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Isolation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Rice Bran Proteins and Evaluation of Activity and Stability

Isolation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Rice Bran Proteins and Evaluation of Activity and Stability

Boxin Dou, Ying Liu*, Yumeng Liu, Lili Fan, Yongqiang Ma, and Yanguo Shi

College of Food Science and Engineering, Harbin University of Commerce, Heilongjiang 150076, China

*     Corresponding author: 101724@hrbcu.edu.cn

 

ABSTRACT

The aim of this study was to investigate anti angiotensin I converting enzyme (ACE) activity of the rice bran (RB) and comparison of its activity with selected commercial antihypertensive pharmaceutical. A new peptide with ACE inhibition properties was obtained by using alkaline protease to enzymatic hydrolysis of RB crude protein purified by ultrafiltration, size exclusion chromatography and RP-HPLC. Using consecutive chromatographic techniques successively, the acidic hydrolysates of RB proteins were fractionated and the new ACE inhibitory triplet was isolated and identified. The amino acid sequence of the ACEI was identified as Ile-Thr-Leu or Leu-Thr-Ile. In vitro, ACE inhibition assays showed that the IC50 value of the peptide was 0.0118 mg.ml-1. The inhibitory activity of the peptide slightly increased after incubation with gastrointestinal proteases. It was revealed that the ACE inhibiting activity of isolated peptide was lower than that of e nalapril maleate, however, higher than that of all the other antihypertensive pharmaceutical tested. Moreover, the peptide with stable and strong ACEI activity has the potential application in functional and novel foods, dietary supplements or even pharmaceuticals as an antihypertensive agent.
 

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Pakistan Journal of Zoology

December

Vol. 52, Iss. 6, Pages 2027-2426

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