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Customized Yeast Cell Factories for Biopharmaceuticals: from Cell Engineering to Process Scale Up

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Publisher Biomed Central
Date 2021 Jul 1
PMID 34193127
Citations 27
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Abstract

The manufacture of recombinant therapeutics is a fastest-developing section of therapeutic pharmaceuticals and presently plays a significant role in disease management. Yeasts are established eukaryotic host for heterologous protein production and offer distinctive benefits in synthesising pharmaceutical recombinants. Yeasts are proficient of vigorous growth on inexpensive media, easy for gene manipulations, and are capable of adding post translational changes of eukaryotes. Saccharomyces cerevisiae is model yeast that has been applied as a main host for the manufacture of pharmaceuticals and is the major tool box for genetic studies; nevertheless, numerous other yeasts comprising Pichia pastoris, Kluyveromyces lactis, Hansenula polymorpha, and Yarrowia lipolytica have attained huge attention as non-conventional partners intended for the industrial manufacture of heterologous proteins. Here we review the advances in yeast gene manipulation tools and techniques for heterologous pharmaceutical protein synthesis. Application of secretory pathway engineering, glycosylation engineering strategies and fermentation scale-up strategies in customizing yeast cells for the synthesis of therapeutic proteins has been meticulously described.

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References
1.
Gasmi N, Ayed A, Ammar B, Zrigui R, Nicaud J, Kallel H . Development of a cultivation process for the enhancement of human interferon alpha 2b production in the oleaginous yeast, Yarrowia lipolytica. Microb Cell Fact. 2011; 10:90. PMC: 3241208. DOI: 10.1186/1475-2859-10-90. View

2.
Vandermies M, Fickers P . Bioreactor-Scale Strategies for the Production of Recombinant Protein in the Yeast . Microorganisms. 2019; 7(2). PMC: 6406515. DOI: 10.3390/microorganisms7020040. View

3.
Jewett M, Hofmann G, Nielsen J . Fungal metabolite analysis in genomics and phenomics. Curr Opin Biotechnol. 2006; 17(2):191-7. DOI: 10.1016/j.copbio.2006.02.001. View

4.
Smith J, Tang B, Robinson A . Protein disulfide isomerase, but not binding protein, overexpression enhances secretion of a non-disulfide-bonded protein in yeast. Biotechnol Bioeng. 2004; 85(3):340-50. DOI: 10.1002/bit.10853. View

5.
Yang Y, Liu G, Chen X, Liu M, Zhan C, Liu X . High efficiency CRISPR/Cas9 genome editing system with an eliminable episomal sgRNA plasmid in Pichia pastoris. Enzyme Microb Technol. 2020; 138:109556. DOI: 10.1016/j.enzmictec.2020.109556. View