Yeast Expression System: Yeast Expression System For Glycoengineering

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Yeast Expression System for Glycoengineering

Yeast expression system is an alternative to prokaryotic and higher eukaryotic expression system since it offers the attributes of speedy growth, ease to manipulate genes and low costing media like for microbes along with post translational modification and secretory expression like in higher eukaryotes. An increasing number of yeast strains are available for protein expression that are said to increase the yield of the protein, improves the affinity tagging of the proteins, reduces protein breakdown, allows the addition of non-native amino acids (Selenomethionine) into the protein and defines the composition of N-glycan in the protein produced. Following are the existing genera of yeast
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Glycosylation is a post translational modification where oligosaccharide moieties are added to the protein. There are two types of glycosylation involved, the O-type and the N-type. The O-type glycosylation involves the addition of N-acetylgalactosamine (GlcNAc) to serine or threonine residues within the protein forming an O-glycosidic bond. N-type glycosylation is quite different from the O-type, here a N-glycosidic bond is formed when an oligosaccharide (glycan) is bound to asparagine residues nitrogen atom. Sequence of amino acids Asn/X/Ser/Thr is the N-glycosylation site where X is any amino acid except proline. Post translational modification specifically talking about glycosylation helps in protein folding, protein targeting, protein stabilization, regulation of proteins half-life in serum, recognition and ligand binding

YEAST EXPRESSION SYSTEM FOR ERYTHROPOIETIN PRODUCTION Recombinant human erythropoietin (rHuEpo) production in methylotrophic yeast P. pastoris reported high levels of secreted recombinant human erythropoietin by batch fermentation. Full length cDNA of recombinant human erythropoietin was inserted into pPICZαA under control of AOX1 promoter and electroporated into P. pastoris X33. Final yield after pH stabilization and addition of certain chemicals gave an improved yirld of
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Hyunah Kim, Su Jin Yoo, Hyun Ah Kang. Yeast synthetic biology for the production of recombinant therapeutic protein. DOI: http://dx.doi.org/10.1111/1567-1364.12195 1-16 First published online: 14 January 2015
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Published online: 4 November 2004 |doi:10.1038/nbt1028
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