Zou_2020_Colloids.Surf.B.Biointerfaces_195_111275

A novel integrated lipase nanogel based on functional ionic liquid modification and polymerization immobilization with improved stability was designed. Characterization before and after modification and polymerization was conducted using infrared spectroscopy, Circular dichroism spectroscopy, fluorescence spectroscopy, and scanning electron microscopy. It was shown that the modification of the ionic liquid influenced the catalytic behavior of lipase significantly due to the changed structure and surface properties of lipase. The enzymatic properties, including acid-base stability, thermal stability, organic solvents stability, and storage stability of CRL nanogel, were investigated in the p-nitrophenyl palmitate hydrolysis reaction (CRL, Lipase from Candida Rugosa). The results indicated that CRL nanogel has a better pH, heat, and organic solvent tolerance after immobilization. After seven weeks of storage, the natural CRL gradually lost its enzymatic activity, and only 17.5+/-1.7 % of the catalytic activity remained, the residual activity of CRL nanogel was 97.3+/-1.8 %. It was indicated that the novel CRL nanogel was an excellent biocatalyst.