Cold plasma reengineers peanut protein isolate: Unveiling changes in functionality, rheology, and structure

This study investigates the effects of cold plasma (CP) treatment on peanut protein isolate (PPI), focusing on functionality, rheology, and structural modifications across various treatment times (0, 90, 180, 270, 360, and 450 s) and voltages (120, 140, and 160 kV). Key findings include a significant increase in solubility from 9.99 mg/mL to 15.98 mg/mL, as well as 161.07 % enhanced water-holding capacity (WHC) and 448.45 % oil-holding capacity (OHC). CP treatment also improved foaming capacity (FC) to 186.46 % and increased emulsion capacity (EC) and emulsion stability (ES) by 185.90 % at 160 kV. Rheological analysis showed shear-thinning behaviour, with viscosity decreasing as the shear rate increased-higher voltages (140 kV and 160 kV) further reduced viscosity, indicating lower resistance to flow. Additionally, CP-treated PPI exhibited viscoelasticity, with increased storage and loss moduli at higher frequencies, indicating greater stiffness. Spectroscopic studies demonstrated shifts in the protein's secondary structure, altering the balance among alpha-helix, beta-sheet, and random coil components, which highlights CP's role in reengineering PPI. FTIR-ATR spectra revealed reductions in the 3200-3400 cm^-1 range, suggesting changes in protein backbone vibrations and hydrogen bonding. Particle size analysis showed significant increases, especially at higher voltages and longer treatment times, stabilizing after 270 s. Zeta potential assays indicated a gradual decrease in negative surface charge, suggesting enhanced protein aggregation. Overall, CP treatment significantly improves the functional and rheological properties of PPI while inducing structural changes, making it more suitable for applications in the food and pharmaceutical industries.