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A General Strategy for Site-Directed Enzyme Immobilization by Using NiO Nanoparticle Decorated Mesoporous Silica

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dc.contributor.authorDaishun Ling-
dc.contributor.authorLiqian Gao-
dc.contributor.authorJianpeng Wang-
dc.contributor.authorMohammadreza Shokouhimehr-
dc.contributor.authorJiahui Liu-
dc.contributor.authorYongsheng Yu-
dc.contributor.authorMichael J. Hackett-
dc.contributor.authorSo P.-K.-
dc.contributor.authorZheng B.-
dc.contributor.authorYao Z.-
dc.contributor.authorXia J.-
dc.contributor.authorTaeg Hwan Hyeon-
dc.date.available2015-04-20T05:53:05Z-
dc.date.created2014-08-11-
dc.date.issued2014-06-
dc.identifier.issn0947-6539-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/1018-
dc.description.abstractMesoporous materials have recently gained much attention owing to their large surface area, narrow pore size distribution, and superior pore structure. These materials have been demonstrated as excellent solid supports for immobilization of a variety of proteins and enzymes for their potential applications as biocatalysts in the chemical and pharmaceutical industries. However, the lack of efficient and reproducible methods for immobilization has limited the activity and recyclability of these biocatalysts. Furthermore, the biocatalysts are usually not robust owing to their rapid denaturation in bulk solvents. To solve these problems, we designed a novel hybrid material system, mesoporous silica immobilized with NiO nanoparticles (SBA-NiO), wherein enzyme immobilization is directed to specific sites on the pore surface of the material. This yielded the biocatalytic species with higher activity than free enzyme in solution. These biocatalytic species are recyclable with minimal loss of activity after several cycles, demonstrating an advantage over free enzymes. Site-directed enzyme immobilization onto the pore surface of NiO nanoparticle decorated mesoporous silica (SBA) leads to a species with higher activity than the free enzyme in solution (see figure). These biocatalysts are recyclable with minimal loss of activity after five cycles, demonstrating an advantage over free enzymes. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.-
dc.description.uri1-
dc.language영어-
dc.publisherWILEY-V C H VERLAG GMBH-
dc.subjectEnzyme activity-
dc.subjectHybrid materials-
dc.subjectMesoporous materials-
dc.subjectNanoparticles-
dc.subjectProteins-
dc.subjectRadioactive waste vitrification-
dc.subjectEnzyme catalysis-
dc.subjectHybrid material systems-
dc.subjectLarge surface area-
dc.subjectMesoporous Silica-
dc.subjectNarrow pore size distributions-
dc.subjectNiO nanoparticles-
dc.subjectPharmaceutical industry-
dc.subjectSpecific sites-
dc.subjectEnzyme immobilization-
dc.titleA General Strategy for Site-Directed Enzyme Immobilization by Using NiO Nanoparticle Decorated Mesoporous Silica-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000337742600009-
dc.identifier.scopusid2-s2.0-84902980198-
dc.identifier.rimsid326ko
dc.date.tcdate2018-10-01-
dc.contributor.affiliatedAuthorDaishun Ling-
dc.contributor.affiliatedAuthorMohammadreza Shokouhimehr-
dc.contributor.affiliatedAuthorMichael J. Hackett-
dc.contributor.affiliatedAuthorTaeg Hwan Hyeon-
dc.identifier.doi10.1002/chem.201403071-
dc.identifier.bibliographicCitationCHEMISTRY-A EUROPEAN JOURNAL, v.20, no.26, pp.7916 - 7921-
dc.citation.titleCHEMISTRY-A EUROPEAN JOURNAL-
dc.citation.volume20-
dc.citation.number26-
dc.citation.startPage7916-
dc.citation.endPage7921-
dc.date.scptcdate2018-10-01-
dc.description.wostc18-
dc.description.scptc21-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.subject.keywordPlusMODIFIED MAGNETIC NANOPARTICLES-
dc.subject.keywordPlusHISTIDINE-TAGGED PROTEINS-
dc.subject.keywordPlusINTRACELLULAR DELIVERY-
dc.subject.keywordPlusRECENT PROGRESS-
dc.subject.keywordPlusBIOCATALYSIS-
dc.subject.keywordPlusADSORPTION-
dc.subject.keywordPlusSURFACE-
dc.subject.keywordPlusPERFORMANCE-
dc.subject.keywordPlusSEPARATION-
dc.subject.keywordPlusPARTICLES-
dc.subject.keywordAuthorenzyme catalysis-
dc.subject.keywordAuthorimmobilization-
dc.subject.keywordAuthormesoporous materials-
dc.subject.keywordAuthornanoparticles-
dc.subject.keywordAuthorproteins-
Appears in Collections:
Center for Nanoparticle Research(나노입자 연구단) > 1. Journal Papers (저널논문)
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