by Miguel Castillo et al.
Volume 8, Issue 4 (Winter 2009/2010)
In general, yeasts offer advantages for recombinant protein expression because their intracellular environment is suitable for the correct folding of recombinant proteins and grow very high cell densities in defined fermentation media. Within the yeast kingdom, Pichia pastoris has been successfully used for expressing several recombinant proteins. The genome of this yeast contains two copies of the alcohol oxidase (AOX) gene, where the AOX1 promoter regulates 85% of the alcohol oxidase activity and drives the recombinant protein expression into the cell. One of the most successfully recombinant proteins expressed in Pichia pastoris is the hepatitis B surface antigen (HBsAg). The current manufacturing process of the active pharmaceutical ingredient (HBsAg) of the Cuban hepatitis B vaccine (HeberBiovacā¢ HB) starts with the expression of the HBsAg in Pichia pastoris….
Citation:
Castillo M et al. Kinetic of Expression Study of the Hepatitis B Surface Antigen in Pichia pastoris. BioProcess J, 2009; 8(4): 16-23.Ā http://dx.doi.org/10.12665/J84.Valdes