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Issue 40, 2017
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In situ hybridization of enzymes and their metal–organic framework analogues with enhanced activity and stability by biomimetic mineralisation

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Abstract

By incorporating Cytochrome c (peroxidase, Cyt c) into a skeleton of its corresponding synthetic MOF analogue (peroxidase mimic, CuBDC), approximately 12-fold catalytic efficiency (kcat/KM) enhancement is observed compared to free Cyt c. Meanwhile, the shield endowed by CuBDC prevents encapsulated enzymes from deactivation by trypsin digestion, thermal treatment and long-term storage in vitro. This concept of combining enzymes and their MOF mimics with enhanced enzymatic activity and stability may provide new insights into the design of highly active, stable enzyme–MOF composite catalysts and holds promise for applications in biocatalysis, biosensing and drug delivery systems.

Graphical abstract: In situ hybridization of enzymes and their metal–organic framework analogues with enhanced activity and stability by biomimetic mineralisation

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Publication details

The article was received on 24 Aug 2017, accepted on 20 Sep 2017 and first published on 20 Sep 2017


Article type: Communication
DOI: 10.1039/C7NR06315F
Citation: Nanoscale, 2017,9, 15298-15302
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    In situ hybridization of enzymes and their metal–organic framework analogues with enhanced activity and stability by biomimetic mineralisation

    Z. Li, H. Xia, S. Li, J. Pang, W. Zhu and Y. Jiang, Nanoscale, 2017, 9, 15298
    DOI: 10.1039/C7NR06315F

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