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Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/118321
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dc.contributor.authorLiang, W.-
dc.contributor.authorXu, H.-
dc.contributor.authorCarraro, F.-
dc.contributor.authorMaddigan, N.K.-
dc.contributor.authorLi, Q.-
dc.contributor.authorBell, S.G.-
dc.contributor.authorHuang, D.M.-
dc.contributor.authorTarzia, A.-
dc.contributor.authorSolomon, M.B.-
dc.contributor.authorAmenitsch, H.-
dc.contributor.authorVaccari, L.-
dc.contributor.authorSumby, C.J.-
dc.contributor.authorFalcaro, P.-
dc.contributor.authorDoonan, C.J.-
dc.date.issued2019-
dc.identifier.citationJournal of the American Chemical Society, 2019; 141(6):2348-2355-
dc.identifier.issn0002-7863-
dc.identifier.issn1520-5126-
dc.identifier.urihttp://hdl.handle.net/2440/118321-
dc.description.abstractEncapsulation of biomacromolecules in metal-organic frameworks (MOFs) can preserve biological functionality in harsh environments. Despite the success of this approach, termed biomimietic mineralization, limited consideration has been given to the chemistry of the MOF coating. Here, we show that enzymes encapsulated within hydrophilic MAF-7 or ZIF-90 retain enzymatic activity upon encapsulation and when exposed to high temperatures, denaturing or proteolytic agents, and organic solvents, whereas hydrophobic ZIF-8 affords inactive catalase and negligible protection to urease.-
dc.description.statementofresponsibilityWeibin Liang, Huoshu Xu, Francesco Carraro, Natasha K. Maddigan, Qiaowei Li, Stephen G. Bell, David M. Huang, Andrew Tarzia, Marcello B. Solomon, Heinz Amenitsch, Lisa Vaccari, Christopher J. Sumby, Paolo Falcaro, and Christian J. Doonan-
dc.language.isoen-
dc.publisherAmerican Chemical Society-
dc.rightsCopyright: Published 2019 by the American Chemical Society-
dc.source.urihttp://dx.doi.org/10.1021/jacs.8b10302-
dc.subjectEnzymes, Immobilized-
dc.subjectUrease-
dc.subjectCatalase-
dc.subjectCapsules-
dc.subjectTemperature-
dc.subjectProtein Conformation-
dc.subjectProtein Denaturation-
dc.subjectModels, Molecular-
dc.subjectHydrophobic and Hydrophilic Interactions-
dc.subjectMetal-Organic Frameworks-
dc.titleEnhanced activity of enzymes encapsulated in hydrophilic metal-organic frameworks-
dc.typeJournal article-
dc.identifier.doi10.1021/jacs.8b10302-
dc.relation.granthttp://purl.org/au-research/grants/arc/DP170103531-
pubs.publication-statusPublished-
dc.identifier.orcidBell, S.G. [0000-0002-7457-9727]-
dc.identifier.orcidHuang, D.M. [0000-0003-2048-4500]-
dc.identifier.orcidSolomon, M.B. [0000-0003-0732-676X]-
dc.identifier.orcidSumby, C.J. [0000-0002-9713-9599]-
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Chemistry publications

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