Abstract

Production of recombinant proteins, including enzymes, in a heterologous host is often necessary to obtain sufficient amounts for functional studies. In particular, yeast expression systems are cost-effective and convenient for producing recombinant proteins having post-translational modifications characteristic of eukaryotes. The yeast Pichia pastoris is a unicellular eukaryote that can be handled in the same environment as Escherichia coli. Here, we present an overview of the construction of expression systems in P. pastoris and their application for the production of recombinant proteins.

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