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 |