An efficient and optimized purification procedure for the superoxide dismutase from Aspergillus niger. Partial characterization of the purified enzyme

Hatzinikolaou, DG; Tsoukia, C; Kekos, D; Macris, BJ

dc.contributor.author	Hatzinikolaou, DG	en
dc.contributor.author	Tsoukia, C	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Macris, BJ	en
dc.date.accessioned	2014-03-01T01:12:37Z
dc.date.available	2014-03-01T01:12:37Z
dc.date.issued	1997	en
dc.identifier.issn	0923-179X	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/12166
dc.subject	Aspergillus niger	en
dc.subject	Ethanol/chloroform extraction	en
dc.subject	Optimization	en
dc.subject	Purification	en
dc.subject	Superoxide dismutase	en
dc.subject.classification	Biochemical Research Methods	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	electrophoresis	en
dc.subject.other	enzyme purification	en
dc.subject.other	extraction	en
dc.subject.other	superoxide dismutase	en
dc.subject.other	Chromatographic analysis	en
dc.subject.other	Electrophoresis	en
dc.subject.other	Enzymes	en
dc.subject.other	Ethanol	en
dc.subject.other	Extraction	en
dc.subject.other	Fungi	en
dc.subject.other	Molecular structure	en
dc.subject.other	Molecular weight	en
dc.subject.other	Anion exchange chromatography	en
dc.subject.other	Chloroform	en
dc.subject.other	Superoxide dismutase	en
dc.subject.other	Purification	en
dc.subject.other	Aspergillus niger	en
dc.subject.other	Biotechnology	en
dc.subject.other	Chloroform	en
dc.subject.other	Chromatography, Ion Exchange	en
dc.subject.other	Enzyme Stability	en
dc.subject.other	Ethanol	en
dc.subject.other	Isoelectric Point	en
dc.subject.other	Molecular Weight	en
dc.subject.other	Protein Conformation	en
dc.subject.other	Superoxide Dismutase	en
dc.subject.other	Aspergillus niger	en
dc.subject.other	Aspergillus sp.	en
dc.subject.other	Fungi	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.language	English	en
heal.publicationDate	1997	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 purification procedure was above 75% while the specific activity of the final preparation was among the highest reported for eucariotic microorganisms. The purified enzyme exhibited similar physicochemical characteristics with other Aspergillus sp. superoxide dismutases revealing an apparent tetrameric structure with a subunit molecular weight of 19 kDa, and a pl of 5.95.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 purification procedure was above 75% while the specific activity of the final preparation was among the highest reported for eucariotic microorganisms. The purified enzyme exhibited similar physicochemical characteristics with other Aspergillus sp. superoxide dismutases revealing an apparent tetrameric structure with a subunit molecular weight of 19 kDa, and a pl of 5.95.	en
heal.publisher	Kluwer Academic Publishers, Dordrecht, Netherlands	en
heal.journalName	Bioseparation	en
dc.identifier.doi	10.1023/A:1007986510153	en
dc.identifier.isi	ISI:000073679200006	en
dc.identifier.volume	7	en
dc.identifier.issue	1	en
dc.identifier.spage	39	en
dc.identifier.epage	46	en