食品科学 ›› 2005, Vol. 26 ›› Issue (8): 185-188.

• 工艺技术 • 上一篇    下一篇

酪朊酸钠制备ACE抑制肽的研究(英文)

 徐鑫, 赵谋明, 王金水, 杨晓泉   

  1. 华南理工大学轻工与食品学院
  • 出版日期:2005-08-15 发布日期:2011-09-19

Angiotensin-I-converting Enzyme Inhibitory Peptides from Tryptic Hydrolysates of Sodium Caseinate

 XU  Xin, ZHAO  Mou-Ming, WANG  Jin-Shui, YANG  Xiao-Quan   

  1. Light Industry and Food Engineering Institute, South China University of Technology
  • Online:2005-08-15 Published:2011-09-19

摘要: 采用商业化的胰蛋白酶对底物浓度为10%的酪朊酸钠进行可控酶解,将酶解液的上清液经截留分子量为10ku的超滤膜分离后利用紫外分光光度法测定各组分ACE体外抑制活性,结果表明酪朊酸钠的胰蛋白酶酶解液具有较强的ACE抑制活性,超滤分离可提高产品的ACE体外抑制活性,为开发新一代降血压保健食品提供广阔的前景。

关键词: 酪朊酸钠, 胰蛋白酶水解物, 高效体积排阻色谱(HPSEC), 超滤, ACE抑制肽

Abstract: Sodium caseinate contained peptidic angiotensin I-converting enzyme (ACE) inhibitors, which were released during hydrolysis by trypsin. The molecular mass distributions of the hydrolysates were identified by high performance size exclusion chromatography (HPSEC). ACE-inhibitory peptides were separated by ultrafiltration in terms of molecular weight. The ACE inhibitory activity of the permeates was IC50=0.42 mg/ml.Ultrafiltration was a effective tool for purification the hydrolysates to obtain thigh ACE-inhibitory activity peptides.

Key words: sodium caseinate, tryptic hydrolysates, HPSEC, ultrafiltration, ACE-inhibitor