Kinetics of the surface hydrolysis of raw starch by glucoamylase

The hydrolysis of raw starch catalyzed by glucoamylase has been studied with starch granules of different sizes by use of an amperometric glucose sensor by which the direct and continuous observation of the concentration of glucose can be achieved even in a thick raw starch suspension. The initial rate of the enzymatic hydrolysis in the raw starch suspension increased with increasing concentration of the enzyme to approach a saturation value and was proportional to the amount of substrate. Also, the rate was proportional to the specific surface area of the substrate. The experimental results can be explained Well by the rate equations derived from a three-step mechanism, which consists of adsorption of the free enzyme onto the surface of the substrate, reaction of the adsorbed enzyme with the substrate, and liberation of the product.