食品科学 ›› 2008, Vol. 29 ›› Issue (4): 249-252.

• 生物工程 • 上一篇    下一篇

酪蛋白源降血压肽稳定性及其抑制作用机理的研究

 姜瞻梅, 吴刚, 刘丽波, 田波, 霍贵成   

  1. 乳品科学教育部重点实验室 东北农业大学食品学院; 乳品科学教育部重点实验室; 东北农业大学食品学院;
  • 出版日期:2008-04-15 发布日期:2011-08-24

Study on Stablization and Inhibitory Mechanism of Antihypertensive Peptide Derived from Bovine Casein

 JIANG  Zhan-Mei, WU  Gang, LIU  Li-Bo, TIAN  Bo, HUO  Gui-Cheng   

  1. Key Laboratory of Dairy Science, Ministry of Education, College of Food Science and Technology, Northeast Agricultural University
  • Online:2008-04-15 Published:2011-08-24

摘要: 酪蛋白源降血压肽经体外胃肠道蛋白酶消化后,其ACE抑制活性仍能保持原来活性的94%。降血压肽与ACE作用前后,其ACE抑制活性和肽谱基本保持不变,证实了酶解乳蛋白源降血压肽是真正的抑制剂类型,不受ACE作用。采用抑制酶解动力学方法,初步探讨降血压肽的抑制作用机理,根据lineweaver-Burk方程,确定酶解酪蛋白源降血压肽是非竞争性抑制类型。

关键词: 降血压肽, 稳定性, 抑制机理

Abstract: In vitro simulation experiment and peptide analysis showed that angiotensin converfing enzyme (ACE) inhibitory activity still contains 94% of initiall activity after antihypertensive peptide digestion with pepsin and trypsin.This also showed that these peptides survive the degradation by gastronintestinal proteinases and peptdases.After antihypertensive peptide reaction with angiotensin converting enzyme, there are very little changes in the ACE inhibitory activity and peptide chromatography. This proved that the antipertensive peptide is the true inhibitor. Antihypertensive inhibitory mechanism was studied by the enzyme inhibition dynamics.This also showed that the antipertensive peptide is of non-competition inhibition according to Lineweaver-Burk equation.

Key words: antihypertensive peptide, stablization, inhibitory mechanism