NATURAL PRODUCT RESEARCH AND DEVELOPMENT ›› 2011, Vol. 23 ›› Issue (2): 295-298.

• Article • Previous Articles     Next Articles

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

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