Abstract
Oxidoreductases are widely recognized for their capability to degrade phenolic pollutants and versatile. However, the lack of enzyme stability makes this technique unrealistic for industrial applications. In order to enhance their catalytic activity, stability and reusability, oxidoreductases namely laccases and peroxidases were entrapped in sol–gel silica and their catalytic activities were measured by an enzymatic assay using 2,6-dimethoxyphenol and guaiacol as substrates, respectively. The sol–gel silica matrices acted as a polymeric framework around the enzyme is a promising tool for improving enzyme stability. After entrapment, the catalytic activity and stability of sol–gel laccase and peroxidase toward pH, temperature and storage duration remarkably enhanced.
Highlights
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The enzyme immobilization using novel sol-gel method is a promising method for improving enzyme catalytic activity and stability.
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After entrapment, the catalytic activity and stability of the immobilized laccase and immobilized peroxidase towards pH, temperature and storage time are significantly improved.
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Oxidoreductase entrapment in sol-gel silica-based matrix shows a bright future for the use of immobilized enzyme in vast industrial process particularly removal of dye from wastewater treatment.
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The authors would like to acknowledge the financial support from the Ministry of Higher Education (MOHE), Malaysia under the Fundamental Research Grant Scheme (FRGS Project No. 78213).
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Mohidem, N.A., Bin Mat, H., Mohamad, M. et al. Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases. J Sol-Gel Sci Technol 98, 462–469 (2021). https://doi.org/10.1007/s10971-021-05522-0
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DOI: https://doi.org/10.1007/s10971-021-05522-0