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

Impact of ultra-high pressure on the physicochemical and functional properties of apple pectin.

The inherent characteristics of pectin often lead to insufficient adaptability. In the study, apple pectin was treated under ultra-high pressure to optimize its properties. The results demonstrated that ultra-high pressure treatment at 100-700 MPa for 15 min significantly improved the physicochemical and functional properties. Specifically, it significantly increased the degree of esterification, emulsifying activity and stability, water- and oil-holding capacities, and swelling power, while also enhancing fat/glucose adsorption and α-amylase inhibition. Treatment at 400-500 MPa for 15 min was identified as maximizing in enhancing these properties. Microstructural analysis revealed that ultra-high pressure disrupted and loosened the pectin matrix, which was closely correlated with the enhanced functionalities. These findings demonstrated that moderate ultra-high pressure treatment effectively improved pectin properties by altering its structure. It provides a theoretical basis for the application of ultra-high pressure modified pectin as the functional foods.

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

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%.

Mechanistic insights into structural remodeling and functional enhancement of peanut protein induced by high-speed shear processing

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.

Effect of high hydrostatic pressure on in vitro digestibility and techno-functional properties of fava bean (Vicia faba L.) protein

The increasing demand for sustainable protein sources has positioned fava beans as a promising alternative; however, their limited techno-functional properties and digestibility restrict broader application within food systems. This study aimed to evaluate the impact of high hydrostatic pressure on the structural, nutritional, and techno-functional properties of fava bean protein isolate under various pressure levels, treatment times, and protein concentrations. Protein dispersions (5–20% w/v) were subjected to pressures ranging from 300 to 600 MPa for up to 9 min, and subsequent changes in protein structure, in vitro digestibility, and functional properties were assessed. Moderate pressures (300–400 MPa) induced partial protein unfolding, thereby increasing the exposure of reactive groups and enhancing enzymatic accessibility, which resulted in improved digestibility, solubility, emulsifying capacity, foaming properties, and water holding capacity. In contrast, higher pressures (≥500 MPa) and extended treatment times promoted protein aggregation, leading to reduced functionality and digestibility. Furthermore, elevated protein concentrations limited structural modifications due to molecular steric hindrance, thereby reducing responsiveness to pressure treatment. These findings demonstrate a biphasic, pressure-dependent behavior whereby controlled structural disruption enhances protein performance, whereas excessive processing induces aggregation and functional decline. Overall, moderate HHP conditions (300–400 MPa) were identified as an effective strategy to enhance the nutritional and techno-functional quality of fava bean protein, offering valuable insights for the development of sustainable plant-based food ingredients.