FOOD SCIENCE ›› 2012, Vol. 33 ›› Issue (5): 208-212.doi: 10.7506/spkx1002-6630-201205044

• Bioengineering • Previous Articles     Next Articles

Response Surface Methodology for Optimization of Hydrolysis Conditions for the Production of Milk-derived Angiotensin-I Converting Enzyme (ACE) Inhibitory Peptides

XU Xin,CAI Li-li,LIU Guo-yan,HE Jia-yi,WEI Xiao-rui,Wang Zhi-ying,ZHANG Jun   

  1. 1. School of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China; 2. Farm of Experiment, Yangzhou University, Yangzhou 225001, China
  • Online:2012-03-15 Published:2012-03-03

Abstract: In our present study, response surface methodology was used to optimize process conditions for the hydrolysis of sodium caseinate by trypsin to prepare highly active angiotensin-I converting enzyme (ACE) inhibitory peptides. ACE inhibitory rate was measured by RP-HPLC. One-factor-at-a-time method followed by response surface analysis was used to analyze the effects of pH, temperature, hydrolysis time, substrate concentration, enzyme/substrate ratio on ACE inhibitory activity of sodium caseinate hydrolysate. A mathematical model describing the relationship of ACE inhibitory activity of sodium caseinate hydrolysate with temperature (A), hydrolysis time (B), substrate concentration (C) and enzyme/substrate ratio (D) was obtained as follows: Y=-11.21347+4.32902A-1.45953B+3.42928C-0.20303D+0.050303AB+0.047422AD+0.14955BC +0.12486BD - 0.054526A2 - 0.079754B2 - 0.53587C2 - 0.28096D2. The optimum hydrolysis conditions were determined as pH 7.0, 52.31 ℃, 19.44 h, substrate concentration of 5.91 g/100 mL and enzyme/substrate ratio of 8.37‰, resulting in an ACE inhibitory rate of 97.11%.

Key words: sodium caseinate, trypsin, ACE inhibiting peptides, response surface methodology, RP-HPLC

CLC Number: