| 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 |
2014-06-06T06:42:21Z |
|
| dc.date.available |
2014-06-06T06:42:21Z |
|
| dc.date.issued |
1993 |
en |
| dc.identifier.issn |
0022-0302 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/572 |
|
| dc.subject |
AMINOPEPTIDASE |
en |
| dc.subject |
LACTOBACILLUS-DELBRUECKII SSP BULGARICUS |
en |
| dc.subject |
STREPTOCOCCUS-THERMOPHILUS |
en |
| dc.subject.classification |
Agriculture, Dairy & Animal Science |
en |
| dc.subject.classification |
Food Science & Technology |
en |
| dc.subject.other |
PROLYL-DIPEPTIDYL-AMINOPEPTIDASE |
en |
| dc.subject.other |
CELL-FREE-EXTRACTS |
en |
| dc.subject.other |
PEPTIDASE ACTIVITIES |
en |
| dc.subject.other |
LACTIC STREPTOCOCCI |
en |
| dc.subject.other |
SUBSP BULGARICUS |
en |
| dc.subject.other |
CREMORIS WG2 |
en |
| dc.subject.other |
PURIFICATION |
en |
| dc.subject.other |
HYDROLASES |
en |
| dc.subject.other |
HELVETICUS |
en |
| dc.subject.other |
PROTEINASE |
en |
| dc.title |
A COMPARATIVE-STUDY - AMINOPEPTIDASE ACTIVITIES FROM LACTOBACILLUS-DELBRUECKII SSP BULGARICUS AND STREPTOCOCCUS-THERMOPHILUS |
en |
| heal.type |
journalArticle |
en |
| heal.language |
English |
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-degrees-C and pH 6.5 and 35-degrees-C, respectively. The L delbrueckii ssp. bulgaricus enzyme had higher activity on L-lysyl-4-nitroanilide than did the S. 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.publisher |
AMER DAIRY SCIENCE ASSN |
en |
| heal.journalName |
JOURNAL OF DAIRY SCIENCE |
en |
| dc.identifier.issue |
8 |
en |
| dc.identifier.volume |
76 |
en |
| dc.identifier.isi |
ISI:A1993LR04400002 |
en |
| dc.identifier.spage |
2145 |
en |
| dc.identifier.epage |
2151 |
en |