject.other	arabinose	en
dc.subject.other	esterase	en
dc.subject.other	ferulic acid	en
dc.subject.other	fructose	en
dc.subject.other	galactose	en
dc.subject.other	glucose	en
dc.subject.other	mannose	en
dc.subject.other	pyranoside	en
dc.subject.other	ribose	en
dc.subject.other	xylose	en
dc.subject.other	article	en
dc.subject.other	binding affinity	en
dc.subject.other	concentration (parameters)	en
dc.subject.other	enzyme active site	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme specificity	en
dc.subject.other	enzyme substrate	en
dc.subject.other	enzyme substrate complex	en
dc.subject.other	hydrolysis	en
dc.subject.other	molecular probe	en
dc.subject.other	priority journal	en
dc.subject.other	Sporothrix	en
dc.subject.other	synthesis	en
dc.title	Mapping the hydrolytic and synthetic selectivity of a type C feruloyl esterase (StFaeC) from Sporotrichum thermophile using alkyl ferulates	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.tetasy.2004.11.037	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.tetasy.2004.11.037	en
heal.publicationDate	2005	en
heal.abstract	The active site of Sporotrichum thermophile type C feruloyl esterase (StFaeC) was probed using a series of C1-C4 alkyl ferulates. The affinities for straight and branched alkyl ferulates were demonstrated by the Km values of 1.64-0.51 and 0.19-0.1, respectively. Comparison of kcat and kcat/Km values shows that the enzyme hydrolyzed n-propyl ferulate faster and iso-propyl ferulate more efficiently. 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. Lengthening the aliphatic side chain was the most significant factor causing lower synthetic activity of the enzyme. The reaction parameters affecting the feruloylation rate and the conversion of the enzymatic process, such as the temperature and substrate concentration have been investigated. Under identical reaction conditions, the enzyme feruloylated other monosaccharides such as d-arabinose, d-glucose, d-xylose, d-mannose, d-fructose, d-galactose, d-ribose and model substrates such as 4-nitrophenyl α-l-arabinofuranoside and 4-nitrophenyl α-l-arabinopyranoside. © 2004 Elsevier Ltd. All rights reserved.	en
heal.journalName	Tetrahedron Asymmetry	en
dc.identifier.doi	10.1016/j.tetasy.2004.11.037	en
dc.identifier.volume	16	en
dc.identifier.issue	2	en
dc.identifier.spage	373	en
dc.identifier.epage	379	en