High-pressure homogenization improves mycoprotein digestibility under an elderly static in vitro digestion model by disrupting cell-wall-related structural barriers.

Enhanced solubility of yeast protein via high-pressure homogenization-assisted limited enzymatic hydrolysis: mechanisms of structural modification and implications for functionality and nutrition.

Yeast protein (YP) is recognized as a sustainable and hypoallergenic microbial protein source, yet its low solubility (typically <22%) severely restricts its utilization in food formulations. Improving solubility is therefore a key step toward broader industrial application of YP. This study investigated a synergistic treatment combining high-pressure homogenization and restriction enzymatic hydrolysis (HPH-neu) to improve the solubility of yeast protein (YP). The HPH-neu treatment significantly enhanced solubility to 81.58 ± 0.29%. In contrast, the individual application of either high-pressure homogenization (HPH) or restriction enzymatic hydrolysis (neu) was less effective in improving solubility than the combined approach. Structural analysis indicated that HPH-neu processing notably increased the contents of α-helix and random coil, and scanning electron microscopy (SEM) revealed a corresponding looser and more disordered microstructure. Furthermore, the combined treatment significantly reduced particle size (242.8 ± 5.59 nm), free sulfhydryl group content (2.20 ± 0.01 μ mol/g), and surface hydrophobicity (H0, 14123.67 ± 257.85).At the same time, it improved functional properties including the emulsifying activity index (40.51 ± 2.86 m2/g), foaming capacity (146.67 ± 2.89%), and in vitro digestibility (90.64 ± 0.33%). The HPH-neu process also yielded high scores for PDCAAS and SRC, reaching 65.96 and 73.11, respectively. In summary, the integrated HPH-neu strategy not only effectively enhanced the solubility of YP but also improved its multifaceted functional properties and digestibility. This strategy offers a promising route for protein valorization and the development of high-quality, nutritious protein ingredients.

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.

Effects of Matrix Forms on Myofibrillar Protein Digestion across In Vitro and In Vivo Perspective: Hydrolysis Kinetics and Gastric Emptying

Dysphagia-adapted fluidized meat products alter the protein matrix structure and may impair digestibility. This work evaluated the digestive and nutritional properties of carboxymethyl cellulose (CMC)-modified myofibrillar protein (MP) thickened fluids across three matrices: liquid solution (MP), semisolid state (MP/CMC), and solid gel (MPgel). In vitro digestion indicated all MP matrices exhibited lower digestibility under elderly digestive conditions than adult systems, especially during gastric stage. CMC promoted protein hydrolysis by enhancing the accessibility of MP to pepsin. Digestive kinetics implied that initial and maximal gastric digestion rates of MP/CMC for adults were 13.07- and 3.65-fold higher than those of liquid MP, while dense cross-linked networks reduced digestion extent and rates in MP gel. In vivo, CMC thickening slowed gastrointestinal transit of semisolid MP, sustaining abundant gastric peptides and maintaining high steady-state serum total amino acids in mice. This work provided fundamental insights into the digestive and nutritional characteristics of CMC-induced meat protein-based fluids.

Spray-Dried Probiotic Microencapsulation Using Hazelnut Protein Modified by High-Pressure Homogenization: Microcapsule Properties, Thermal Stability, In Vitro Gastrointestinal Resilience, and Storage Stability

Process-dependent structural and functional modification of yeast protein: Alkaline extraction-acid precipitation versus high-pressure homogenization-assisted pH shifting.

Limited redispersibility constrains commercial yeast-protein ingredients. This study compared preparation efficiency, structure, and function of yeast protein prepared by alkaline extraction-acid precipitation (ASAP) and high-pressure homogenization-assisted pH shift (HPHS). ASAP achieved higher product yield (69.23% ± 1.42%) and protein recovery (57.81% ± 2.42%) than HPHS. ASAP-YP exhibited dense sheet-like morphology, higher β-turn content (55.71%), and preserved reactive groups, whereas HPHS-YP formed porous aggregates with higher α-helix content and lower sulfhydryl availability. Under tested conditions, ASAP-YP showed higher solubility (pH 3-13), water absorption (17.99 ± 0.62 g/g), oil absorption (7.98 ± 0.12 g/g), emulsifying activity (59.88 ± 2.58 m2/g), and foaming capacity (124.00% ± 2.00%). Multivariate analysis indicated β-turn content, surface hydrophobicity, and reactive-group content were positively associated with selected functional properties. These findings support ASAP as a promising route, while validation across additional raw materials remains necessary.

Contrasting structural evolution of starch and protein in aged wheat is associated with interfacial disintegration: implications for nutrient utilization and predictive modeling

Wheat aging alters starch-protein organization within the endosperm, but its consequences for nutrient digestion and animal performance remain unexplored. This study showed that starch disordering and protein oxidative cross-linking (disulfide bonds: 5.47 μmol/g) were associated with deterioration of the starch–protein interface. Quantitative confocal microscopy supported this interpretation, showing a 28.8% reduction in spatial colocalization. This deterioration was accompanied by altered digestive kinetics, characterized by an 11.35% increase in starch digestibility and a 51.17% decrease in protein digestibility (P < 0.05). In vivo broiler trials supported the physiological relevance of these alterations, as aged-wheat diets were associated with a 28.9% reduction in 42-day body weight. Gluten-hydration-based equations were developed to track nutrient evolution, and predictive models using physicochemical traits were established to assess digestibility (R2 ≥ 0.81) and broiler metabolic performance (R2 ≥ 0.91). These findings provide mechanistic insights and a preliminary framework for targeted utilization of aged wheat.