Purification and Identification of Angiotensin I-Converting Enzyme Inhibitor from Morokheiya (Corchorus olitorius)

Abstract

In order to invesigate another function such as food in Morokheiya, the angiotensin-converting enzyme (ACE) inhibitor was extracted with 80% ethanol from the leaves of Morokheiya (Corchorus olitorious). The extract was dried, dissolved in water, defatted with ether and decolored with activated carbon. The ACE inhibitor was purified by successive ion-exchange chromatography, Amberlite IR-120B, Dowex 50W-X8 and Dowex 1-X4, respectively. The ACE inhibitor was further purified by silica gel column chromatography and finally purified and isolated by high performance liquid chromatography (HPLC) on Asahipak NH2P-50. The ACE inhibitor showed a positive ninhydrin reaction and no significant absorbance. The present ACE inhibitor was identified as Nicotianamine based on the comparative study using amino acid analyzer, TLC and capillary electrophoresis.