DC Field | Value | Language |
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dc.contributor.author | Moon Sun Hahm | - |
dc.contributor.author | Bong Hyun Chung | - |
dc.date.accessioned | 2017-04-19T08:58:29Z | - |
dc.date.available | 2017-04-19T08:58:29Z | - |
dc.date.issued | 2001 | - |
dc.identifier.issn | 1017-7825 | - |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/5621 | - |
dc.description.abstract | The gene encoding yeast pro-carboxypeptidase Y (pro-CPY) has been cloned and expressed in Escherichia coli. Most of the expressed pro-CPY was accumulated as cytoplasmic insoluble aggregates. In our previous study [3], active CPY was obtained by renaturation of entirely denatured pro-CPY followed by in vitro proteolytic processing with proteinase K along with the activation process. The same refolding process was performed to produce an active CPY from pro-CPY inclusion bodies with renaturation buffers containing proteinase K at different concentrations. The refolding efficiency decreased from 25% to 2% in the renaturation buffers containing proteinase K at concentrations of 60 μg/ml and 0.6 μg/ml, respectively. In an attempt to increase the refolding efficiency with a lesser amount of proteinase K, a novel fed-batch refolding process was developed. In a fed-batch refolding, 99 ml of the renaturation buffer containing pro-CPY was gradually added into 1 ml of the renaturation buffer containing 60 μg/ml of proteinase K to give a final proteinase K concentration of 0.6 μg/ml. The fed-batch refolding process resulted in a refolding efficiency of 18%, which corresponded to a 9-fold increase over that (2%) in the batch process. | - |
dc.publisher | Korea Soc-Assoc-Inst | - |
dc.title | In vitro formation of active carboxypeptidase Y from pro-carboxypeptidase Y inclusion bodies by fed-batch operation | - |
dc.title.alternative | In vitro formation of active carboxypeptidase Y from pro-carboxypeptidase Y inclusion bodies by fed-batch operation | - |
dc.type | Article | - |
dc.citation.title | Journal of Microbiology and Biotechnology | - |
dc.citation.number | 5 | - |
dc.citation.endPage | 889 | - |
dc.citation.startPage | 887 | - |
dc.citation.volume | 11 | - |
dc.contributor.affiliatedAuthor | Moon Sun Hahm | - |
dc.contributor.affiliatedAuthor | Bong Hyun Chung | - |
dc.contributor.alternativeName | 함문선 | - |
dc.contributor.alternativeName | 정봉현 | - |
dc.identifier.bibliographicCitation | Journal of Microbiology and Biotechnology, vol. 11, no. 5, pp. 887-889 | - |
dc.subject.keyword | E. coli | - |
dc.subject.keyword | pro-carboxypeptidase Y (pro-CPY) | - |
dc.subject.keyword | carboxypeptidase Y (CPY) | - |
dc.subject.keyword | refolding | - |
dc.subject.keyword | proteinase K | - |
dc.subject.local | Escherichia coli. | - |
dc.subject.local | escherichia coli | - |
dc.subject.local | Escherichia Coli | - |
dc.subject.local | Escherichia coli | - |
dc.subject.local | E.coli | - |
dc.subject.local | escherichia coil | - |
dc.subject.local | E. coli | - |
dc.subject.local | E. Coli | - |
dc.subject.local | pro-carboxypeptidase Y | - |
dc.subject.local | pro-carboxypeptidase Y (pro-CPY) | - |
dc.subject.local | carboxypeptidase Y (CPY) | - |
dc.subject.local | Refolding | - |
dc.subject.local | refolding | - |
dc.subject.local | proteinase K | - |
dc.description.journalClass | Y | - |
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