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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제23권 제5호
- 발행연도
- 2013.1
- 수록면
- 587 - 601 (15page)
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초록· 키워드
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During the last few decades, it has become evident that the compatibility of the yeast biochemical environment with the ability to process and translate the RNA transcript,along with its capacity to modify a translated protein, are relevant requirements for selecting this host cell for protein expression in several pharmaceutical and clinical applications. In particular, Pichia pastoris is used as an industrial host for recombinant protein and metabolite production, showing a powerful capacity to meet required biomolecular target production levels in high-throughput assays for functional genomics and drug screening. In addition, there is a great advantage to using P. pastoris for protein secretion, even at high molecular weights, since the recovery and purification steps are simplified owing to relatively low levels of endogenous proteins in the extracellular medium. Clearly, no single microexpression system can provide all of the desired properties for human protein production. Moreover, chemical and physical bioprocess parameters, including culture medium formulation,temperature, pH, agitation, aeration rates, induction, and feeding strategies, can highly influence product yield and quality. In order to benefit from the currently available wide range of biosynthesis strategies using P. pastoris, this mini review focuses on the developments and technological fermentation achievements, providing both a comparative and an overall integration analysis. The main aim is to highlight the relevance and versatility of the P. pastoris biosystem to the design of more cost-effective microfactories to meet the increasing demands for recombinant membrane proteins and clinical antibodies for several therapeutic applications.
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참고문헌 (23)
참고문헌 신청
Abdulaev, N. G. / 1997 / Functional expression of bovine opsin in the methylotrophic yeast Pichia pastoris / Protein Expr. Purif 10 : 61 ~ 69
Alisio, A / 2010 / Purification and characterization of mammalian glucose transporters expressed in Pichia pastoris / Protein Expr. Purif 70 : 81 ~ 87
Andre, N. / 2006 / Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen
Asada, H. / 2011 / Evaluation of the Pichia pastoris expression system for the production of GPCRs for structural analysis / Microb. Cell Fact 10 : 24 ~
Barnard, G. C. / 2010 / High-throughput screening and selection of yeast cell lines expressing monoclonal antibodies / J. Ind. Microbiol. Biotechnol 37 : 961 ~ 971
Alisio, A / 2010 / Purification and characterization of mammalian glucose transporters expressed in Pichia pastoris / Protein Expr. Purif 70 : 81 ~ 87
Andre, N. / 2006 / Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen
Asada, H. / 2011 / Evaluation of the Pichia pastoris expression system for the production of GPCRs for structural analysis / Microb. Cell Fact 10 : 24 ~
Barnard, G. C. / 2010 / High-throughput screening and selection of yeast cell lines expressing monoclonal antibodies / J. Ind. Microbiol. Biotechnol 37 : 961 ~ 971
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