FOOD SCIENCE ›› 2011, Vol. 32 ›› Issue (19): 120-124.doi: 10.7506/spkx1002-6630-201119027

• Bioengineering • Previous Articles     Next Articles

A Method for Screening Angiotensin I Converting Enzyme Inhibitory Peptides

JIN Qing1，WU Jian-ping2， ZHANG Gui-chuan3，DENG Ya-fei4，YUAN Lu-jiang1,*   

  1. (1. Key Laboratory on Luminescence and Real-Time Analysis, Ministry of Education, Southwest University, Chongqing 400715, China； 2. Department of Human Ecology, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada； 3. College of Food Science, Southwest University, Chongqing 400716, China； 4. College of Pharmaceutical Sciences, Southwest University, Chongqing 400716, China)
  • Published:2011-10-12

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Abstract: A rapid and highly efficient method for identifying angiotensin I converting enzyme inhibitory peptides from protein hydrolysates was established based on quantitative structure activity relationship (QSAR) and protein sequence. First, a small peptide library was constructed by protein sequence searching according to the hydrolysis sites of a specific enzyme. Then, the activities of peptides in the library were predicted using QSAR model. Target peptides were synthesized and their IC50 values were measured. Finally, a real protein hydrolysate was prepared and HPLC was employed to analyze the target peptides in the hydrolysates. Totally 34 tripeptides with an IC50 of less than 10 μmol/L were predicted from rapeseed protein, wheat protein and rice protein and 11of them with higher activity were synthesized. LRL with the lowest IC50 of 3.42μmol/L located in rapeseed cruciferin BNC1 (P33523) sequence 347-349 was characterized from the synthesized peptides.

Key words: ACE inhibitor, quantitative structre activity relationship(QSAR), activity prediction, rapeseed protein, wheat protein, rice protein

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