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https://hdl.handle.net/2440/118321
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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 1520-5126 |
Statement of Responsibility: | 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 Urease Catalase Capsules Temperature 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: | http://purl.org/au-research/grants/arc/DP170103531 |
Published version: | http://dx.doi.org/10.1021/jacs.8b10302 |
Appears in Collections: | Aurora harvest 4 Chemistry publications |
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