dc.contributor.author |
Hatzinikolaou, D |
en |
dc.contributor.author |
Tsoukia, C |
en |
dc.contributor.author |
Kekos, D |
en |
dc.contributor.author |
Macris, B |
en |
dc.date.accessioned |
2014-03-01T01:46:40Z |
|
dc.date.available |
2014-03-01T01:46:40Z |
|
dc.date.issued |
1998 |
en |
dc.identifier.uri |
https://dspace.lib.ntua.gr/xmlui/handle/123456789/24979 |
|
dc.subject |
Aspergillus Niger |
en |
dc.subject |
Enzyme |
en |
dc.subject |
Response Surface Methodology |
en |
dc.subject |
Superoxide Dismutase |
en |
dc.subject |
Molecular Weight |
en |
dc.subject |
Specific Activity |
en |
dc.title |
An efficient and optimized purification procedure for the superoxide dismutase from Aspergillus niger . Partial characterization of the purified enzyme |
en |
heal.type |
journalArticle |
en |
heal.identifier.primary |
10.1023/A:1007986510153 |
en |
heal.identifier.secondary |
http://dx.doi.org/10.1023/A:1007986510153 |
en |
heal.publicationDate |
1998 |
en |
heal.abstract |
Cu, Zn-superoxide dismutase was isolated from Aspergillus niger mycelia, harvested at the mid-logarithmic growth phase. The purification scheme aimed at the optimization of the ethanol/chloroform extraction (Tsuchihashi extraction) through response surface methodology. Upon optimum extraction conditions, it was possible to obtain electrophoretically pure enzyme preparations, by the application of one step anion exchange chromatography. The enzyme yield of this simple |
en |
dc.identifier.doi |
10.1023/A:1007986510153 |
en |