ISOLATION AND PARTIAL CHARACTERIZATION OF AN INTRACELLULAR ESTERASE FROM ENTEROCOCCUS-FAECIUM ACA-DC-237

dc.contributor.author	TSAKALIDOU, E	en
dc.contributor.author	DALEZIOS, I	en
dc.contributor.author	KALANTZOPOULOS, G	en
dc.date.accessioned	2014-06-06T06:42:44Z
dc.date.available	2014-06-06T06:42:44Z
dc.date.issued	1994	en
dc.identifier.issn	0168-1656	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/783
dc.subject	ENTEROCOCCUS FAECIUM	en
dc.subject	ESTERASE	en
dc.subject	PURIFICATION	en
dc.subject	CHARACTERIZATION	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	LACTOBACILLUS-HELVETICUS	en
dc.subject.other	STREPTOCOCCUS-FAECALIS	en
dc.subject.other	LIPOLYTIC-ACTIVITIES	en
dc.subject.other	LIPASE	en
dc.subject.other	LACTIS	en
dc.subject.other	PURIFICATION	en
dc.subject.other	BACTERIOCIN	en
dc.subject.other	BULGARICUS	en
dc.subject.other	CREMORIS	en
dc.subject.other	STARTER	en
dc.title	ISOLATION AND PARTIAL CHARACTERIZATION OF AN INTRACELLULAR ESTERASE FROM ENTEROCOCCUS-FAECIUM ACA-DC-237	en
heal.type	journalArticle	en
heal.language	English	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 degrees C, with K-m = 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.publisher	ELSEVIER SCIENCE BV	en
heal.journalName	JOURNAL OF BIOTECHNOLOGY	en
dc.identifier.issue	3	en
dc.identifier.volume	37	en
dc.identifier.isi	ISI:A1994PU02600002	en
dc.identifier.spage	201	en
dc.identifier.epage	208	en