DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kang, DG | - |
dc.contributor.author | Li, L | - |
dc.contributor.author | Ha, JH | - |
dc.contributor.author | Choi, SS | - |
dc.contributor.author | Cha, HJ | - |
dc.date.accessioned | 2016-04-01T09:04:46Z | - |
dc.date.available | 2016-04-01T09:04:46Z | - |
dc.date.created | 2009-08-13 | - |
dc.date.issued | 2008-07 | - |
dc.identifier.issn | 0256-1115 | - |
dc.identifier.other | 2008-OAK-0000010912 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/29410 | - |
dc.description.abstract | Recombinant Escherichia coli systems expressing organophosphorous hydrolase (OPH) have been used for detoxifying toxic organophosphate compounds. However, a whole cell biocatalyst system has an intrinsic problem due to substrate diffusion limitation by its cell membrane. As a strategy for reducing this diffusion barrier limitation to enhance whole cell biocatalytic activity, we engineered E coli cells to target OPH on cell surface using ice nucleation protein (InaK) as a surface targeting motif, especially N-terminal domain of InaK (InaK-N). The whole cell OPH activities of the cells expressing InaK/OPH fusion constructs were higher (similar to 2.5-fold for InaK-N and similar to 5.7-fold for combined N- and C-terminal domain of InaK (InaK-NC)) than that of the cells expressing cytosolic OPH. Interestingly, the membrane targeting efficiency of the cells expressing InaK-N/OPH fusion proteins was similar to 2.2-fold higher compared to the cells expressing InaK-NC/OPH even though both whole cell and total cell lysate OPH activities were lower. Therefore, we found that the small size N-terminal domain of InaK is more efficient for targeting OPH on the cell surface, and the surface display of OPH using N-terminal InaK domain can reduce the mass-transfer problem in whole cell bioconversion system. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | KOREAN INST CHEM ENGINEERS | - |
dc.relation.isPartOf | KOREAN JOURNAL OF CHEMICAL ENGINEERING | - |
dc.subject | cell surface display | - |
dc.subject | ice nucleation protein | - |
dc.subject | N-terminal domain | - |
dc.subject | organophosphorus hydrolase | - |
dc.subject | Escherichia coli | - |
dc.subject | whole cell biocatalyst | - |
dc.subject | PSEUDOMONAS-DIMINUTA | - |
dc.subject | PERIPLASMIC SECRETION | - |
dc.subject | PHOSPHOTRIESTERASE | - |
dc.subject | HYDROLYSIS | - |
dc.subject | GENE | - |
dc.subject | BIODEGRADATION | - |
dc.subject | DETOXIFICATION | - |
dc.subject | PESTICIDES | - |
dc.subject | PATHWAY | - |
dc.subject | CLONING | - |
dc.title | Efficient cell surface display of organophosphorous hydrolase using N-terminal domain of ice nucleation protein in Escherichia coli | - |
dc.type | Article | - |
dc.contributor.college | 화학공학과 | - |
dc.identifier.doi | 10.1007/s11814-008-0132-0 | - |
dc.author.google | Kang, DG | - |
dc.author.google | Li, L | - |
dc.author.google | Ha, JH | - |
dc.author.google | Choi, SS | - |
dc.author.google | Cha, HJ | - |
dc.relation.volume | 25 | - |
dc.relation.issue | 4 | - |
dc.relation.startpage | 804 | - |
dc.relation.lastpage | 807 | - |
dc.contributor.id | 10057405 | - |
dc.relation.journal | KOREAN JOURNAL OF CHEMICAL ENGINEERING | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | KOREAN JOURNAL OF CHEMICAL ENGINEERING, v.25, no.4, pp.804 - 807 | - |
dc.identifier.wosid | 000258549600030 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 807 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 804 | - |
dc.citation.title | KOREAN JOURNAL OF CHEMICAL ENGINEERING | - |
dc.citation.volume | 25 | - |
dc.contributor.affiliatedAuthor | Cha, HJ | - |
dc.identifier.scopusid | 2-s2.0-52349118100 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 11 | - |
dc.type.docType | Article; Proceedings Paper | - |
dc.subject.keywordPlus | PSEUDOMONAS-DIMINUTA | - |
dc.subject.keywordPlus | PERIPLASMIC SECRETION | - |
dc.subject.keywordPlus | PHOSPHOTRIESTERASE | - |
dc.subject.keywordPlus | HYDROLYSIS | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | BIODEGRADATION | - |
dc.subject.keywordPlus | DETOXIFICATION | - |
dc.subject.keywordPlus | PESTICIDES | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordAuthor | cell surface display | - |
dc.subject.keywordAuthor | ice nucleation protein | - |
dc.subject.keywordAuthor | N-terminal domain | - |
dc.subject.keywordAuthor | organophosphorus hydrolase | - |
dc.subject.keywordAuthor | Escherichia coli | - |
dc.subject.keywordAuthor | whole cell biocatalyst | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.relation.journalWebOfScienceCategory | Engineering, Chemical | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalResearchArea | Engineering | - |
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