dc.contributor.author |
Sharipova M. |
|
dc.contributor.author |
Balaban N. |
|
dc.contributor.author |
Nekhotyaeva N. |
|
dc.contributor.author |
Mardanova A. |
|
dc.contributor.author |
Dementiev A. |
|
dc.contributor.author |
Leshchinskaya I. |
|
dc.date.accessioned |
2018-09-17T21:01:40Z |
|
dc.date.available |
2018-09-17T21:01:40Z |
|
dc.date.issued |
1996 |
|
dc.identifier.issn |
1039-9712 |
|
dc.identifier.uri |
https://dspace.kpfu.ru/xmlui/handle/net/134416 |
|
dc.description.abstract |
A new alkaline phosphatase was obtained as homogeneous preparation from culture filtrate of the spore-forming Bacillus intermedius. B. intermedius phosphatase was shown to be monomer with molecular weight of 47 kDa. The enzyme possesses phosphomonoesterase and phosphodiesterase activities and exhibits a broad specificity towards a wide variety of substrates. The purified phosphatase had an optimum temperature of 50°C, optimum pH of 9.5 and was stable until 60°C at pH 8-10. The effect of divalent metal ions and thiol reagents on catalytic activity of the enzyme was studied. |
|
dc.relation.ispartofseries |
Biochemistry and Molecular Biology International |
|
dc.subject |
Alkaline phosphatase |
|
dc.subject |
Inhibition |
|
dc.subject |
Purification |
|
dc.subject |
Substrate specificity |
|
dc.title |
A novel Bacillus intermedius extracellular alkaline phosphatase: Isolation, physico-chemical and catalytic characteristics |
|
dc.type |
Article |
|
dc.relation.ispartofseries-issue |
4 |
|
dc.relation.ispartofseries-volume |
38 |
|
dc.collection |
Публикации сотрудников КФУ |
|
dc.relation.startpage |
753 |
|
dc.source.id |
SCOPUS10399712-1996-38-4-SID0029775085 |
|