The control of the hyperglycemia is crucial in the treatment of type II diabetes and other metabolic syndromes. In these situations, the α-amylases could play an important role in the increasing of the blood glucose level due the breakdown of the polysaccharides. The αamylases are the first enzymes, which take a part in the process of the releasing glucose monomers from complex polysaccharides. Therefore, the investigations of both α-amylase activities and the quantity of their inhibition are important on the field of anti-diabetic drug research. Our presented research was aimed to develop a new HPLC based method for the measurement of reaction product of α-amylase reaction using specially synthetized, pnitrophenyl-labelled maltooligomer substrate. After the enzyme reaction, three product was detectable possessing the chromophore-group during the reversed-phase separation. One of them was selected to follow the enzyme kinetic of the human salivary amylase applying linear regression on the area data acquired at different time points of the reaction. Furthermore, due to the specific substrate measuring only the α-amylase activity, our method could be used successfully also for the accurate measurement in the inhibition studies
