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Alpha-amylase inhibitor extracted from different sources i.e.wheat grains (sohag 2 and Giza 164),legume seeds such as Cow pea (Carim 7 and Giza 3),and Kidney bean (Giza 6 and Giza 133) was purified and tested for activity using human salivary and pancreatic alpha-amylase.Results showed that the alpha-amylase inhibitor activity from samples studied were 120 to 285 unit / mg protein.The inhibitor was found to be stable at pH range from 2 to 4.It was also stable to digestion by proteolytie enzymes (pepsin and trypsin).