Production of recombinant proteins by high cell density culture of Escherichia coli

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dc.contributor.authorChoi J.H.ko
dc.contributor.authorKeum K.C.ko
dc.contributor.authorLee, SangYupko
dc.date.accessioned2010-11-15T06:32:17Z-
dc.date.available2010-11-15T06:32:17Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued2006-02-
dc.identifier.citationCHEMICAL ENGINEERING SCIENCE, v.61, pp.876 - 885-
dc.identifier.issn0009-2509-
dc.identifier.urihttp://hdl.handle.net/10203/19918-
dc.description.abstractEscherichia coli has been the most widely used host for the production of recombinant proteins because it is the best characterized system in every aspect. Furthermore, the high cell density culture of recombinant E. coli has allowed production of various proteins with high yield and high productivities. Various cultivation strategies employing different host strains and expression systems have been successfully employed for the production of recombinant proteins. New strategies for strain improvement towards the goal of enhanced protein production are actively being developed based on high-throughput omics approaches such as transcriptomics and proteomcs. This paper reviews recent advances in the production of recombinant proteins by high cell density culture of E. coli. (c) 2005 Elsevier Ltd. All rights reserved.-
dc.description.sponsorshipOur work described in this paper was supported by the National Research Laboratory Program (2000-N-NL-01-C- 237) from the Ministry of Science and Technology. Further supports by the KOSEF through the Center for Ultramicrochemical Process Systems, IBM-SUR program, LG Chem Chair Professorship, and by the BK21 program are greatly appreciated.en
dc.languageEnglish-
dc.language.isoen_USen
dc.publisherPERGAMON-ELSEVIER SCIENCE LTD-
dc.titleProduction of recombinant proteins by high cell density culture of Escherichia coli-
dc.typeArticle-
dc.identifier.wosid000233814600002-
dc.identifier.scopusid2-s2.0-27844581254-
dc.type.rimsART-
dc.citation.volume61-
dc.citation.beginningpage876-
dc.citation.endingpage885-
dc.citation.publicationnameCHEMICAL ENGINEERING SCIENCE-
dc.identifier.doi10.1016/j.ces.2005.03.031-
dc.embargo.liftdate9999-12-31-
dc.embargo.terms9999-12-31-
dc.contributor.localauthorLee, SangYup-
dc.contributor.nonIdAuthorChoi J.H.-
dc.contributor.nonIdAuthorKeum K.C.-
dc.type.journalArticleReview-
dc.subject.keywordAuthorhigh cell density culture-
dc.subject.keywordAuthortranscriptomics-
dc.subject.keywordAuthorproteomics-
dc.subject.keywordAuthorsystems biology-
dc.subject.keywordAuthorEscherichia coli-
dc.subject.keywordAuthorrecombinant protein-
dc.subject.keywordPlusSINGLE-STEP PURIFICATION-
dc.subject.keywordPlusCOLONY-STIMULATING FACTOR-
dc.subject.keywordPlusEPIDERMAL-GROWTH-FACTOR-
dc.subject.keywordPlusHIGH-LEVEL EXPRESSION-
dc.subject.keywordPlusFED-BATCH CULTURE-
dc.subject.keywordPlusSECRETORY PRODUCTION-
dc.subject.keywordPlusHETEROLOGOUS PROTEINS-
dc.subject.keywordPlusENHANCED PRODUCTION-
dc.subject.keywordPlusINCLUSION-BODIES-
dc.subject.keywordPlusHUMAN LEPTIN-
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