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Food Science and Technology International
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Mung-bean Protein Hydrolysates Obtained with Alcalase Exhibit Angiotensin I-converting Enzyme Inhibitory Activity

Guan Hong Li

Guo Wei Le

Huan Liu

School of Food Science and Technology, Southern Yangtze University, 170 Huihe Road, Wuxi, Jiangsu 214036, P.R. China; Key Laboratory of Industrial Biotechnology, Ministry of Education, Southern Yangtze University, 170 Huihe Road, Wuxi, Jiangsu 214036, P.R. China

Yong Hui Shi

School of Food Science and Technology, Southern Yangtze University, 170 Huihe Road, Wuxi, Jiangsu 214036, P.R. China; Key Laboratory of Industrial Biotechnology, Ministry of Education, Southern Yangtze University, 170 Huihe Road, Wuxi, Jiangsu 214036, P.R. Chinalgw{at}sytu.edu.cn

Mung-bean protein isolates were hydrolysed by two proteases alcalase and neutrase commercially available for food industry use, and the angiotensin I-converting enzyme (ACE) inhibitory activities of the enzymatic hydrolysates were measured at different hydrolysis times. The non-hydrolysed protein showed no inhibitory activity. Hydrolysates generated with neutrase displayed very low ACE inhibitory activity, while those obtained with alcalase exhibited high inhibitory activity. The highest ACE inhibitory activity with the IC50 value of 0.64 mg protein/mL was found in the hydrolysate obtained with alcalase at 2h of hydrolysis time. These results indicated that mung-bean protein is a good protein source of ACE inhibitory peptides when hydrolysed with the protease alcalase. The mung-bean protein hydrolysates prepared with alcalase might be utilised for physiologically functional foods with antihypertensive activity.

Key Words: angiotensin I • enzyme inhibitors • bioactive peptides • mung-bean protein • hydrolysates • alcalase • neutrase

Food Science and Technology International, Vol. 11, No. 4, 281-287 (2005)
DOI: 10.1177/1082013205056781
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