In order to master the enzymatic hydrolysis characteristics of buckwheat starch by fungal-α-amylase, the effects of substrate concentration, enzymatic concentration, pH value and temperature on reaction velocity were determined. The kinetics of the hydrolysis reaction were described with the Michaelis-Menten equation, and the kinetic parameters were calculated by the Lineweaver-Burk and Wilkinson methods. The results show that buckwheat starch hydrolysis by fungal-α-amylase obeys the classical first-order reaction rate, and the kinetics can be modeled by Michaelis-Menten equation. In the condition of 55℃ and pH 5.5, the Minchaeli constant(K_m) and maximum rate(V_m) for 0.5 U/mL of fungal-α-amylase are 5.470 mg/mL and 1.587 mg/(mL·min). The kinetic model, including the parameters such as substrate concentration, enzymatic concentration and temperature, is suit for the hydrolysis under the temperature range from 303.15 K to 333.15 K.