Abstract
TEMPO or Anchoring 2,2,6,6-tetra-methylpiperidine-1oxyl radical into the nanospaces a fibre of phosphosilicate with laccase compound causes an unheard potent to be producing which called bifunctional nanocatalyst (TEMPO@FPS-laccase). TEMPO@FPS-laccase indicated proper catalytic activity for synthesis of β-oxopropylcarbamates in aqueous medium without any pollutants through a multi component coupling of CO2, amines and propargyl alcohols in moderate condition. Free laccases may not be recovered but can be easily disabled in different environmental conditions. Enzyme immobilization is known as an expanding way to enhance resistor to extreme conditions and stability as well as recycled of laccase.
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Acknowledgements
The study was supported by “Natural Science Foundation of Shandong Province (Grant Nos. ZR201702200464, ZR2019QB013)” and “Science and Technology Development Plan Project of Zaozhuang City (Grant No. 2019GX07)”.
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Fan, L., Wang, J., Zhang, X. et al. Co-immobilization of Laccase and TEMPO onto Glycidyloxypropyl Functionalized Fibrous Phosphosilicate Nanoparticles for Fixing CO2 into β-Oxopropylcarbamatesin. Catal Lett 149, 3465–3475 (2019). https://doi.org/10.1007/s10562-019-02894-5
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DOI: https://doi.org/10.1007/s10562-019-02894-5