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Proteinase, peptidase and esterase activities of cell-free extracts from wild strains of Lactobacillus delbrueckii subsp. bulgaricus and Streptococcus salivarius subsp. thermophilus isolated from traditional Greek yogurt

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dc.contributor.author Kalantzopoulos, G en
dc.contributor.author Tsakalidou, E en
dc.contributor.author Manolopoulou, E en
dc.date.accessioned 2014-06-06T06:41:56Z
dc.date.available 2014-06-06T06:41:56Z
dc.date.issued 1990 en
dc.identifier.issn 00220299 en
dc.identifier.uri http://dx.doi.org/10.1017/S0022029900029642 en
dc.identifier.uri http://62.217.125.90/xmlui/handle/123456789/342
dc.subject.other Bovinae en
dc.subject.other Lactobacillus delbrueckii en
dc.subject.other Lactobacillus delbrueckii subsp. bulgaricus en
dc.subject.other Streptococcus salivarius en
dc.subject.other Streptococcus thermophilus en
dc.title Proteinase, peptidase and esterase activities of cell-free extracts from wild strains of Lactobacillus delbrueckii subsp. bulgaricus and Streptococcus salivarius subsp. thermophilus isolated from traditional Greek yogurt en
heal.type journalArticle en
heal.identifier.primary 10.1017/S0022029900029642 en
heal.publicationDate 1990 en
heal.abstract Proteinase, peptidase and esterase activities were detected in cell-free extracts of four Lactobacillus delbrueckii subsp. bulgaricus and four Streptococcus salivarius subsp. thermophilics strains. Post-electrophoretic detection was based on hydrolysis of L-leucine-β-naphthylamide and α-naphthylacetate. The substrates L-leucine-p-nitroanilide, N-aeetyl-L-alanine-p-nitroanilide, 2-nitrophenylbutyrate and 4-nitrophenylbutyrate were used for the spectrophotometric detection of the enzymes. Estimation of total proteolytic activity was based on hydrolysis of bovine whole casein. Interesting differences were observed between the two French strains and those isolated from traditional Greek yogurt. en
heal.journalName Journal of Dairy Research en
dc.identifier.issue 4 en
dc.identifier.volume 57 en
dc.identifier.doi 10.1017/S0022029900029642 en
dc.identifier.spage 593 en
dc.identifier.epage 601 en


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