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Cell-wall-bound proteinase of Lactobacillus delbrueckii subsp. lactis ACA-DC 178: Characterization and specificity for β-casein

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dc.contributor.author Tsakalidou, E en
dc.contributor.author Anastasiou, R en
dc.contributor.author Vandenberghe, I en
dc.contributor.author Van Beeumen, J en
dc.contributor.author Kalantzopoulos, G en
dc.date.accessioned 2014-06-06T06:43:55Z
dc.date.available 2014-06-06T06:43:55Z
dc.date.issued 1999 en
dc.identifier.issn 00992240 en
dc.identifier.uri http://62.217.125.90/xmlui/handle/123456789/1558
dc.relation.uri http://www.scopus.com/inward/record.url?eid=2-s2.0-0032899032&partnerID=40&md5=d5a9b71ac64322adde98797be65a349c en
dc.subject.other bacterial enzyme en
dc.subject.other beta casein en
dc.subject.other amino acid sequence en
dc.subject.other article en
dc.subject.other bacterial cell wall en
dc.subject.other enzyme activity en
dc.subject.other enzyme analysis en
dc.subject.other enzyme specificity en
dc.subject.other enzyme synthesis en
dc.subject.other lactobacillus delbrueckii en
dc.subject.other nonhuman en
dc.subject.other protein localization en
dc.subject.other Amino Acid Sequence en
dc.subject.other Caseins en
dc.subject.other Cell Wall en
dc.subject.other Cheese en
dc.subject.other Endopeptidases en
dc.subject.other Hydrogen-Ion Concentration en
dc.subject.other Lactobacillus en
dc.subject.other Molecular Sequence Data en
dc.subject.other Peptide Fragments en
dc.subject.other Substrate Specificity en
dc.subject.other Temperature en
dc.subject.other Bacteria (microorganisms) en
dc.subject.other Lactobacillus en
dc.subject.other Lactobacillus delbrueckii subsp. lactis en
dc.subject.other Posibacteria en
dc.title Cell-wall-bound proteinase of Lactobacillus delbrueckii subsp. lactis ACA-DC 178: Characterization and specificity for β-casein en
heal.type journalArticle en
heal.publicationDate 1999 en
heal.abstract Lactobacillus delbrueckii subsp. lactis ACA-DC 178, which was isolated from Greek Kasseri cheese, produces a cell-wall-bound proteinase. The proteinase was removed from the cell envelope by washing the cells with a Ca2+-free buffer. The crude proteinase extract shows its highest activity at pH 6.0 and 40°C. It is inhibited by phenylmethylsulfonyl fluoride, showing that the enzyme is a serine-type proteinase. Considering the substrate specificity, the enzyme is similar to the lactococcal P1-type proteinases, since it hydrolyzes β-casein mainly and α- and κ-caseins to a much lesser extent. The cell-wall-bound proteinase from L. delbrueckii subsp. lactis ACA-DC 178 liberates four main peptides from β-casein, which have been identified. en
heal.journalName Applied and Environmental Microbiology en
dc.identifier.issue 5 en
dc.identifier.volume 65 en
dc.identifier.spage 2035 en
dc.identifier.epage 2040 en


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