Primary and secondary structure of novel ACE-inhibitory peptides from egg white protein

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• 作者：Zhipeng Yu^a ; ¹ ; Boqun Liu^a ; ¹ ; Wenzhu Zhao^a ; Yongguang Yin^a ; Jingbo Liu^a ; ^{ljb168@sohu.com} ; Feng Chen^b
• 关键词：ACE inhibitory activity ; Peptide ; Egg white protein ; Secondary structure ; Antioxidant property ; Anticoagulation activity
• 刊名：Food Chemistry
• 出版年：2012
• 期刊代码：48_03088146
• 类别：abs
• 出版时间：15 July, 2012
• 卷：133
• 期：2
• 页码：315-322
• 文件大小：613 K

摘要

The primary structure of novel angiotensin converting enzyme (ACE) inhibitory peptide from egg white protein was investigated, and secondary structure of the peptide was explored for the first time. The potential effects of bioactive peptides were submitted to bioactivity screening with ACE inhibitory activity, antioxidant property, and anticoagulation activity. Bioactive peptides from egg white protein were characterized by LC tandem mass spectrometric, and secondary structures of those peptides were investigated by FT-IR. Our results showed that total 11 bioactive peptides with three new and eight known structures were identified with LC/MS/MS, which then were synthesized by Fmoc solid phase method. Peptide Thr-Asn-Gly-Ile-Ile-Arg (TNGIIR) exhibited higher activity against ACE to other two new peptides. The concentration of the peptide TNGIIR, necessary to inhibit 50%the activity of ACE was 70 渭M. Results also suggested that the secondary structural differences between peptides could also influence the ACE inhibition capacity. Thus, it appears that primary and secondary structure of peptide plays the potential role inhibiting the ACE activity.