A comparative summary of expression systems for the recombinant production of galactose oxidase |
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| Authors: | Oliver Spadiut,Lisbeth Olsson,Harry Brumer Suffix" >III |
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| Affiliation: | (1) Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), SE-106 91 Stockholm, Sweden;(2) Industrial Biotechnology, Department of Chemical and Biological Engineering, Chalmers University of Technology, SE-412 96 Gothenburg, Sweden;(3) Wallenberg Wood Science Center, Royal Institute of Technology (KTH), SE-100 44 Stockholm, Sweden;(4) Wallenberg Wood Science Center, Chalmers University of Technology, SE-412 96 Gothenburg, Sweden |
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| Abstract: | Background The microbes Escherichia coli and Pichia pastoris are convenient prokaryotic and eukaryotic hosts, respectively, for the recombinant production of proteins at laboratory scales. A comparative study was performed to evaluate a range of constructs and process parameters for the heterologous intra- and extracellular expression of genes encoding the industrially relevant enzyme galactose 6-oxidase (EC 1.1.3.9) from the fungus Fusarium graminearum. In particular, the wild-type galox gene from F. graminearum, an optimized variant for E. coli and a codon-optimized gene for P. pastoris were expressed without the native pro-sequence, but with a His-tag either at the N- or the C-terminus of the enzyme. |
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