Chickpea protein isolates and the protease alcalase were used for the production of protein hydrolysates that inhibit angiotensin I-converting enzyme (ACE). The highest degree of inhibition was found in a hydrolysate obtained by 30 min of treatment with alcalase. This hydrolysate was used as starting material for the purification of ACE-inhibitory peptides. After Biogel P2 gel filtration chromatography and HPLC C18 reverse phase chromatography, four peptides with ACE-inhibitory activity were purified. Two of them were competitive inhibitors of ACE, while the other two were uncompetitive inhibitors. These results show that chickpea proteins are a good source of ACE-inhibitory peptides when hydrolysed with the protease alcalase.
© 2002 Society of Chemical Industry