天然产物研究与开发 ›› 2011, Vol. 23 ›› Issue (2): 295-298.

• 研究简报 • 上一篇    下一篇

胰蛋白酶水解β-乳球蛋白获得ACE抑制肽的条件优化

梅 林,王志耕*,王子龙,薛秀恒   

  1. 安徽农业大学茶与食品科技学院,合肥 230036
  • 收稿日期:2010-12-10 出版日期:2011-04-25 发布日期:2011-10-14
  • 通讯作者: wzhg56@yahoo.com.cn
  • 基金资助:

    科技部科技人员服务企业行动项目(2009JGC30016)

Optimizing Hydrolysis Conditions of β-Lactoglobulin with Trypsin to Obtain the ACE Inhibitory Peptide

MEI Lin, WANG Zhi-geng*, WANG Zi-long, XUE Xiu-heng   

  1. College of Tea & Food Science and Technology of Anhui Agricultural University, Hefei 230036
  • Received:2010-12-10 Online:2011-04-25 Published:2011-10-14

摘要:

采用三因素二次通用旋转设计和体外检测法,对胰蛋白酶水解β-乳球蛋白获得ACE抑制肽的条件进行优化。结果表明,底物浓度(X1)、温度(X2)、酶与底物的质量比(X3)对ACE抑制率的影响回归方程为:Y=50.62–2.33X1–1.97X2+5.81X3–3.36X2X3–6.56X22–1.96X32,胰蛋白酶水解β-乳球蛋白获得ACE抑制肽的最优水解条件为:底物质量浓度为60 g/L,水解温度30 ℃,酶与底物的质量比为5.5%,水解时间6 h,水解产物对ACE抑制活性最大抑制率为53.86%。

关键词: β-乳球蛋白, 胰蛋白酶, ACE

Abstract:

Three-factor quadratic orthogonal rotation design and in vitro assay was adopted to optimize the hydrolysis conditions of β-lactoglobulin with trypsin for obtaining the Angiotensin-I-converting enzyme (ACE) inhibitory peptide. The results showed that the regression equation of the impacts of the substrate concentration (X1),temperature (X2),enzyme,and substrate mass ratio (X3) on the ACE inhibition rate was Y = 50.62–2.33X1–1.97X2+5.81 X3–3. 36X2X3–6.56X22–1.96X32. The optimum conditions were as following: when substrate concentration was at 60 g/L,the hydrolysis temperature at 30 ℃,enzyme and substrate mass ratio at 5.5%,the hydrolysis time in 6 h,the hydrolysis product of ACE inhibitory activity was on the maximal inhibition rate of 53.86%.

Key words: β-lactoglobulin, trypsin, ACE