Biology

High-performance liquid chromatography

Angiotensin-converting enzyme

Rice protein

Chromatography

Peptide

Endocrinology

Antiretroviral therapy

Inhibitory postsynaptic potential

Hydrolysate

Biochemistry

Viral load

Food science

Protease inhibitor (pharmacology)

Immunology

Blood pressure

Protease

Renin–angiotensin system

Human immunodeficiency virus (HIV)

Enzyme

Hydrolysis

Chemistry

Size-exclusion chromatography

Journal of the Science of Food and Agriculture

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 C 18 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

Utilisation of chickpea protein isolates for production of peptides with angiotensin I‐converting enzyme (ACE)‐inhibitory activity