Improved catalytic hydrolysis of carboxy methyl cellulose using cellulase immobilized on functionalized meso cellular foam

Cellulase from Penicillium funiculosum was immobilized on functionalized MCF (Meso Cellular Foam) silica by imine bond formation followed by reduction using NaBH(4). The specific activities of free and immobilized enzyme were measured for hydrolysis of soluble carboxymethyl cellulose (CMC). The highest activity of MCF immobilized and native enzyme was obtained at optimum pH 5 and 4.5 respectively. Kinetic parameters, Michaelis-Menten constant (Km) and maximum reaction velocity (Vmax), were calculated as Km = 0.025 X 10(-2) mg/mL, Vmax = 5.327 X 10(-3) U/mg for the free enzyme and Km = 0.024 X 10(-2) mg/mL, Vmax = 9.794 X 10(-3) U/mg for MCF immobilized enzyme respectively. The reusability of immobilized enzymes showed that 66% of its activity is retained even after 15 cycles. The availability of polar groups (-NH-, -OH) and large pore size of surface modified MCF could be electrostatically stabilizing the cellulase. Functionalized MCF was found to be a promising material for stabilizing cellulase with 16.4 wt% loading of enzyme.