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Type: Journal article
Title: Enhanced activity of enzymes encapsulated in hydrophilic metal-organic frameworks
Author: Liang, W.
Xu, H.
Carraro, F.
Maddigan, N.K.
Li, Q.
Bell, S.G.
Huang, D.M.
Tarzia, A.
Solomon, M.B.
Amenitsch, H.
Vaccari, L.
Sumby, C.J.
Falcaro, P.
Doonan, C.J.
Citation: Journal of the American Chemical Society, 2019; 141(6):2348-2355
Publisher: American Chemical Society
Issue Date: 2019
ISSN: 0002-7863
Statement of
Weibin 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
Abstract: Encapsulation 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.
Keywords: Enzymes, Immobilized
Protein Conformation
Protein Denaturation
Models, Molecular
Hydrophobic and Hydrophilic Interactions
Metal-Organic Frameworks
Rights: Copyright: Published 2019 by the American Chemical Society
DOI: 10.1021/jacs.8b10302
Grant ID:
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Chemistry publications

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