The aim of the work was to contribute to the understanding of the roles played by specific binding interactions and electrostatic effects of the catalytic sites of αamylase from Lactobacillus plantarum, which reacts with maltoheptaose. The αamylases (E.C.3.2.1.1) from glycoside hydrolase family 13 (GH13) are one of the most important and oldest industrial enzymes. Amylasesare enzymes which hydrolyze the starch molecules into polymers composed of glucose units. Although amylases be derived from several sources, including plants, animals and microorganisms. However, enzymes from fungal and bacterial sources have dominated applications in industrial sectors. Amylolytic lactic acid bacteria (ALAB) utilize starchy biomass and convert into lacticacid in single step fermentation. Only minority of lactic acid bacterial species have the capacity to produce hydrolysis enzymes. A strain L. plantarum was found to produce amylase enzyme. The results indicated that homology based approach for predicting the three dimensional (3D) structures of αamylase from L. plantarum using αamylase Amy 2 as start structure as templatesshowed a very similar structure as expected from the high sequence identity. Moreover alignment studies raised amino acid substitutions in αamylase from L. plantarum compare to αamylase from Bacillus subtilis which may affect the αamylase putative active site leading to the formation of an extra hydrogen bond between Asp171, Glu200, Asp277 and Asp176, Gln 208,Asp269, respectively. The interactions between αamylase from L. plantarum and maltoheptaose were predicted by flexible docking including minimization. Further investigations are underway to explore the positions binding site of αamylase complexed with maltoheptaose.