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A comparative study: Aminopeptidase activities from Lactobaclllus delbrueckii ssp. Bulgaricus and Streptococcus thermophllus

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dc.contributor.author Tsakalidou, E en
dc.contributor.author Dalezios, I en
dc.contributor.author Georgalaki, M en
dc.contributor.author Kalantzopoulos, G en
dc.date.accessioned 2014-06-06T06:42:30Z
dc.date.available 2014-06-06T06:42:30Z
dc.date.issued 1993 en
dc.identifier.issn 00220302 en
dc.identifier.uri http://dx.doi.org/10.3168/jds.S0022-0302(93)77549-9 en
dc.identifier.uri http://62.217.125.90/xmlui/handle/123456789/659
dc.subject Aminopeptidase en
dc.subject Bulgaricus en
dc.subject Lactobacillus delbrueckii ssp en
dc.subject Streptococcus thermophilus en
dc.subject.other Lactobacillus delbrueckii en
dc.subject.other Streptococcus en
dc.subject.other Streptococcus thermophilus en
dc.title A comparative study: Aminopeptidase activities from Lactobaclllus delbrueckii ssp. Bulgaricus and Streptococcus thermophllus en
heal.type journalArticle en
heal.identifier.primary 10.3168/jds.S0022-0302(93)77549-9 en
heal.publicationDate 1993 en
heal.abstract Aminopeptidases from Lactobacillus delbrueckii ssp. bulgaricus and Streptococcus thermophilus were isolated. Enzymes were purified by chromatography on DEAE-cellulose and Sephadex G-150. The enzymes had molecular weights of 98,000 and 89,000 and optimal activity at pH 6.0 and 40°C and pH 6.5 and 35°C, respectively. The L delbrueckii ssp. bulgaricus enzyme had higher activity on L-lysyl-4-nitroanilide than did the 5. thermophilus enzyme. Both enzymes were inactivated by EDTA and 1,10-phenanthroline. Classical sulfhydryl and serine group reagents had little or no inhibitory effect on the enzymes; nevertheless, Cu ++ and Hg ++ resulted in strong inhibition; Ca ++ stimulated the L. delbrueckii ssp. bulgaricus enzyme, and Mg ++ stimulated the S. thermophilus enzyme. en
heal.journalName Journal of Dairy Science en
dc.identifier.issue 8 en
dc.identifier.volume 76 en
dc.identifier.doi 10.3168/jds.S0022-0302(93)77549-9 en
dc.identifier.spage 2145 en
dc.identifier.epage 2151 en


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