Peptide with angiotensin I-converting enzyme inhibitory activity from hydrolyzed corn gluten meal |
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Authors: | Yang Yanjun Tao Guanjun Liu Ping Liu Jia |
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Institution: | School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, 214122, PR China. yangyj2005@hotmail.com |
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Abstract: | Corn gluten meal (CGM) was hydrolyzed by Alcalase after starch removal of CGM was applied as a pretreatment. A new inhibitory peptide for angiotensin I-converting enzyme (ACE) was isolated from the hydrolysate of CGM with the use of Bio-Rad P-2 gel filtration and followed by reverse-phase high-performance liquid chromatography (RP-HPLC). The sequence of the active peptide was determined to be Ala-Tyr after the application of amino acid analysis and HPLC/MS. The IC50 of the peptide was 14.2 microM, and it was not affected by preincubation with 30 mU of ACE at 37 degrees C for 3 h. Ala-Tyr also exerted antihypertensive effects after oral administration to spontaneously hypertensive rats. A maximal reduction of systolic blood pressure of 9.5 mmHg was observed 2 h after oral administration of Ala-Tyr at doses of 50 mg/kg. |
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