FOOD SCIENCE ›› 2013, Vol. 34 ›› Issue (23): 118-122.doi: 10.7506/spkx1002-6630-201323025

Previous Articles     Next Articles

Separation, Purification and Structural Analysis of Angiotensin-converting Enzyme (ACE) Inhibitory Peptides from Hydrolysate of Silkworm Pupae Protein

WU Qiong-ying1,DU Jin-juan1,XU Jin-ling1,JIA Jun-qiang2,YAN Hui1,GUI Zhong-zheng2   

  1. 1. School of Biotechnology and Chemical Engineering, Jiangsu University of Science and Technology, Zhenjiang 212018, China;
    2. Sericultural Research Institute, Chinese Academy of Agricultural Sciences, Jiangsu University of Science and Technology,
    Zhenjiang 212018, China
  • Received:2012-11-23 Revised:2013-10-28 Online:2013-12-15 Published:2014-01-03
  • Contact: WU Qiong-ying E-mail:wuqy1@163.com

Abstract:

Objective: In order to investigate the structural characteristics of angiotensin-converting enzyme (ACE)
inhibitory peptides from silkworm pupae protein. Methods: The ACE-inhibitory peptides from hydrolysate of silkworm
pupae protein were separated and purified by ultrafiltration, DEAE-52 ion exchange chromatography and Sephadex G-50 gel
filtration chromatography. Then, the structural characteristics of purified ACE-inhibitory peptides were analyzed by liquid
chromatography-mass spectrometry (LC-MS). Results: Fraction 2 (IC50 0.072 mg/mL) with higher ACE-inhibitory activity
was obtained from silkworm pupae protein hydrolysate. This fraction was the major component of ACE-inhibitory peptides,
and its ACE-inhibitory activity was increased by 2.95 times over that of silkworm pupae protein hydrolysate. Conclusion: In
fraction 2, ACE-inhibitory peptides were mainly composed of the peptide fragments from dipeptide to octapeptide, and their
relative molecular weights were 226.34 to 983.61 u.

Key words: silkworm pupae protein, angiotensin-converting enzyme (ACE) inhibitory peptide, separation and purification, liquid chromatography-mass spectrometry

CLC Number: