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 |