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

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

dc.contributor.author	Vafiadi, C	en
dc.contributor.author	Topakas, E	en
dc.contributor.author	Suckling, ID	en
dc.contributor.author	Christakopoulos, P	en
dc.date.accessioned	2014-03-01T01:54:36Z
dc.date.available	2014-03-01T01:54:36Z
dc.date.issued	2005	en
dc.identifier.issn	0957-4166	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/27445
dc.subject.classification	Chemistry, Inorganic & Nuclear	en
dc.subject.classification	Chemistry, Organic	en
dc.subject.classification	Chemistry, Physical	en
dc.subject.other	ASPERGILLUS-NIGER	en
dc.subject.other	PHENOLIC-ACIDS	en
dc.subject.other	ENZYMATIC-SYNTHESIS	en
dc.subject.other	CANDIDA-ANTARCTICA	en
dc.subject.other	FAE-III	en
dc.subject.other	PURIFICATION	en
dc.subject.other	RELEASE	en
dc.subject.other	LIPASE	en
dc.subject.other	OLIGOSACCHARIDES	en
dc.subject.other	TRANSESTERIFICATION	en
dc.title	Mapping the hydroltic and synthetic selectivity of a type C feruloyl esterase (StFaeC) from Sporotrichum thermophile using alkyl ferulates	en
heal.type	journalArticle	en
heal.language	English	en
heal.publicationDate	2005	en
heal.abstract	The active site of Sporotrichum thermophile type C feruloyl esterase (StFaeC) was probed using a series Of C-1-C-4 alkyl ferulates. The affinities for straight and branched alkyl ferulates were demonstrated by the K-m values of 1.64-0.51 and 0.19-0.1, respectively. Comparison of k(cat), and k(cat)/K-m 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 alpha-L-arabinofuranoside and 4-nitrophenyl alpha-L-arabinopyranoside. (C) 2004 Elsevier Ltd. All rights reserved.	en
heal.publisher	PERGAMON-ELSEVIER SCIENCE LTD	en
heal.journalName	TETRAHEDRON-ASYMMETRY	en
dc.identifier.isi	ISI:000227002600010	en
dc.identifier.volume	16	en
dc.identifier.issue	2	en
dc.identifier.spage	373	en
dc.identifier.epage	379	en