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dc.contributor.author김호건-
dc.date.accessioned2020-04-16T01:17:07Z-
dc.date.available2020-04-16T01:17:07Z-
dc.date.issued2004-07-
dc.identifier.citationCOLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS, v. 241, No. 1-3, Page. 113-117en_US
dc.identifier.issn0927-7757-
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0927775704002298#!-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/151016-
dc.description.abstractNanoporous silica suitable for enzyme support was synthesized via a salt route and the pore morphology in the silica was characterized. Then, Glutaryl-7-ACA acylase—the enzyme for the bioconversion process to synthesize an antibiotic—was immobilized and the enzyme activity was investigated in relation to the pore morphology. It became clear that the activity of the enzyme was influenced to a great extent by the pore size and there existed an optimum pore size that lead to the maximum activity of the enzyme. In this study, the optimum pore size (diameter) was found to be 60.9 nm at which the enzyme activity was maximized to 97 units/g.en_US
dc.language.isoen_USen_US
dc.publisherELSEVIER SCIENCE BVen_US
dc.subjectNanoporous silicaen_US
dc.subjectSupporten_US
dc.subjectEnzyme immobilizationen_US
dc.subjectEnzyme activityen_US
dc.titleSynthesis and characterization of nanoporous silica support for enzyme immobilizationen_US
dc.typeArticleen_US
dc.identifier.doi10.1016/j.colsurfa.2004.04.048-
dc.relation.journalCOLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS-
dc.contributor.googleauthorKim, Jong-Kil-
dc.contributor.googleauthorPark, Jin-Koo-
dc.contributor.googleauthorKim, Ho-Kun-
dc.relation.code2009202091-
dc.sector.campusE-
dc.sector.daehakCOLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E]-
dc.sector.departmentDEPARTMENT OF CHEMICAL AND MOLECULAR ENGINEERING-
dc.identifier.pidhkkim-


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