International Journal of Peptide Research and Therapeutics

, Volume 18, Issue 4, pp 353-360

First online:

Structure and ACE-Inhibitory Activity of Peptides Derived from Hen Egg White Lysozyme

  • Mina Memarpoor-YazdiAffiliated withDepartment of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University
  • , Ahmad AsoodehAffiliated withDepartment of Chemistry, Faculty of Sciences, Ferdowsi University of MashhadCellular and Molecular Research Group, Institute of Biotechnology, Ferdowsi University of Mashhad Email author 
  • , JamshidKhan ChamaniAffiliated withDepartment of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University

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Angiotensin I-converting enzyme plays an important role in hypertension and therefore its inhibition is considered to be a useful procedure in the prevention of hypertension. Two novel ACE inhibitory peptides were purified and identified from the papain-trypsin hydrolysate of hen egg white lysozyme using reverse phase-high performance liquid chromatography. The sequences of identified peptides were NTDGSTDYGILQINSR (MW: 1,753.98 ± 0.5 Da) and VFGR (MW: 459.26 ± 0.5 Da), which were named F2 and F9 peptide, respectively. Analyses of the far-UV CD spectra of ACE in the absence and presence of the F2 peptide revealed ACE secondary structural changes. In the presence of the F2 peptide, a loss of helical content of ACE was observed, which can lead to decrease of the enzymatic activity. Lineweaver–Burk plots show that the identified peptides both act as non-competitive ACE inhibitors. These findings would be helpful on the understanding of interaction between ACE and its inhibitory peptides.


RP-HPLC ACE inhibitory activity Inhibition pattern Circular dichroism spectroscopy