Secretory production of recombinant proteins in Escherichia coli

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dc.contributor.authorSung Ho Yoon-
dc.contributor.authorSeong Keun Kim-
dc.contributor.authorJihyun Kim-
dc.date.accessioned2017-04-19T09:17:28Z-
dc.date.available2017-04-19T09:17:28Z-
dc.date.issued2010-
dc.identifier.issn1872-2083-
dc.identifier.uri10.2174/187220810790069550ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9426-
dc.description.abstractExtracellular production of heterologous proteins using the Escherichia coli cell factory offers several advantages over intracellular production and mammalian culture. Properly folded proteins can be rapidly accumulated in the culture media, and downstream processes for isolation and purification can be much simplified. Efforts to enhance the secretory production of target proteins can be largely classified as selection and modification of the signal peptide, co-expression of proteins to assist translocation and folding, improvement of periplasmic release, and protection of target proteins from degradation and contamination. Here, we review recent patents on the secretory production of recombinant proteins in E. coli.-
dc.publisherBentham Science Publishersko
dc.titleSecretory production of recombinant proteins in Escherichia coli-
dc.title.alternativeSecretory production of recombinant proteins in Escherichia coli-
dc.typeArticle-
dc.citation.titleRecent Patents on Biotechnology-
dc.citation.number1-
dc.citation.endPage29-
dc.citation.startPage23-
dc.citation.volume4-
dc.contributor.affiliatedAuthorSung Ho Yoon-
dc.contributor.affiliatedAuthorSeong Keun Kim-
dc.contributor.affiliatedAuthorJihyun Kim-
dc.contributor.alternativeName윤성호-
dc.contributor.alternativeName김성근-
dc.contributor.alternativeName김지현-
dc.identifier.bibliographicCitationRecent Patents on Biotechnology, vol. 4, no. 1, pp. 23-29-
dc.identifier.doi10.2174/187220810790069550-
dc.subject.keywordSecretion-
dc.subject.keywordexcretion-
dc.subject.keywordperiplasm-
dc.subject.keywordextracellular production-
dc.subject.keywordsignal peptide-
dc.subject.keywordrecombinant protein-
dc.subject.keywordEscherichia coli.-
dc.subject.localsecretion-
dc.subject.localSecretion-
dc.subject.localExcretion-
dc.subject.localexcretion-
dc.subject.localperiplasm-
dc.subject.localPeriplasm-
dc.subject.localextracellular production-
dc.subject.localsignal peptide-
dc.subject.localSignal peptide-
dc.subject.localRecombinant Protein-
dc.subject.localrecombinant protein-
dc.subject.localrecombinant proteins-
dc.subject.localRecombinant protein-
dc.subject.localecombinant proteins-
dc.subject.localRecombinant proteins-
dc.subject.localEscherichia coli.-
dc.subject.localescherichia coli-
dc.subject.localEscherichia Coli-
dc.subject.localEscherichia coli-
dc.subject.localE.coli-
dc.subject.localescherichia coil-
dc.subject.localE. coli-
dc.subject.localE. Coli-
dc.description.journalClassN-
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > Synthetic Biology Research Center > 1. Journal Articles
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