Decoding salty peptides from pea protein: Isolation, characterization, and structure-activity relationship.

Area of Science:

• Food Science
• Biochemistry
• Nutritional Science

Background:

• Pea protein is a valuable source of amino acids.
• Developing savory peptides is crucial for food formulation.
• Reducing sodium content in foods is a public health priority.

Purpose of the Study:

• To identify and characterize salty peptides from pea protein hydrolysates.
• To investigate the structure-activity relationships of these peptides.
• To explore their potential in salt-reducing food applications.

Main Methods:

• Pea protein hydrolysates were fractionated using ultrafiltration and gel permeation chromatography.
• Peptide identification was performed using Liquid Chromatography-Mass Spectrometry/Mass Spectrometry (LC-MS/MS).
• Sensory evaluation, molecular docking, 3D-QSAR, and molecular dynamics simulations were employed.

Main Results:

• Ten peptides were selected based on specific criteria, including saltiness-related amino acid sequences.
• FDDKVR showed the highest saltiness intensity, while RSDPQNPF significantly boosted NaCl solution saltiness.
• Hydrogen bonding, particularly involving arginine and alanine, was identified as the key interaction with the TMC4 receptor.

Conclusions:

• Pea protein is a viable source for generating potent salty peptides.
• Understanding peptide-receptor interactions aids in designing salt-reducing agents.
• These findings support the development of innovative, low-sodium food products using pea protein.