Isolation and partial characterization of an intracellular esterase from Enterococcus faecium ACA-DC 237

dc.contributor.author	Tsakalidou, E	en
dc.date.accessioned	2014-06-06T06:42:34Z
dc.date.available	2014-06-06T06:42:34Z
dc.date.issued	1994	en
dc.identifier.issn	01681656	en
dc.identifier.uri	http://dx.doi.org/10.1016/0168-1656(94)90127-9	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/686
dc.subject	Characterization	en
dc.subject	Enterococcus faecium	en
dc.subject	Esterase	en
dc.subject	Purification	en
dc.subject.other	esterase	en
dc.subject.other	thiol group	en
dc.subject.other	article	en
dc.subject.other	cheese	en
dc.subject.other	Enterococcus faecalis	en
dc.subject.other	enzyme purification	en
dc.subject.other	Michaelis constant	en
dc.subject.other	molecular weight	en
dc.subject.other	nonhuman	en
dc.subject.other	priority journal	en
dc.subject.other	Enterococcus faecalis	en
dc.subject.other	Enterococcus faecium	en
dc.subject.other	Streptococcus	en
dc.title	Isolation and partial characterization of an intracellular esterase from Enterococcus faecium ACA-DC 237	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/0168-1656(94)90127-9	en
heal.publicationDate	1994	en
heal.abstract	An intracellular esterase from Enterococcus faecium ACA-DC 237, isolated from Greek Feta cheese, was purified on DEAE-cellulose and Sephadex G-150. The enzyme had a molecular weight of 45 000, with an optimum activity on 4-nitrophenyl butyrate at pH 8.0 and at 35°C, with Km = 0.85 mM. The esterase was capable of degrading synthetic substrates of low and medium molecular weight (C2 to C12). It was inactivated by PMSF; sulfhydryl group reagents and metal chelators had little or no effect on enzyme activity.	en
heal.journalName	Journal of Biotechnology	en
dc.identifier.issue	3	en
dc.identifier.volume	37	en
dc.identifier.doi	10.1016/0168-1656(94)90127-9	en
dc.identifier.spage	201	en
dc.identifier.epage	208	en