| dc.contributor.author |
Kakariari, E |
en |
| dc.contributor.author |
Georgalaki, MD |
en |
| dc.contributor.author |
Kalantzopoulos, G |
en |
| dc.contributor.author |
Tsakalidou, E |
en |
| dc.date.accessioned |
2014-06-06T06:44:20Z |
|
| dc.date.available |
2014-06-06T06:44:20Z |
|
| dc.date.issued |
2000 |
en |
| dc.identifier.issn |
00237302 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/1814 |
|
| dc.relation.uri |
http://www.scopus.com/inward/record.url?eid=2-s2.0-0034375079&partnerID=40&md5=eb091bac8c67d5cbe500a8497fdbee9e |
en |
| dc.subject |
Characterization |
en |
| dc.subject |
Esterase |
en |
| dc.subject |
Propionibacterium freudenreichii ssp. freudenreichii |
en |
| dc.subject |
Purification |
en |
| dc.title |
Purification and characterization of an intracellular esterase from Propionibacterium freudenreichii ssp. freudenreichii ITG 14 |
en |
| heal.type |
journalArticle |
en |
| heal.publicationDate |
2000 |
en |
| heal.abstract |
An intracellular esterase from Propionibacterium freudenreichii ssp. freudenreichii ITG 14 was purified by anion exchange and gel filtration chromatography. The enzyme had a molecular weight of 47 400 g-mol-1 as determined by gel filtration chromatography, with an optimum activity on α-naphthyl-acetate at pH 6.0 and at 65 °C, with KM = 1.2 mmol·L-1. The esterase hydrolyzed synthetic substrates of low molecular weight (C2-C4), and among triglycerides only triacetin. Sulfhydryl group reagents and metal chelators had limited or no effect on enzyme activity; highest inhibition was observed with phenylmethylsulfonylfluoride (PMSF). |
en |
| heal.journalName |
Lait |
en |
| dc.identifier.issue |
5 |
en |
| dc.identifier.volume |
80 |
en |
| dc.identifier.spage |
491 |
en |
| dc.identifier.epage |
501 |
en |