Kinetic studies of the enzymatic hydrolysis of molasses were conducted using glucoamylase. Central Sugar Refinery SDN BHD contains 13-20% glucose. The molasses was diluted and the kinetic experiments were conducted at 67 degrees C with 100-1000 mg/l of glucoamylase. The glucose contents of the molasses were enhanced after hydrolysis of molasses solution with 1000 mg/l glucoamylase. A Lineweaver-Burk plot was obtained based on enzyme kinetic data. The rate constant, Km and maximum reaction rate, Vmax for 500 mg/l of glucoamylase were 100 mmol/l (18 g/l) and 5 mmol/l min (0.9 g/l min), respectively. The maximum reaction rate, Vmax for 1000 mg/l of glucoamylase was doubled, to 100 mmol/l (18 g/l) and the rate constant, Km was the same for 500 mg/l of glucoamylase. The substrate inhibition model was noncompetitive based on the resulting Lineweaver-Burk plot for enzyme concentration of 500 and 1000 mg/l.