食品科学 ›› 2013, Vol. 34 ›› Issue (9): 52-55.doi: 10.7506/spkx1002-6630-201309012

• 基础研究 • 上一篇    下一篇

核桃蛋白源血管紧张素转化酶抑制剂的分离纯化

顾 欣1,2,李 迪3,侯雅坤1,2,崔 洁1,2,王建中1,2,*   

  1. 1.北京林业大学生物科学与技术学院,北京 100083;2.林业食品加工与安全北京市重点实验室,北京 100083;
    3.河北化工医药职业技术学院,河北 石家庄 050026
  • 收稿日期:2012-08-28 修回日期:2013-03-13 出版日期:2013-05-15 发布日期:2013-05-07
  • 通讯作者: 王建中 E-mail:w62338221@163.com
  • 基金资助:

    北京市科委科技创新基地培育与发展工程项目(Z121106002812037);国家林业公益性行业科研专项(201004081)

Separation and Purification of Angiotensin Ⅰ-Converting Enzyme Inhibitor from Walnut Protein

GU Xin1,2,LI Di3,HOU Ya-kun1,2,CUI Jie1,2,WANG Jian-zhong1,2,*   

  1. 1. College of Biological Sciences and Technology, Beijing Forestry University, Beijing 100083, China;
    2. Beijing Key Laboratory of Forest Food Processing and Safety, Beijing 100083, China;
    3. Hebei Chemical and Pharmaceutical College, Shijiazhuang 050026, China
  • Received:2012-08-28 Revised:2013-03-13 Online:2013-05-15 Published:2013-05-07

摘要:

从核桃蛋白源的胃蛋白酶水解物中分离纯化出具有高体外血管紧张素转化酶(ACE)抑制活性的抑制剂。利用超滤、凝胶色谱、高效液相色谱等方法进行分离纯化,以体外ACE抑制活性为检测指标,并用N端氨基酸测序鉴定其结构为酪氨酸-谷氨酸-脯氨酸(Tyr-Glu-Pro,YEP),对筛选出的抑制剂进行体外模拟消化稳定性研究。结果表明,胃蛋白酶酶解液通过纯化所得ACE抑制剂的IC50值为0.32μg/mL,该ACE抑制剂在经过体外模拟消化后仍保持良好的ACE抑制活性。

关键词: 血管紧张素转化酶, 胃蛋白酶, 纯化, 分离, 核桃蛋白

Abstract:

An angiotensin Ⅰ-converting enzyme (ACE) inhibitor was separated and purified from pepsin hydrolysate of
walnut protein by ultrafiltration, gel permeation chromatography and HPLC. The inhibitory activity and in vitro digestive
stability of the ACE inhibitor were examined. Its structure was identified through N terminus amino acid sequencing as Tyr-
Glu-Pro. The IC50 of this inhibitor derived from walnut protein was 0.32 μg/mL. This activity was well maintained after
simulated digestion in vitro.

Key words: angiotensin Ⅰ-converting enzyme (ACE), pepsin, purification, separation, walnut protein

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