Recombinant proteins in Priestia megaterium (formerly Bacillus megaterium) and other Bacillus sp.
There are many reasons to apply Priestia megaterium (formerly Bacillus megaterium) for the production of recombinant proteins in biotechnological processes. In contrast to Escherichia coli it does not produce any endotoxins and can metabolize various cheap carbon sources. Recombinant plasmids are stably maintained. Moreover, P. megaterium shows only low activity of extracellular proteases. Consequently, many recombinantly produced secretory proteins exhibit an excellent stability.
One general aim of our project is to make P. megaterium - by upgrading the vector system and by using the sequence of the genome - an alternative tool for a broad utilization in research and industry. For this we construct optimized expression vectors for the production of recombinant intracellular and extracellular proteins, i. e. different signal peptides, different affinity tags for protein purification, coexpression of certain genes, coproduction of tRNAs. These plasmid systems are commerciallized by MoBiTec GmbH (Göttingen) since 2005. Further on we use metabolic engineering to optimize the recombinant production and secretion process of proteins.