Aug 2026· Journal of Agricultural and Food Chemistry· 0 citations· 41 references
Abstract
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.
Collagen peptide (CP) and whey protein are common ingredients in protein-rich functional beverages. However, their synergistic effects on digestion dynamics and nutraceutical bioaccessibility remain insufficiently elucidated. We here investigated how CP modulated the digestive fate, and curcumin bioaccessibility of whey protein concentrate (WPC)-stabilized emulsions. CP incorporation exhibited minimal influence on the initial physicochemical stability, droplet characteristics, or curcumin encapsulation efficiency (>88%). However, in vitro gastrointestinal digestion revealed that CP significantly increased curcumin bioaccessibility by 1.07- to 1.19-fold and accelerated the proteolysis of WPC-emulsified droplets. Microstructural analysis of the intestinal digesta demonstrated that CP induced the formation of distinct hollow vesicle-like structures, which were absent in the control emulsions. The soluble fraction of the digesta from CP-supplemented systems showed enhanced oleic acid solubilization in a dose-dependent manner, strongly associating with the formation of these hollow vesicular assemblies. Together, these findings indicate that CP modulates intestinal colloidal structures, thereby improving curcumin bioaccessibility.
Exocrine pancreatic insufficiency remains a major therapeutic challenge because orally administered enzymes undergo rapid degradation in the acidic gastric environment before reaching the intestine. The present study developed a scalable solid-in-oil (s/o) spray-drying technique for encapsulating protease within semi-permeable ethylcellulose (EC) microcapsules intended for targeted intestinal enzyme delivery. Pre-formulation studies identified a critical thermal deactivation threshold above 55°C, emphasizing the need for effective thermal stabilization during spray drying. Trehalose and sucrose were investigated as thermoprotective excipients, with 1.5 M trehalose demonstrating the highest protective effect by preserving 95.7% of the native enzyme activity following thermal exposure at 75°C. Circular dichroism spectroscopy confirmed the preservation of the native secondary structure in the stabilized formulations. The optimized microcapsules exhibited a production yield of 71.8%, an encapsulation efficiency of 85.3%, a median particle size (dv50) of 5.19 μm, and a narrow particle size distribution (span = 1.80), indicating excellent manufacturing reproducibility and particle uniformity. In vitro release studies demonstrated a biphasic release profile characterized by an initial burst release followed by sustained diffusion through the ethylcellulose membrane. Mathematical modeling revealed excellent agreement with the Higuchi model (R² = 0.9974), confirming that solute transport occurred predominantly through Fickian diffusion across the hydrated polymer matrix. The semi-permeable membrane effectively retained the encapsulated enzyme while allowing diffusion of low-molecular-weight substrates and reaction products. Overall, the developed solid-in-oil spray-dried ethylcellulose microcapsules represent a promising oral enzyme delivery platform with potential applications in enzyme replacement therapy for exocrine pancreatic insufficiency, phenylketonuria, and related metabolic disorders.
Amit Kumar, Gyan Singh, G. S. Chakraborthy et al.· Adolescência e Saúde· 0 citations
Mycoprotein, with a balanced amino acid profile and potential benefits for muscle maintenance, is a promising protein source for elderly-friendly high-protein foods. Yet, rigid fungal cell walls and entangled hyphal networks enclosing intracellular proteins may restrict enzymatic accessibility under elderly digestive conditions. In this study, high-pressure homogenization (HPH) was applied as a food-grade structural regulation strategy to improve the digestive adaptability of mycoprotein. Native mycoprotein (MYC), HPH-treated mycoprotein (HMYC), pork (PORK), and commercial plant-based meat (PLANT) were evaluated using a static in vitro oral-gastric-intestinal digestion model simulating elderly physiological conditions. Structural disintegration, hydrolysis behavior, free amino acid release, multiple light scattering, and microrheological properties were analyzed to elucidate digestive adaptation mechanisms. HPH markedly disrupted the cell-wall-associated and hypha-entangled structure of mycoprotein without significantly altering its major nutrient composition, thereby improving enzyme accessibility and digestion-induced disintegration. During gastric and intestinal digestion, the particle size D[4,3] of HMYC decreased by over 80%, indicating enhanced structural breakdown efficiency. HMYC exhibited a significantly higher hydrolysis degree than MYC, while its free amino acid release approached that of PORK and exceeded those of both MYC and PLANT. Multiple light scattering revealed improved enzyme-substrate interaction and greater physical structural transformation after HPH treatment. Microrheological analysis further confirmed improved restructuring behavior and reduced structural resistance during digestion. Overall, HPH effectively improved the digestive adaptability of mycoprotein under elderly digestive conditions, making its digestive behavior closer to that of PORK, while the distinct digestion behavior of PLANT was mainly associated with matrix effects from added lipids and hydrocolloids, supporting the development of elderly-friendly mycoprotein-based foods.
Yifei Gao, Chengpu Chen, Dan Yang et al.· Food & Function· 0 citations
In this study, we evaluated how varying concentrations of two exogenous proteins, egg white protein (EWP) and whey protein isolate (WPI) influence heat-induced aggregation and gelation of cod myofibrillar proteins (MPs). Addition of exogenous proteins enhanced the MP solubility and surface hydrophobicity while reducing the turbidity and total sulfhydryl levels. These physicochemical changes occurred during heating in three kinetic phases, an initial rapid phase (0-30 min), a slower transitional phase (30-60 min), and a second rapid aggregation phase (70-90 min) until equilibrium was reached. Dynamic rheology revealed that EWP enhanced G' at moderate concentrations but reduced it at higher levels, while WPI caused a progressive decline in G' with increasing concentration. Gel property analysis showed that EWP-M (MP:EWP = 2:14) produced the highest gel strength, whereas WPI-L (MP:WPI = 1:15) resulted in the lowest cooking loss and highest water-holding capacity (WHC). WPI-containing systems exhibited slightly lower gel strength but showed improved water retention and a uniform microstructure. Notably, a 1:1 EWP-WPI combination showed synergistic network solubility, hydrophobic exposure, and uniform microstructure, leading to high gel strength with minimal cooking loss and maximum WHC. Mechanistically, EWP acted as a structural enhancer, promoting gel network strengthening and increased rigidity, whereas WPI functioned primarily as a filler, enhancing water retention and reducing structural heterogeneity. These findings offer key insights into MP/EWP-WPI interactions and support the optimization of composite protein gel systems.
Safia Aslam, Jinjin Xing, Hui Tao et al.· Journal of texture studies· 0 citations
Dysphagia is characterized by difficulties in swallowing and chewing. Texture-modified soft foods are intended for patients with dysphagia to facilitate safe swallowing and meet nutritional requirements, with a primary focus on increasing protein intake. This study examined the feasibility of creating high-protein (35%) gel systems suitable for dysphagia patients by adjusting the levels of egg white protein and collagen hydrolysate.
It was observed that increasing the concentration of egg white and decreasing the amount of collagen improved water-binding capacity (from 95.23% to 100%), hardness (0.85 N to 5.43 N), elasticity (higher G' moduli), and network protein content (from 89.59% to 96.33%), while structural recovery declined (from 54.89% to 36.85%). Based on the International Dysphagia Diet Standardization Initiative test, hydrogels are classified as Level 6, fulfilling texture safety standards for dysphagia management. This classification makes them more appropriate for patients with mild dysphagia. FTIR, DSC, and SEM analysis confirmed that the main network in the hydrogel composition is formed by egg white protein, with collagen serving more as an inactive filler. Hydrophobic interactions were dominant and primarily contributed to the stabilization of the gel network. The protein hydrolysis rate in hydrogels gradually declined as egg white concentration increased, resulting in a denser, firmer, and less porous structure that may reduce enzyme interactions.
The findings offer a viable approach for designing tailored high-protein food formulations for dysphagia.
Deimantė Dagytė, Ieva Bartkuvienė, Evren Gölge et al.· International Journal of Foo...· 0 citations
Background Collagen hydrolysates differ in molecular weight distribution and composition, which may influence gastrointestinal absorption and epithelial transport. Objective The objective of this study is to compare the digestion and absorption kinetics of an ultra-low molecular weight collagen with >45% di- and tripeptides (LMWCP; 500 Da) and a standard collagen hydrolysate (CP; 2,000–3,000 Da) using a Caco-2 cell model and an exploratory human study. Materials and methods A Caco-2 cell Transwell model was used to assess the apical-to-basolateral appearance of collagen-derived free amino acids over 240 minutes after in vitro digestion of the test products. Product characterization included quantification of free amino acids and selected hydroxyproline-containing di- and tripeptides. In parallel, an exploratory single-blind, parallel-group human study in 15 healthy male participants measured postprandial plasma free amino acid kinetics at 0, 15, 30, 120, and 240 minutes after ingestion of LMWCP, CP, or placebo. Results In both models, LMWCP showed faster early-phase kinetics than CP. In the Caco-2 model, collagen-derived amino acids appeared in the basolateral compartment within the first minutes and were highest during the first 30 minutes with LMWCP. In the human study, plasma glycine and proline/hydroxyproline peaked earlier after LMWCP group (30 minutes) compared to CP group (120 minutes). Conclusion Across both in vitro and in vivo models, ultra-low-molecular-weight collagen (LMWCP; 500 Da), with more than 45% di- and tripeptides, exhibited faster early-phase absorption kinetics, thereby enhancing early-phase bioavailability. Collagen-derived amino acids appeared across the epithelial layer within minutes and reached plasma peaks earlier, compared to a standard collagen hydrolysate. These findings suggest that LMWCP exhibits distinct, accelerated absorption kinetics compared to conventional collagen hydrolysates.
Reyhan Nergiz-Unal, Stephan Dierckx, C. Roye et al.· PeerJ· 0 citations