FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (11): 189-193.doi: 10.7506/spkx1002-6630-200911042

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Study on Preparation of Angiotensin I-converting Enzyme (ACE) Inhibitory Peptide from Oat Protein by Enzymatic Hydrolysis

ZHANG Xiao-ping1,ZHAO Shi-feng2,JIANG Qiong1,DONG Yin-mao1,LIU Yong-guo1,REN Qing1,*   

  1. (1. Beijing Key Laboratory of Plant Resources Research and Development, Beijing Technology and Business University, Beijing
    100037, China;2. Zhangjiakou Academy of Agricultural Sciences, Zhangjiakou 075000, China)
  • Received:2008-10-10 Revised:2009-01-08 Online:2009-06-01 Published:2010-12-29
  • Contact: REN Qing1,* E-mail:renqing1349@sina.com

Abstract:

Oat protein was hydrolyzed by Alcalase, Neutrase, and Protamex individually or jointly and the obtained hydrolysates were further subjected to decolorization with activated carbon YD-303 and purification with macroporous adsorption resin DA201-C II for desalination and Sephadex G-25 column for fractionation. The results showed that the hydrolysates of oat protein by individual Alcalase had the highest ACE inhibitory activity of 85.40%. The optimum decolorization conditions with YD-303 contained quantity of activated carbon 1.5%, pH 3.5, 40 ℃, and adsorption time 75 min. Fractions eluted with 75% ethanol from macroporous adsorption resin displayed the highest inhibitory activity and were further separated by Sephadex G-25 into 4 subfractions. The fourth subfraction presented the most effective elution and its inhibitory activity was 95.6%.

Key words: oats protein, enzymatic hydrolysis, ACE inhibitory peptide, decolorization, desalination

CLC Number: