Detailed Information

Cited 0 time in webofscience Cited 0 time in scopus
Metadata Downloads

SiO2 microparticles with carbon nanotube-derived mesopores as an efficient support for enzyme immobilization

Full metadata record
DC Field Value Language
dc.contributor.authorKumar, Ashok-
dc.contributor.authorPark, Gi Dae-
dc.contributor.authorPatel, Sanjay K. S.-
dc.contributor.authorKondaveeti, Sanath-
dc.contributor.authorOtari, Sachin-
dc.contributor.authorAnwar, Muhammad Zahid-
dc.contributor.authorKalia, Vipin C.-
dc.contributor.authorSingh, Yogendra-
dc.contributor.authorKim, Sun Chang-
dc.contributor.authorCho, Byung-Kwan-
dc.contributor.authorSohn, Jung-Hoon-
dc.contributor.authorKim, Dong Rip-
dc.contributor.authorKang, Yun Chan-
dc.contributor.authorLee, Jung-Kul-
dc.date.accessioned2021-09-01T17:55:35Z-
dc.date.available2021-09-01T17:55:35Z-
dc.date.created2021-06-19-
dc.date.issued2019-03-01-
dc.identifier.issn1385-8947-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/67048-
dc.description.abstractNovel mesoporous SiO2 microparticles were synthesized by spray pyrolysis using multiwalled carbon nanotubes (MCNTs) as a template. The synthesized multicompartment structure with uniform pores of 12.0 nm was used to immobilize lipase from Thermomyces lanuginosus. The total surface area of mesoporous SiO2 microparticles prepared from silica colloidal solution was increased by 26-folds compared to that of dense SiO2 particles (494 vs 19.0 m(2) g(-1), respectively). Mesoporous SiO2 particles showed 236% higher protein loading for lipase, than dense SiO2 particles. The maximum velocity (V-max) and catalytic efficiencies of immobilized lipase were 3.80 and 5.90 folds higher than that of free enzyme. Contact angle analysis revealed increased hydrophobicity of the mesoporous particles, which is advantageous for lid opening at the active center, and increased activity after immobilization. We next developed a lipase/SiO2/glassy carbon electrode (GCE) biosensors. Cyclic voltammetric results showed linear responses of the lipase/SiO2/GCE bioelectrode towards tributyrin (50-300 mg dL(-1)) as a surface-limited reaction in Tris-HCl buffer. After 12 repetitive uses, dense SiO2- and mesoporous SiO2-bound lipase retained 74.2 and 95.4% of its original activities, respectively. Thus, given their desirable characteristics and industrial utility, greatly porous SiO2 particles may provide an excellent support for enzyme immobilization in biosensor development or biocatalysis in organic media.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherELSEVIER SCIENCE SA-
dc.subjectMAGNETIC ORGANOSILICA NANOFLOWERS-
dc.subjectPENICILLIN-G ACYLASE-
dc.subjectGRAPHENE OXIDE-
dc.subjectDIRECT ELECTROCHEMISTRY-
dc.subjectASSISTED SYNTHESIS-
dc.subjectMODIFIED ELECTRODE-
dc.subjectGLUCOSE-OXIDASE-
dc.subjectLIPASE-
dc.subjectNANOPARTICLES-
dc.subjectSILICA-
dc.titleSiO2 microparticles with carbon nanotube-derived mesopores as an efficient support for enzyme immobilization-
dc.typeArticle-
dc.contributor.affiliatedAuthorPark, Gi Dae-
dc.contributor.affiliatedAuthorKang, Yun Chan-
dc.identifier.doi10.1016/j.cej.2018.11.052-
dc.identifier.scopusid2-s2.0-85056604576-
dc.identifier.wosid000454137400122-
dc.identifier.bibliographicCitationCHEMICAL ENGINEERING JOURNAL, v.359, pp.1252 - 1264-
dc.relation.isPartOfCHEMICAL ENGINEERING JOURNAL-
dc.citation.titleCHEMICAL ENGINEERING JOURNAL-
dc.citation.volume359-
dc.citation.startPage1252-
dc.citation.endPage1264-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaEngineering-
dc.relation.journalWebOfScienceCategoryEngineering, Environmental-
dc.relation.journalWebOfScienceCategoryEngineering, Chemical-
dc.subject.keywordPlusMAGNETIC ORGANOSILICA NANOFLOWERS-
dc.subject.keywordPlusPENICILLIN-G ACYLASE-
dc.subject.keywordPlusGRAPHENE OXIDE-
dc.subject.keywordPlusDIRECT ELECTROCHEMISTRY-
dc.subject.keywordPlusASSISTED SYNTHESIS-
dc.subject.keywordPlusMODIFIED ELECTRODE-
dc.subject.keywordPlusGLUCOSE-OXIDASE-
dc.subject.keywordPlusLIPASE-
dc.subject.keywordPlusNANOPARTICLES-
dc.subject.keywordPlusSILICA-
dc.subject.keywordAuthorMesoporous silica-
dc.subject.keywordAuthorEnzyme immobilization-
dc.subject.keywordAuthorHydrophobicity-
dc.subject.keywordAuthorBiosensor-
dc.subject.keywordAuthorStability-
Files in This Item
There are no files associated with this item.
Appears in
Collections
College of Engineering > Department of Materials Science and Engineering > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Altmetrics

Total Views & Downloads

BROWSE