Broccoli byproducts protein concentrate: Microwave treatment effect on functional, thermal, and structural properties.

Germinated Red Lentil Protein Concentrate: Effect of Microwave Pretreatment on Physicochemical, Functional, Thermal, and Structural Properties

This study examines the effect of microwave treatment on the properties of protein concentrate derived from germinated red lentil ( Lens culinaris ) flour. Germinated red lentil flour was subjected to microwave (MW) treatment at two power intensities (540 and 720 W) for varying durations (2, 4, and 6 min), following which protein was extracted. The extracted protein was subsequently analyzed to determine modifications in proximate composition, water and oil absorption capacities, foaming and emulsifying properties, as well as structural attributes, employing SEM, FTIR, DSC, and XRD techniques. MW treatment at 540 W for 4 min exhibited significant improvement in the functional properties of the protein concentrate, notably enhancing water and oil absorption capacities. Foaming capacity increased from 125.24% to 175.35% for 540 W at 2 and 4 min, respectively, but declined with prolonged exposure, suggesting protein aggregation and diminished surface activity. Thermal analysis by DSC revealed a disappearance of denaturation peaks in treated samples, indicating pre‐existing conformational changes induced by microwave energy. XRD and FTIR results confirmed disruption of semi‐crystalline regions and secondary structure, with SEM imaging highlighting microstructural loosening and porosity. The findings underscore the potential of microwave processing to tailor protein functionality through targeted structural modification, offering promising applications in the formulation of novel plant‐based foods. However, excessive treatment may compromise thermal stability and emulsifying ability, underscoring the need to optimize microwave parameters to strike a balance between structural integrity and functional enhancement.

Alcalase hydrolysis enhances solubility and foaming properties of perilla protein isolate through structural modification

Temperature-Mediated Structure–Functionality Changes in Soybean Meal Protein via Extrusion

Soybean meal protein, a byproduct of soybean processing, has limited functional properties such as emulsifying performance, which restricts its application in foods. Given that high-temperature extrusion tends to cause excessive denaturation and irreversible aggregation, this study aimed to investigate the effects of relatively low extrusion temperatures (85–105 °C) on the structural and functional properties of soybean meal protein. The results showed that extrusion altered the molecular structure and functional characteristics of the protein. With increasing extrusion temperature, the β-sheet content increased while the α-helix content decreased in the secondary structure, and tertiary structural rearrangements occurred, with hydrophobic groups being exposed and subsequently buried. At 95 °C, the protein formed a relatively porous and loose microstructure and exhibited the strongest surface hydrophobicity, water-holding capacity, oil-holding capacity, and emulsifying properties; at 100 °C and above, excessive aggregation occurred, pore structure collapsed, and functional properties declined. Meanwhile, extrusion generally reduced protein solubility. Therefore, 95 °C is identified as the optimal extrusion temperature under the conditions of this study. In addition, this study reveals the correlation between structural reconstruction and functional changes of soybean meal protein, providing a theoretical basis for its high-value utilization and application in the food industry.

Tailoring the structure-functionality and volatile properties of pea protein isolate by high-pressure homogenization: Impact of pass number and pressure.

Pea protein is increasingly used in food formulations due to its nutritional value and sustainability. However, its limited solubility, weak interfacial properties, and undesirable off-flavors remain major constraints for broader application. In this study, pea protein isolate (PPI) was subjected to multi-stage high-pressure homogenization (HPH) at pressures ranging from 100/1000 psi to 500/5000 psi with various pass numbers (1, 2, and 3) to examine how processing intensity affects its structural, functional, and volatile properties. SDS-PAGE showed no detectable changes in molecular weight distribution, whereas FTIR, particle size distribution, and zeta potential analyses collectively indicated that HPH induced subtle physicochemical modifications in PPI. These modifications improved functional properties, particularly solubility, which increased from 83.18% in the untreated sample to 88.14% under optimized conditions. Enhancements in foaming capacity and emulsifying activity were also observed, most prominently at 500/5000 psi, although excessive processing resulted in a slight decline in foaming performance. In contrast, emulsifying stability remained largely unchanged across conditions. Furthermore, GC-MS was used to evaluate the changes in the volatile profile of PPI after HPH treatment. Seven major compounds dominated by lipid oxidation products were identified. Their relative abundances varied with homogenization conditions with pressure exerting a more pronounced influence than pass number. Overall, HPH effectively tailored the properties of PPI by reducing particle size, improving solubility and interfacial properties, and altering its volatile profile, although at higher homogenization pressures the potential trade-off between functionality and oxidative flavor stability needs to be considered.

Laccase-induced structural remodeling of cottonseed protein for improving its emulsion stability and curcumin bioaccessibility.

BACKGROUND Cottonseed is an important byproduct of cottonseed processing and is rich in proteins. A literature review indicated that cottonseed protein isolate (CPI) demonstrated a compact structure because of its limited exposure of hydrophobic groups, leading to poor emulsifying performance. This limited the functional performance and practical application of CPI in food systems. This study aimed to enhance CPI interfacial functionality through laccase-induced structural remodeling and to evaluate its performance in curcumin (Cur)-loaded emulsions. RESULTS This study designed a control group (0%) and laccase-treated groups (0.3%, 0.5%, and 0.8%, w/w). It was found that protein aggregation and network formation became more pronounced following laccase treatment and followed a dose-dependent pattern. Importantly, this investigation revealed that free sulfhydryl and free amino groups decreased, whereas random coil content, hydrophobic residue exposure, surface hydrophobicity, emulsifying activity, foaming capacity and oil-holding capacity increased, in which surface hydrophobicity increased by 61.09%, and emulsifying activity, foaming capacity, and oil-holding capacity increased by 30.55%, 57.24%, and 10.94%, respectively. Pearson correlation analysis showed that surface hydrophobicity was closely related to functional improvement. Compared with the control, 0.8% laccase-modified CPI produced smaller, more uniform Cur-loaded droplets. Encapsulation efficiency increased from 74.04% to 81.97%, and Cur bioaccessibility increased from 26.84% to 40.88%. CONCLUSION These findings indicated that laccase modification improved the functional properties and interfacial characteristics of CPI by altering its molecular conformation, thereby enhancing the encapsulation and bioaccessibility of Cur. This study provided a promising strategy for improving the delivery of hydrophobic bioactive compounds through enzymatic modified proteins. © 2026 Society of Chemical Industry.

Modifying Structure–Functionality of Common Bean ( Phaseolus vulgaris L.) Protein via Cold Atmospheric Plasma Processing and Maillard Reaction

Structural and functional modifications of common bean (Phaseolus vulgaris L.) protein were investigated using cold atmospheric plasma (CAP) and Maillard reaction (MR) with pectin. CAP treatment (20 kV, 1–5 min) significantly enhanced protein solubility and emulsifying activity. Conversely, MR (90 °C, 0.5–3 h) reduced solubility and foaming properties but improved gelling capacity, achieving the lowest gelation concentration (LGC) at 2–3 h of heating. Conformational shifts in secondary structures (α-helix, β-turn, and β-sheet) were confirmed by FTIR and correlated with protein unfolding and structural modifications, as characterized by SDS-PAGE. Zeta potential measurements indicated that CAP improved colloidal stability, whereas extended MR heating decreased stability. These findings demonstrate that CAP is an effective nonthermal tool for enhancing protein functionality, while MR is better suited for developing stable gel-based food matrices, lowering the LGC from 8% to 5%.