Organic–Inorganic Hybrid Nanocomposites: A Novel Way to Immobilize l-Glutamate Oxidase with Manganese Phosphate
Autor: | Yan Chen, Xinrui Hao, Qingling Wang, Chu Xiaohe, Yuchi Lu, Pengfu Liu |
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Rok vydání: | 2019 |
Předmět: |
chemistry.chemical_classification
Oxidase test Nanocomposite Polymers and Plastics Immobilized enzyme Bioconversion 02 engineering and technology 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences 0104 chemical sciences Enzyme catalysis Enzyme chemistry Chemical engineering Materials Chemistry Fourier transform infrared spectroscopy 0210 nano-technology L-glutamate oxidase |
Zdroj: | Journal of Inorganic and Organometallic Polymers and Materials. 30:1686-1694 |
ISSN: | 1574-1451 1574-1443 |
Popis: | $$\alpha$$-Ketoglutaric acid is a versatile chemical. Traditional methods for producing $$\alpha$$-ketoglutaric acid rely on certain some enzymes, but these methods have disadvantages related to difficult separation and high costs. Therefore, it is necessary to make improvements based on the original route. The novel immobilized enzyme, nanocomposite is a relatively superior method. Manganese-l-glutamate oxidase hybrid nanocomposites (Mn-LGOX) were obtained, characterized and optimized in terms of their structural and enzymatic properties. Field emission scanning electron microscopy (FE-SEM), Fourier transform infrared spectroscopy (FTIR) and X-ray diffraction (XRD) assays were used to discover and confirm that l-glutamate oxidase (LGOX) was successfully assembled with manganese phosphate. In addition, the nanocomposites exhibited improved resistance to temperature and pH and increased recyclability compared to the earlier free enzyme catalyst method. After recycling six times, the activity of the nanocomposites was maintained over 30% more compared to the original more. In short, the hybrid nanocomposites ideally improve the structural character, the resistance to pH and temperature in the reaction and the storage stability. These data emphasize that Mn-LGOX nanocomposites show great potential for industrial bioconversion |
Databáze: | OpenAIRE |
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