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Utilisation of chickpea protein isolates for production of peptides with angiotensin I‐converting enzyme (ACE)‐inhibitory activity
Author(s) -
Pedroche Justo,
Yust María M,
GirónCalle Julio,
Alaiz Manuel,
Millán Francisco,
Vioque Javier
Publication year - 2002
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.1126
Subject(s) - hydrolysate , protease , chemistry , enzyme , size exclusion chromatography , hydrolysis , chromatography , angiotensin converting enzyme , peptide , biochemistry , rice protein , high performance liquid chromatography , protease inhibitor (pharmacology) , renin–angiotensin system , biology , human immunodeficiency virus (hiv) , antiretroviral therapy , blood pressure , viral load , immunology , endocrinology
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