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Purification and characterisation of an intracellular X-prolyl-dipeptidyl aminopeptidase from Streptococcus thermophilus ACA-DC 4

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dc.contributor.author Tsakalidou, E en
dc.contributor.author Anastasiou, R en
dc.contributor.author Papadimitriou, K en
dc.contributor.author Manolopoulou, E en
dc.contributor.author Kalantzopoulos, G en
dc.date.accessioned 2014-06-06T06:43:46Z
dc.date.available 2014-06-06T06:43:46Z
dc.date.issued 1998 en
dc.identifier.issn 0168-1656 en
dc.identifier.uri http://62.217.125.90/xmlui/handle/123456789/1449
dc.subject Streptococcus thermophilus en
dc.subject X-prolyl-dipeptidyl aminopeptidase en
dc.subject purification en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other LACTIS SUBSP CREMORIS en
dc.subject.other LACTOCOCCUS-LACTIS en
dc.subject.other SEQUENCE-ANALYSIS en
dc.subject.other ACID BACTERIA en
dc.subject.other PEPTIDASE en
dc.subject.other CLONING en
dc.subject.other GENE en
dc.subject.other BULGARICUS en
dc.subject.other PROTEINS en
dc.subject.other MUTANTS en
dc.title Purification and characterisation of an intracellular X-prolyl-dipeptidyl aminopeptidase from Streptococcus thermophilus ACA-DC 4 en
heal.type journalArticle en
heal.language English en
heal.publicationDate 1998 en
heal.abstract An intracellular X-prolyl-dipeptidyl aminopeptidase from Streptococcus thermophilus ACA-DC 4, isolated from traditional Greek yoghurt, was purified by anion exchange and gel filtration chromatography. A single band of molecular weight of about 80 000 appeared in SDS-PAGE; by gel filtration it was shown that the native enzyme was dimeric. The peptidase showed optimum activity on glycyl-prolyl 4-nitroanilide at pH 7.0 and at 50 degrees C, with K-m = 3.1 mM and V-max = 3500 U mg(-1); over 50 degrees C the enzyme activity declined rapidly. It was inactivated by PMSF; sulfhydryl group reagents and metal chelators had little effect on enzyme activity. (C) 1998 Elsevier Science B.V. en
heal.publisher ELSEVIER SCIENCE BV en
heal.journalName JOURNAL OF BIOTECHNOLOGY en
dc.identifier.issue 3 en
dc.identifier.volume 59 en
dc.identifier.isi ISI:000072375100005 en
dc.identifier.spage 203 en
dc.identifier.epage 211 en


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