| dc.contributor.author |
Tsakalidou, E |
en |
| dc.contributor.author |
Kalantzopoulos, G |
en |
| dc.date.accessioned |
2014-06-06T06:42:18Z |
|
| dc.date.available |
2014-06-06T06:42:18Z |
|
| dc.date.issued |
1992 |
en |
| dc.identifier.issn |
00218847 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/547 |
|
| dc.relation.uri |
http://www.scopus.com/inward/record.url?eid=2-s2.0-0026589249&partnerID=40&md5=a8979c96bac18f3f3474455dcd570d90 |
en |
| dc.subject.other |
aminopeptidase |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
chromatography |
en |
| dc.subject.other |
enzyme purification |
en |
| dc.subject.other |
food |
en |
| dc.subject.other |
greece |
en |
| dc.subject.other |
nonhuman |
en |
| dc.subject.other |
streptococcus salivarius |
en |
| dc.subject.other |
Aminopeptidases |
en |
| dc.subject.other |
Animal |
en |
| dc.subject.other |
Edetic Acid |
en |
| dc.subject.other |
Enzyme Stability |
en |
| dc.subject.other |
Food Microbiology |
en |
| dc.subject.other |
Heat |
en |
| dc.subject.other |
Hydrogen-Ion Concentration |
en |
| dc.subject.other |
Molecular Weight |
en |
| dc.subject.other |
Streptococcus |
en |
| dc.subject.other |
Substrate Specificity |
en |
| dc.subject.other |
Support, Non-U.S. Gov't |
en |
| dc.subject.other |
Temperature |
en |
| dc.subject.other |
Yogurt |
en |
| dc.title |
Purification and partial characterization of an intracellular aminopeptidase from Streptococcus salivarius subsp. thermophilus strain ACA-DC 114 |
en |
| heal.type |
journalArticle |
en |
| heal.publicationDate |
1992 |
en |
| heal.abstract |
An intracellular aminopeptidase from Streptococcus salivarius subsp. thermophilus strain ACA-DC 114, isolated from traditional Greek yoghurt, was purified by chromatography on DEAE-cellulose and Sephadex G-100. The enzyme had a molecular weight of 89000. It was active over a pH range 4.5-9.5 and had optimum activity on L-lysyl-4-nitroanilide at pH 6.5 and 35°C with K(m) = 1.80 mmol/l; above 55°C the enzyme activity declined rapidly. The aminopeptidase was capable of degrading substrates by hydrolysis of the N-terminal amino acid; it had very low endopeptidase and no carboxypeptidase activity. The enzyme was strongly inactivated by EDTA. Serine and sulphydryl group reagents had no effect on enzyme activity. |
en |
| heal.journalName |
Journal of Applied Bacteriology |
en |
| dc.identifier.issue |
3 |
en |
| dc.identifier.volume |
72 |
en |
| dc.identifier.spage |
227 |
en |
| dc.identifier.epage |
232 |
en |