Heterologous protein expression in psychrophilic hosts

Abstract

The vast number of candidate proteins generated from genome projects are creating enormous opportunities for biologists. However, efficient expression of genes in homologous/heterologous expression systems and rapid purification steps are actually major bottlenecks. In fact, although many recombinant proteins have been successfully produced from common prokaryotic (Escherichia coli) and eukaryotic (yeast and CHO cells) hosts, these conventional systems have often proved to be unproductive due to the peculiar properties of the protein to be produced. Indeed, beside the obvious impossibility of achieving a large scale production of thermally labile proteins at the normal E. coli growth temperature, degradation of the product by the host proteases and the incorrect folding of the nascent polypeptides, resulting in the proteins aggregation and accumulation as insoluble inclusion bodies, are sometimes observed (Speed et al. 1996). © 2008 Springer-Verlag Berlin Heidelberg.