FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (18): 25-28.doi: 10.7506/spkx1002-6300-200918001

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Macroporous Adsorption Resin Isolation and Stability of Angiotensin-converting Enzyme (ACE) Inhibitory Activity of Antihypertensive Peptides Derived from Grass Carp Protein

CHEN Ji-wang1,SUN Qing1,XIA Wen-shui1,2   

  1. 1. School of Food Science and Technology, Wuhan Polytechnic University, Wuhan 430023, China ;
    2. School of Food Science and Technology, Jiangnan Unviersity, Wuxi 214122, China
  • Received:2009-03-02 Revised:2009-06-07 Online:2009-09-15 Published:2010-12-29
  • Contact: CHEN Ji-wang E-mail:jiwangchen@yahoo.com.cn

Abstract:

Various macroporous adsorption resins were used for the isolation of antihypertensive peptides from grass carp protein hydrolysate with the hydrolysis degree of 34.52% and the stability of angiotensin-converting enzyme (ACE) inhibitory activity of the peptides was analyzed. Among 8 types of macroporous adsorption resin tested, DA201-C had the best adsorption capability. The peptide fraction eluted by 75% ethanol displayed the highest ACE inhibitory activity with the IC50 of 1.52 mg/ml. After isolation, the ash content was decreased from 9.47% to 2.34%, while the contents of peptide and protein were increased from 72.81% to 81.26% and 80.24% to 92.42%, respectively. Pepsin, pancreatin, neutral and low acidic pH, heating at temperatures below 55 ℃ and concentrations of NaCl solution below 1000 mmol/L all had slight effects on the ACE inhibitory activity of the peptides.

Key words: grass carp, antihypertensive peptides, macroporous adsorption resin, angiotensin-converting enzyme (ACE) inhibitory activity

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