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Increased expression level and catalytic activity of internally-duplicated carbonic anhydrase from Dunaliella species by reconstitution of two separate domains

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dc.contributor.authorKi, Mi-Ran-
dc.contributor.authorKanth, Bashistha Kumar-
dc.contributor.authorMin, Ki Ha-
dc.contributor.authorLee, Jinwon-
dc.contributor.authorPack, Seung Pil-
dc.date.accessioned2021-09-06T16:07:11Z-
dc.date.available2021-09-06T16:07:11Z-
dc.date.created2021-06-18-
dc.date.issued2012-09-
dc.identifier.issn1359-5113-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/107588-
dc.description.abstractAlthough internally-duplicated, alpha-type carbonic anhydrase (CA) from Dunaliella species (Dsp-CA) can be expressed in Escherichia coli system, the produced amount is not sufficient for practical application. Here, we demonstrated to express the N- and C-half CA domains of Dsp-CA as distinct proteins to increase the expression levels further. The purified N-half CA domain (Dsp-CA-n) showed very low detectable activities of esterase or CO2 hydratase. In contrast, the purified C-half CA domain (Dsp-CA-c) retained both activities, which were enhanced by the presence of Dsp-CA-n. The expression levels of both domains were increased by 2-5-fold as compared to that of Dsp-CA. The CA activity was successfully reconstituted by mixing the two domains, N- and C-half domains, and more activity level was achieved than dimeric intact CA. These results newly suggest that the produced amount and activity of a duplicated CA are enhanced successfully by expressing each half CA domain individually and in vitro reconstitution. (C) 2012 Elsevier Ltd. All rights reserved.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherELSEVIER SCI LTD-
dc.subjectBIOMIMETIC SEQUESTRATION-
dc.subjectESCHERICHIA-COLI-
dc.subjectCO2-
dc.subjectPRECIPITATION-
dc.subjectMORPHOLOGY-
dc.subjectCALCITE-
dc.subjectACETATE-
dc.subjectSALINA-
dc.subjectSALT-
dc.titleIncreased expression level and catalytic activity of internally-duplicated carbonic anhydrase from Dunaliella species by reconstitution of two separate domains-
dc.typeArticle-
dc.contributor.affiliatedAuthorKi, Mi-Ran-
dc.contributor.affiliatedAuthorPack, Seung Pil-
dc.identifier.doi10.1016/j.procbio.2012.05.005-
dc.identifier.scopusid2-s2.0-84862875051-
dc.identifier.wosid000306777400018-
dc.identifier.bibliographicCitationPROCESS BIOCHEMISTRY, v.47, no.9, pp.1423 - 1427-
dc.relation.isPartOfPROCESS BIOCHEMISTRY-
dc.citation.titlePROCESS BIOCHEMISTRY-
dc.citation.volume47-
dc.citation.number9-
dc.citation.startPage1423-
dc.citation.endPage1427-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiotechnology & Applied Microbiology-
dc.relation.journalResearchAreaEngineering-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiotechnology & Applied Microbiology-
dc.relation.journalWebOfScienceCategoryEngineering, Chemical-
dc.subject.keywordPlusBIOMIMETIC SEQUESTRATION-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusCO2-
dc.subject.keywordPlusPRECIPITATION-
dc.subject.keywordPlusMORPHOLOGY-
dc.subject.keywordPlusCALCITE-
dc.subject.keywordPlusACETATE-
dc.subject.keywordPlusSALINA-
dc.subject.keywordPlusSALT-
dc.subject.keywordAuthorCarbonic anhydrase-
dc.subject.keywordAuthorDunaliella species-
dc.subject.keywordAuthorRepeat domain-
dc.subject.keywordAuthorCO2 mineralization-
dc.subject.keywordAuthorCalcite-
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