A novel expression system for intracellular production and purification of recombinant affinity-tagged proteins in Aspergillus niger.

2.50
Hdl Handle:
http://hdl.handle.net/10033/97513
Title:
A novel expression system for intracellular production and purification of recombinant affinity-tagged proteins in Aspergillus niger.
Authors:
Roth, Andreas H F J; Dersch, Petra
Abstract:
A 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.
Affiliation:
Institute of Microbiology, Technical University Braunschweig, Spielmannstrasse 7, 38106, Braunschweig, Germany.
Citation:
A novel expression system for intracellular production and purification of recombinant affinity-tagged proteins in Aspergillus niger. 2010, 86 (2):659-70 Appl. Microbiol. Biotechnol.
Journal:
Applied microbiology and biotechnology
Issue Date:
Mar-2010
URI:
http://hdl.handle.net/10033/97513
DOI:
10.1007/s00253-009-2252-9
PubMed ID:
19908039
Type:
Article
Language:
en
ISSN:
1432-0614
Appears in Collections:
publications of the department of molecular Infectionbiology (MIBI)

Full metadata record

DC FieldValue Language
dc.contributor.authorRoth, Andreas H F Jen
dc.contributor.authorDersch, Petraen
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.en
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

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