DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, TW | ko |
dc.contributor.author | Chung, BH | ko |
dc.contributor.author | Chang, YongKeun | ko |
dc.date.accessioned | 2013-03-06T23:42:48Z | - |
dc.date.available | 2013-03-06T23:42:48Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2005-03 | - |
dc.identifier.citation | BIOTECHNOLOGY PROGRESS, v.21, no.2, pp.524 - 531 | - |
dc.identifier.issn | 8756-7938 | - |
dc.identifier.uri | http://hdl.handle.net/10203/88850 | - |
dc.description.abstract | The major objective of this study is to identify fed-batch culture conditions optimal for the production of human interleukin-6 (hIL-6) in a soluble form. Five different expression vectors were constructed for the expression of hIL-6 and hIL-6s fused with NusA, maltose binding protein (MBP), thioredoxin (Trx) or ubiquitin (Ubi). A series of flask cultures were conducted in LB medium at 37 degrees C. The intact hIL-6 was expressed mostly in the form of inclusion body. More than 95% of the hIL-6 fused with NusA (NusA/hIL-6) and about 90% of MBP/hIL-6 were expressed in a soluble form, whereas Trx/hIL-6 and Ubi/hIL-6 were expressed mostly in the form of inclusion body. Based on this result, NusA was selected as the fusion partner for the production of hIL-6 in the subsequent experiments. A series of pH-stat fed-batch cultures of an E. coli BL21(DE3) transformed with a NusA/hIL-6 expression vector were conducted in a bioreactor with a working volume of about 3 L. As the amount of nitrogen source was increased in the feeding medium, more soluble NusA/hIL-6 was produced, while the total amount was not significantly changed. Under the best conditions tested, about 90% of NusA/hIL-6 was produced in the soluble form. In this case, the concentration of soluble NusA/hIL-6 was 7.5 g/L with a volumetric productivity of 0.43 g/L-h. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | HIGH-CELL-DENSITY | - |
dc.subject | SECRETORY PRODUCTION | - |
dc.subject | EXPRESSION | - |
dc.subject | GROWTH | - |
dc.subject | PURIFICATION | - |
dc.subject | PROTEINS | - |
dc.subject | FERMENTATION | - |
dc.subject | CULTIVATION | - |
dc.subject | STRAINS | - |
dc.subject | CLONING | - |
dc.title | Production of soluble human interleukin-6 in cytoplasm by fed-batch culture of recombinant E-coli | - |
dc.type | Article | - |
dc.identifier.wosid | 000228127200028 | - |
dc.identifier.scopusid | 2-s2.0-16344362895 | - |
dc.type.rims | ART | - |
dc.citation.volume | 21 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 524 | - |
dc.citation.endingpage | 531 | - |
dc.citation.publicationname | BIOTECHNOLOGY PROGRESS | - |
dc.identifier.doi | 10.1021/bp049645j | - |
dc.contributor.localauthor | Chang, YongKeun | - |
dc.contributor.nonIdAuthor | Kim, TW | - |
dc.contributor.nonIdAuthor | Chung, BH | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | HIGH-CELL-DENSITY | - |
dc.subject.keywordPlus | SECRETORY PRODUCTION | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | FERMENTATION | - |
dc.subject.keywordPlus | CULTIVATION | - |
dc.subject.keywordPlus | STRAINS | - |
dc.subject.keywordPlus | CLONING | - |
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