Recombinant DNA (rDNA) technologies (genetic, protein, and metabolic engineering) allow the production of a wide range of peptides, proteins, and biochemicals from naturally nonproducing cells. These technologies, now approx 25 yr old, have become one of the most important technologies developed in the twentieth century. Pharmaceutical products and industrial enzymes were the first biotech products on the world market made by means of rDNA. Despite important advances in rDNA applications in mammalian cells, yeasts still represent attractive hosts for the production of heterologous proteins. In this review we summarize advantages and limitations of the main and most promising yeast hosts.

Porro, D., Sauer, M., Branduardi, P., Mattanovich, D. (2005). Recombinant protein production in yeasts. MOLECULAR BIOTECHNOLOGY, 31(3), 245-259 [10.1385/MB:31:3:245].

Recombinant protein production in yeasts

PORRO, DANILO;BRANDUARDI, PAOLA;
2005

Abstract

Recombinant DNA (rDNA) technologies (genetic, protein, and metabolic engineering) allow the production of a wide range of peptides, proteins, and biochemicals from naturally nonproducing cells. These technologies, now approx 25 yr old, have become one of the most important technologies developed in the twentieth century. Pharmaceutical products and industrial enzymes were the first biotech products on the world market made by means of rDNA. Despite important advances in rDNA applications in mammalian cells, yeasts still represent attractive hosts for the production of heterologous proteins. In this review we summarize advantages and limitations of the main and most promising yeast hosts.
Articolo in rivista - Articolo scientifico
yeasts; heterologous proteins; expression; industrial biotechnology
English
nov-2005
31
3
245
259
none
Porro, D., Sauer, M., Branduardi, P., Mattanovich, D. (2005). Recombinant protein production in yeasts. MOLECULAR BIOTECHNOLOGY, 31(3), 245-259 [10.1385/MB:31:3:245].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/1619
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