Drying-resistant pea protein powders: Decoding structural determinants of redispersibility

Area of Science:

• Food Science
• Protein Chemistry
• Materials Science

Background:

• Drying processes often reduce plant protein solubility, limiting their industrial use.
• Pea protein isolate (PPI) is a valuable plant-based protein source, but its solubility challenges hinder wider application.

Purpose of the Study:

• To develop an effective method for enhancing pea protein isolate (PPI) powder solubility after drying.
• To investigate the structural changes responsible for improved PPI solubility.

Main Methods:

• Media milling of PPI combined with alkaline pH (10) shifting and heat treatment (100°C, 1 h).
• Analysis of PPI solubility, particle size distribution, Fourier-transform infrared spectroscopy (FTIR), Differential scanning calorimetry (DSC), Circular dichroism (CD) spectroscopy, Small-angle X-ray scattering (SAXS), and SDS-PAGE.

Main Results:

• The combined treatment increased PPI solubility from 26.68% to 95.57%, significantly improving dispersibility.
• Structural analysis revealed protein unfolding, a shift from α-helix to β-sheet conformations, reduced surface hydrophobicity, and subunit rearrangement without altering functional groups.
• Enhanced thermal stability was observed, with the denaturation temperature increasing from 94.53°C to 100.29°C.

Conclusions:

• A novel and efficient strategy was established for producing highly soluble PPI powders.
• The method effectively mitigates irreversible aggregation during drying, enhancing protein functionality.
• This approach holds significant potential for expanding the industrial applications of pea protein isolate.