A comparative summary of expression systems for the recombinant production of galactose oxidase.

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.

Results

The intracellular expression of a codon-optimized gene with an N

SUBMITTER: Spadiut O 

PROVIDER: S-EPMC2949794 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature