2014
DOI: 10.1016/b978-0-12-420070-8.00012-x
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Protein Expression-Yeast

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Cited by 21 publications
(9 citation statements)
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“…In vitro cellulose biosynthesis by heterologously expressed and purified plant CESAs has been achieved with single CESAs from hybrid aspen (PttCESA8), the moss Physcomitrella patens (PpCESA5), and six CESAs from bamboo (Bambusa oldhamii) . Production of functional plant CESAs requires expression in a eukaryotic organism such as yeast, as opposed to bacterial expression. Eukaryotic expression systems are favorable for plant protein expression likely due to compatible translational mechanisms and post-translational modifications . However, purification of active CESAs is challenging, requiring detergent solubilization, affinity purification, chromatographic separation, and reconstitution into proteoliposomes, thereby limiting the scale at which pure CESAs are isolated.…”
Section: Enzymatic Polysaccharide Synthesis With Glycosyltrasferasesmentioning
confidence: 99%
See 1 more Smart Citation
“…In vitro cellulose biosynthesis by heterologously expressed and purified plant CESAs has been achieved with single CESAs from hybrid aspen (PttCESA8), the moss Physcomitrella patens (PpCESA5), and six CESAs from bamboo (Bambusa oldhamii) . Production of functional plant CESAs requires expression in a eukaryotic organism such as yeast, as opposed to bacterial expression. Eukaryotic expression systems are favorable for plant protein expression likely due to compatible translational mechanisms and post-translational modifications . However, purification of active CESAs is challenging, requiring detergent solubilization, affinity purification, chromatographic separation, and reconstitution into proteoliposomes, thereby limiting the scale at which pure CESAs are isolated.…”
Section: Enzymatic Polysaccharide Synthesis With Glycosyltrasferasesmentioning
confidence: 99%
“…141−143 Eukaryotic expression systems are favorable for plant protein expression likely due to compatible translational mechanisms and post-translational modifications. 144 However, purification of active CESAs is challenging, requiring detergent solubilization, affinity purification, chromatographic separation, and reconstitution into proteoliposomes, 141−143 thereby limiting the scale at which pure CESAs are isolated. Additionally, the physical and mechanical properties of cellulosic products from recombinant plant CESAs are not well characterized, although the products from PttCESA8 are partially resistant to acid hydrolysis suggesting coalescence of glucans into crystals.…”
Section: ■ Introductionmentioning
confidence: 99%
“…Unlike E. coli, yeasts can secrete recombinant proteins extracellularly, which makes the downstream purification process simpler and less costly. The inclusion of certain PTMs in this eukaryotic expression system also often facilitates proper folding of the recombinant protein [69]. Several currently licensed hepatitis B vaccines, such as Engerix-B ® , Recombivax HB, and HEPLISAV-B, use recombinant hepatitis B surface antigens (HBsAg) synthesized in yeast [70].…”
Section: Yeastsmentioning
confidence: 99%
“…Although a few biologics are still produced in E. coli (e.g., IL-2, as described in section Interleukin-2), the lack of N-glycans that ensure quality control during folding ( 306 ) makes prokaryotic production untenable for most glycoproteins including mAbs. Yeast ( S. cerevisiae and Pichia pastoris ) provide another high productivity, low cost production platform ( 307 , 308 ) and—being eukaryotic cells—do have N-glycans; yeast glycans, however, tend to be highly mannosylated which reduces serum longevity thus compromising pharmacokinetics and also impacting downstream effector functions ( 309 ). Even though efforts have been made to “humanize” yeast glycosylation, these cells have not become a widely-accepted biomanufacturing platform ( 309 ).…”
Section: Design Considerations and Biomanufacturingmentioning
confidence: 99%