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The immobilization of Amano Lipase A from Aspergillus niger by adsorption onto Stöber silica matrix obtained by sol-gel method was studied. The effectiveness of the enzyme immobilization and thus the usefulness of the method was demonstrated by a number of physicochemical analysis techniques including Fourier Transform Infrared Spectroscopy (FT-IR), elemental analysis (EA), thermogravimetric analysis (TG), porous structure of the support and the products after immobilization from the enzyme solution with various concentration at different times. The analysis of the process’ kinetics allowed the determination of the sorption parameters of the support and optimization of the process. The optimum initial concentration of the enzyme solution was found to be 5 mg mL-1, while the optimum time of the immobilization was 120 minutes. These values of the variable parameters of the process were obtained by as ensuring the immobilization of the largest possible amount of the biocatalyst at

Immobilization of Amano Lipase A onto Stöber silica surface: process characterization and kinetic studies