Poster: Modulation Of Chaperone Gene Expression In Mutagenised S. Cerevisiae Strains Developed For rHA Production Results In Increased Production Of Multiple Heterologous Proteins

The yeast S. cerevisiae has been successfully established as a commercially viable system for the production of recombinant proteins. A wide range of both industrially and medically important proteins have been produced using this organism, from hormones and antibodies to cytokines and blood proteins. Manipulation of chaperone gene expression has been utilised extensively to increase recombinant protein production from S. cerevisiae, focusing predominantly on the protein disulphide isomerise PDI1 and the hsp70 KAR2.