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Journal of Materials Science
Erschienen in: Journal of Materials Science 12/2018

13.03.2018 | Biomaterials

The oxidase-like activity of hemin encapsulated by single-ring GroEL mutant and its application for colorimetric detection

verfasst von: Xiaoqiang Wang, Baomei Xu, Zhenzhen Liu

Erschienen in: Journal of Materials Science | Ausgabe 12/2018

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Abstract

Supramolecular anchoring of metalloporphyrins in a protein is an attractive approach to the generation of artificial enzymes. Here, we employ the hydrophobic nanocage of single-ring mutant of bacterial GroEL protein for this purpose. We found that multiple monomeric hemin cofactors can be efficiently loaded into the protein nanocage. The as-prepared biohybrid possessed an oxidase-like catalytic activity and followed the typical Michaelis–Menten kinetics and a ping-pong mechanism in the H2O2-mediated oxidation of model substrates. In comparison with natural peroxidase, the artificial enzyme exhibited higher affinity for the model substrate. A simple and sensitive colorimetric method for the quantitative detection of H2O2 and glucose was also developed based on the artificial enzyme, with the detection limits determined to be 3.0 μM for H2O2 and 5.0 μM for glucose, respectively. The protein nanocage-based artificial enzyme is very flexible and is envisioned to be adapted readily for binding other metal complexes and catalysis of other reactions.
Vorheriger Artikel Synthesis of bactericidal polymer coatings by sequential plasma-induced polymerization of 4-vinyl pyridine and gas-phase quaternization of poly-4-vinyl pyridine
Nächster Artikel Cell attachment/detachment behavior on poly(N-isopropylacrylamide)-based microgel films: the effect of microgel structure and swelling ratio

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Metadaten
Titel
The oxidase-like activity of hemin encapsulated by single-ring GroEL mutant and its application for colorimetric detection
verfasst von
Xiaoqiang Wang
Baomei Xu
Zhenzhen Liu
Publikationsdatum
13.03.2018
Verlag
Springer US
Erschienen in
Journal of Materials Science / Ausgabe 12/2018
Print ISSN: 0022-2461
Elektronische ISSN: 1573-4803
DOI
https://doi.org/10.1007/s10853-018-2215-6

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