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Polymer-templated supramolecular co-assemblies of proteins and metal oxide clusters as versatile platform for chemo-enzymatic catalysis
- Source :
- Journal of Colloid and Interface Science. 594:874-881
- Publication Year :
- 2021
- Publisher :
- Elsevier BV, 2021.
-
Abstract
- The hybridization of enzymes and inorganics in controlled manner is challenging, however, critical for the development of chemo-enzymatic cascade catalyst with high efficiency and selectivity. Here, proteins and metal oxide clusters can be facilely co-assembled on the surface of colloid of poly(4-vinylpyridine) (P4VP) via hydrogen bonding, due to their enriched surface hydrogen bonding donors. The co-assembly method can be generally applied for preparing chemo-enzymatic catalyst within the selected database of various proteins and metal oxide clusters while the assembly units retain their structures and activities. Typically, a 2.5 nm metal oxide cluster {Mo72Fe30}, with peroxidase-like activity, are complexed with glucose oxidase (GOX) on P4VP for the catalysis against the oxidization of o-dianisidine (ODA) with the existence of glucose. Due to the synergistic effects of chemical and enzymatic catalysis, the co-assemblies show even higher ODA oxidation activity compared to GOX/catalase bi-enzymatic system, confirming the effectiveness of the co-assembly protocol for cascade catalysis and enabling its applications in rapid glucose detection and biomass conversion.
- Subjects :
- Polymers
Supramolecular chemistry
Oxide
02 engineering and technology
010402 general chemistry
01 natural sciences
Catalysis
Enzyme catalysis
Biomaterials
Metal
Glucose Oxidase
chemistry.chemical_compound
Colloid and Surface Chemistry
Glucose oxidase
chemistry.chemical_classification
biology
Hydrogen bond
Oxides
Polymer
021001 nanoscience & nanotechnology
Combinatorial chemistry
0104 chemical sciences
Surfaces, Coatings and Films
Electronic, Optical and Magnetic Materials
chemistry
visual_art
visual_art.visual_art_medium
biology.protein
0210 nano-technology
Oxidation-Reduction
Subjects
Details
- ISSN :
- 00219797
- Volume :
- 594
- Database :
- OpenAIRE
- Journal :
- Journal of Colloid and Interface Science
- Accession number :
- edsair.doi.dedup.....c7fe9780183888ea08369724518135b8