Identification of a novel hypotensive peptide from porcine plasma hydrolysate by in vitro digestion and rat model

Junqi Zhan; Gaoshang Li; Yali Dang; Daodong Pan

doi:10.1016/j.fochms.2022.100101

Identification of a novel hypotensive peptide from porcine plasma hydrolysate by in vitro digestion and rat model

Food Chem (Oxf). 2022 Mar 17:4:100101. doi: 10.1016/j.fochms.2022.100101. eCollection 2022 Jul 30.

Authors

Junqi Zhan^{1

2}, Gaoshang Li³, Yali Dang^{1

2}, Daodong Pan^{1

2}

Affiliations

¹ State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo 315211, China.
² Key Laboratory of Animal Protein Food Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, Zhejiang, China.
³ Institute of Food Engineering, Zhejiang University, Hangzhou 310058, Zhejiang, China.

Abstract

We separated a novel functional peptide IFPPKPKDTL from porcine plasma hydrolysate by chromatography, HPLC, and identified by Q Exactive LC-MS/MS. Results showed that IFPPKPKDTL had a significant ability of ACE inhibition (76.6%) likely due to the presence of hydrophobic, aromatic, and acidic amino acids that can inactivate ACE by binding Zn²⁺, providing a hydrogen atom to maintain the link between ACE and the peptide. Furthermore, the ACE inhibition of synthetic IFPPKPKDTL was improved by 15.6% after in vitro digestion. Additionally, the systolic blood pressure and diastolic blood pressure of spontaneously hypertensive rats gavaged by the peptide (30 mg/kg). Thereby, ACE inhibitory peptide IFPPKPKDTL from porcine plasma was stable and has potential functional value.

Keywords: ACE inhibition; In vitro digestion; Peptide; Plasma; Spontaneously hypertensive rats.