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.
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
The feasibility of creating high-protein gel systems suitable for dysphagia patients by adjusting the levels of egg white protein and collagen hydrolysate is examined, offering 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
Across both in vitro and in vivo models, ultra-low molecular weight collagen (LMWCP), with more than 45% di- and tripeptides, exhibited faster early-phase absorption kinetics, thereby enhancing early-phase bioavailability.
Reyhan Nergiz-Unal, Stephan Dierckx, C. Roye et al.· PeerJ· 0 citations
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