Food Chemistry: Molecular Sciences (Jul 2022)

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

Journal volume & issue
Vol. 4
p. 100101

Abstract

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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.

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