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dc.contributor.authorRoth, Andreas H F J
dc.contributor.authorDersch, Petra
dc.date.accessioned2010-04-28T07:34:12Z
dc.date.available2010-04-28T07:34:12Z
dc.date.issued2010-03
dc.identifier.citationA novel expression system for intracellular production and purification of recombinant affinity-tagged proteins in Aspergillus niger. 2010, 86 (2):659-70 Appl. Microbiol. Biotechnol.en
dc.identifier.issn1432-0614
dc.identifier.pmid19908039
dc.identifier.doi10.1007/s00253-009-2252-9
dc.identifier.urihttp://hdl.handle.net/10033/97513
dc.description.abstractA set of different integrative expression vectors for the intracellular production of recombinant proteins with or without affinity tag in Aspergillus niger was developed. Target genes can be expressed under the control of the highly efficient, constitutive pkiA promoter or the novel sucrose-inducible promoter of the beta-fructofuranosidase (sucA) gene of A. niger in the presence or absence of alternative carbon sources. All expression plasmids contain an identical multiple cloning sequence that allows parallel construction of N- or C-terminally His6- and StrepII-tagged versions of the target proteins. Production of two heterologous model proteins, the green fluorescence protein and the Thermobifida fusca hydrolase, proved the functionality of the vector system. Efficient production and easy detection of the target proteins as well as their fast purification by a one-step affinity chromatography, using the His6- or StrepII-tag sequence, was demonstrated.
dc.language.isoenen
dc.titleA novel expression system for intracellular production and purification of recombinant affinity-tagged proteins in Aspergillus niger.en
dc.typeArticleen
dc.contributor.departmentInstitute of Microbiology, Technical University Braunschweig, Spielmannstrasse 7, 38106, Braunschweig, Germany.en
dc.identifier.journalApplied microbiology and biotechnologyen
refterms.dateFOA2018-06-13T00:05:14Z
html.description.abstractA set of different integrative expression vectors for the intracellular production of recombinant proteins with or without affinity tag in Aspergillus niger was developed. Target genes can be expressed under the control of the highly efficient, constitutive pkiA promoter or the novel sucrose-inducible promoter of the beta-fructofuranosidase (sucA) gene of A. niger in the presence or absence of alternative carbon sources. All expression plasmids contain an identical multiple cloning sequence that allows parallel construction of N- or C-terminally His6- and StrepII-tagged versions of the target proteins. Production of two heterologous model proteins, the green fluorescence protein and the Thermobifida fusca hydrolase, proved the functionality of the vector system. Efficient production and easy detection of the target proteins as well as their fast purification by a one-step affinity chromatography, using the His6- or StrepII-tag sequence, was demonstrated.


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