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[9] Use of Pichia pastoris for expression of recombinant proteins

1999; Academic Press; Linguagem: Inglês

10.1016/s0076-6879(99)06011-5

1557-7988

Stuart A. Rosenfeld,

Fungal and yeast genetics research

Publisher Summary Several features of P. pastoris make it attractive as a host for expressing recombinant proteins. The characterization and exploitation of the alcohol oxidase (AOX) promoter to drive heterologous gene expression was instrumental to the successful implementation of the P. pastoris expression system. This chapter emphasizes the strategies and methods for optimizing the selection, screening, and scale-up production of recombinant proteins expressed using this system. P. pastoris has proven to be a useful addition to existing prokaryotic and eukaryotic protein production systems. Multisubunit protein complexes have been produced using this system, which may facilitate more involved protein chemistry/enzymology and characterization. The high biomass and protein productivity attained by P. pastoris may be exploited for the production of biocatalysts. Pichia pastoris may be useful for the expression of pharmacologically interesting receptors, including the important G-protein-coupled receptors.