Kinetic study of free and immobilized enzymes for bioconversion of tapioca slurry into BioSugar

This paper highlights the kinetic parameter of the free and immobilized enzymes (alpha-amylase, glucoamylase and cellulase) systems. The kinetic parameters were calculated using Lineweaver-Burk plot. The Michaelis constant (K_m) of free alpha-amylase, glucoamylase and cellulase were 4.542, 1.069 and 9.082 mg/mL, respectively. For the immobilized enzymes (alphaamylase, glucoamylase and cellulase), the K_m values were 4.488, 2.196, 6.309 mg/mL, respectively. In general, the results showed immobilized alpha-amylase performed better compared to free alpha-amylase. However, for glucoamylase the K_m value doubled which indicated the affinity reduction of enzyme towards the substrate. The affinity of immobilized alpha-amylase and cellulase were equal or better than the free alpha-amylase and cellulase. The overall results for immobilized enzymes system showed that glucoamylase has higher affinity towards the substrate followed by alpha-amylase and cellulase. Therefore, the immobilized enzymes system has high potential for bioconversion of tapioca slurry into glucose.