| dc.contributor.author |
TSAKALIDOU, E |
en |
| dc.contributor.author |
KALANTZOPOULOS, G |
en |
| dc.date.accessioned |
2014-06-06T06:42:18Z |
|
| dc.date.available |
2014-06-06T06:42:18Z |
|
| dc.date.issued |
1992 |
en |
| dc.identifier.issn |
0023-7302 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/554 |
|
| dc.subject |
LACTOCOCCUS-LACTIS SSP LACTIS |
en |
| dc.subject |
ESTERASE |
en |
| dc.subject |
PURIFICATION |
en |
| dc.subject |
ACTIVITY |
en |
| dc.subject |
CHARACTERIZATION |
en |
| dc.subject.classification |
Food Science & Technology |
en |
| dc.subject.other |
LIPOLYTIC-ACTIVITIES |
en |
| dc.subject.other |
LACTOBACILLUS-HELVETICUS |
en |
| dc.subject.other |
STREPTOCOCCUS-CREMORIS |
en |
| dc.subject.other |
LIPASE |
en |
| dc.subject.other |
MUTANTS |
en |
| dc.subject.other |
BULGARICUS |
en |
| dc.subject.other |
SYSTEMS |
en |
| dc.title |
PURIFICATION AND PARTIAL CHARACTERIZATION OF AN ESTERASE FROM LACTOCOCCUS-LACTIS SSP LACTIS STRAIN ACA-DC 127 |
en |
| heal.type |
journalArticle |
en |
| heal.language |
English |
en |
| heal.publicationDate |
1992 |
en |
| heal.abstract |
An esterase from Lactococcus lactis spp lactis strain ACA-DC 127, isolated from Greek Feta cheese, was purified on DEAE-cellulose and Sephadex G-100. The enzyme had a molecular weight of 68 000, with an optimum activity on 4-nitrophenyl butyrate at pH 8.0 at 45-degrees-C with K(m) = 1.11 mmol.l-1. The esterase was capable of degrading synthetic substrates of low molecular weight. It was strongly inactivated by PMSF. 1,10-phenanthroline and EDTA had no effect on enzyme activity. The bivalent cations Hg2+ and Cu2+ inhibited the esterase activity. |
en |
| heal.publisher |
EDITIONS SCIENTIFIQUES ELSEVIER |
en |
| heal.journalName |
LAIT |
en |
| dc.identifier.issue |
6 |
en |
| dc.identifier.volume |
72 |
en |
| dc.identifier.isi |
ISI:A1992KJ79200003 |
en |
| dc.identifier.spage |
533 |
en |
| dc.identifier.epage |
543 |
en |