| dc.contributor.author |
Galiotou-Panayotou, M |
en |
| dc.contributor.author |
Rodis, P |
en |
| dc.contributor.author |
Macris, B |
en |
| dc.contributor.author |
Stathakos, D |
en |
| dc.date.accessioned |
2014-06-06T06:41:40Z |
|
| dc.date.available |
2014-06-06T06:41:40Z |
|
| dc.date.issued |
1988 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1007/BF00250409 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/194 |
|
| dc.subject |
Enzyme |
en |
| dc.subject |
Kinetics |
en |
| dc.subject |
Molecular Weight |
en |
| dc.subject |
Specific Activity |
en |
| dc.title |
Purification of a novel enzyme involved in catechin degradation by Calvatia gigantea |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1007/BF00250409 |
en |
| heal.publicationDate |
1988 |
en |
| heal.abstract |
A novel enzyme, involved in the degradation of catechin by Calvatia gigantea, was purified 114-fold over the crude extract yielding 24% purified enzyme with a specific activity 16.1 U/mg protein. Two isozymic forms (I and II) were isolated, both exhibiting the same kinetic characteristics with maximum activity at pH 8 and 35°C. SDS electrophoresis of I and II revealed the |
en |
| heal.journalName |
Applied Microbiology and Biotechnology |
en |
| dc.identifier.doi |
10.1007/BF00250409 |
en |