食品科学 ›› 2010, Vol. 31 ›› Issue (24): 222-229.doi: 10.7506/spkx1002-6630-201024048

• 工艺技术 • 上一篇    下一篇

燕麦ACE 抑制肽的分离纯化及其活性研究

王 双1,2,王昌涛1,*,韩 扬1   

  1. 1.北京工商大学 植物资源研究开发重点实验室
    2.黑龙江中医药大学药学院
  • 收稿日期:2010-08-30 出版日期:2010-12-25 发布日期:2010-12-29
  • 通讯作者: 王昌涛1 E-mail:wangct@th.btbu.edu
  • 基金资助:

    北京市科技新星项目(2008B08)

Separation, Purification and Activity of ACE Inhibitory Peptides from Oat

WANG Shuang1,2,WANG Chang-tao1,*,HAN Yang1   

  1. Beijing Technology and Business University, Beijing Key Laboratory of Plant Resources Research and Development, Beijing
    100048, China;2. College of Pharmaceutical, Heilongjiang University of Chinese Medicine, Harbin 150040, China
  • Received:2010-08-30 Online:2010-12-25 Published:2010-12-29
  • Contact: WANG Chang-tao1 E-mail:wangct@th.btbu.edu

摘要:

通过对3 种大孔吸附树脂的比较,选择DA201-C 树脂对燕麦ACE 抑制肽进行纯化。纯化后的燕麦肽产物的ACE 抑制率达到92.86%,利用HPLC 测得纯化后燕麦ACE 抑制肽的分子质量分布在240.10~1292.11D 之间,这部分物质在整个纯化产物中占99.82%。采用SephadexG-15 凝胶分离燕麦ACE 抑制肽得到D峰,其IC50 为0.103mg/mL,分子质量545D。采用大孔吸附树脂及凝胶层析法能够较好地分离纯化燕麦ACE 抑制肽。

关键词: 燕麦, ACE 抑制肽, 大孔吸附树脂, 凝胶层析

Abstract:

Through comparing three kinds of macroporous resins, DA201-C resin was selected to purify ACE inhibitory peptides from oat. The ACE inhibition rate of purified peptide from oat was 92.86%. The molecular mass of HPLC-purified oat ACE inhibitory peptides was the range of 240.10-1292.11 D. SephadexG-15 gel was used to purify ACE inhibitory peptides to obtain a fraction D with IC50 of 0.103 mg/mL and molecular weight of 545 D. Results indicated that macroporous resin and gel filtration chromatography could better purify ACE inhibitory peptides from oat.

Key words: oat, ACE inhibitory peptide, macroporous resin, gel filtration chromatography

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