ISSN: 0973-7510

E-ISSN: 2581-690X

Shu-juan Jiang, Fang Qian, Xiaowen Shen and Guangqing Mu1
1Department of Food Engineering, Dalian Polytechnic University, Dalian Liaoning – 116 034, P R China.
J Pure Appl Microbiol. 2013;7(Spl. Edn.: November):789-793
© The Author(s). 2013
Received: 04/03/2013 | Accepted: 10/06/2013 | Published: 30/11/2013

Angiotensin-converting enzyme plays an important physiological role in the blood pressure regulation of people, and antihypertensive peptides from natural food have been seen as the hotspots in the physiological bioactive peptides. In the presented work the hydrolysate of bovine casein with high inhibitory activity to angiotensin-converting enzyme (IC50=0.76mg/mL) was produced by alcalase, and its fraction (3-2) with a inhibitory ratio of 93.56% was obtained by the consecutive separation method including ultrafiltration and preparation reverse-phase high performance liquid chromatography. Amino acid sequence analysis by mass spectrography showed the molecular weight of antihypertensive fraction (3-2) was 956 Da and the most probable structure unit is Gly-Ala.


Angiotensin-converting enzyme (ACE), Inhibitory peptide, Bovine casein

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