Yeast expression systems have produced recombinant proteins for more than 20 years having proven to be efficient in production of pharmaceutical metabolites. The methylotrophic yeast Pichia pastoris has been widely reported as a suitable host cell for expression of recombinant proteins which has been dramatically used in recent years in pharmaceutical industry. Expression system of Pichia Pastoris has more advantages including easy genetic manipulation, high cell densities than mammalian cells, high potential for the production of recombinant protein with post-translational modifications, strong promoters for expression of recombinant protein and transformation of DNA external containing multiple copies of a target protein through homologous recombination process that they can be efficient for wide application in industrial fields. In this review, we investigated the system characteristics of Pichia pastoris yeast through genetic engineering, protein chemistry and molecular design that are necessary for the expression of the target proteins.
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