Issue 1, 2019

Immobilization of enzymes on an organic–inorganic hybrid network consisting of Dawson-type polyoxotungstate and a zinc(ii)-biimidazole complex moiety

Abstract

A new polyoxometalate (POM)-based organic–inorganic hybrid compound, {[(Zn(H2biim)2)3(P2W18O62)]·6H2O}n (1) (H2biim = 2,2′-biimidazole), has been hydrothermally synthesized and characterized by physico-chemical and spectroscopic methods. The structure of compound 1 exhibits a two-dimensional (2-D) network character, in which each Dawson-type polyoxoanion [P2W18O62]6− ({P2W18}) is connected with six [Zn(H2biim)2]2+ ({Zn(II)-H2biim}) complex fragments, while each {Zn(II)-H2biim} unit bridges two {P2W18} clusters, forming a 2-D network with a (6,3)-net topology. Compound 1 shows high enzyme-immobilizing capability for horseradish peroxidase (HRP). The maximum HRP load is 90.1 mg g−1 under optimal conditions. Furthermore, the immobilized enzyme (HRP/1) exhibits high catalytic activity and good stability, which can be applied to detect trace amounts of H2O2 in solution with a low detection limit of 3.11 × 10−3 mmol L−1.

Graphical abstract: Immobilization of enzymes on an organic–inorganic hybrid network consisting of Dawson-type polyoxotungstate and a zinc(ii)-biimidazole complex moiety

Supplementary files

Article information

Article type
Paper
Submitted
29 Jul 2018
Accepted
12 Nov 2018
First published
13 Nov 2018

New J. Chem., 2019,43, 146-153

Immobilization of enzymes on an organic–inorganic hybrid network consisting of Dawson-type polyoxotungstate and a zinc(II)-biimidazole complex moiety

H. Zhu, J. Du, Y. Lu, F. Su and Y. Li, New J. Chem., 2019, 43, 146 DOI: 10.1039/C8NJ03776K

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