Unraveling the underlying mechanism: how processing methods alter muscle protein structure and in vitro digestibility of shrimp (Litopenaeus vannamei).

Effects of dietary fibers varying in physicochemical properties on total endogenous protein losses and protein digestibility in broilers.

Assessment of the energy and protein requirements for tambaqui (Colossoma macropomum, Cuvier 1818) using the factorial approach

There is a lack of information about the nutritional requirements of European catfish ( Silurus glanis ) for aquaculture. This study aimed to fill this gap using a bioenergetic factorial model. To develop the model, a series of sub-studies were carried out. Accordingly, the growth potential of fish was determined using the data collected in this study and from the literature. The whole-body moisture, protein, lipid, ash, and energy content changes were analyzed to reveal how they vary as size increased up to 4000 g. An experiment was conducted to determine the maintenance requirements and utilization efficiencies for digestible protein (DP) and digestible energy (DE). The maintenance requirements of DP and DE were estimated as 0.163 g/kg 0.7 /day and 16.44 kJ/kg 0.8 /day and their utilization efficiencies were 51.72% and 52.52% respectively. Another sub-model for estimating digestible essential amino acid requirements was also run based on the ideal protein concept (IPC) of the European catfish fillet amino acid profile. Each sub-model was then combined to estimate the daily requirements of DP, DE, DP:DE ratio, and amino acids across different sizes of fish. The estimations of DP:DE ratio requirements were converted to dietary specifications for different stages of fish growing from 10 g to 4000 g using a sequential application of two-breakpoint models, which yielded 5 different diets during the farming period of European catfish. The whole model suggested that European catfish require high dietary protein during the early stages, which can be reduced over the culture period by increasing DE. Based on the IPC, dietary digestible essential amino acid requirements were estimated depending on the sizes and diet specifications. This study provides valuable information about dietary DP, DE, DP/DE ratio, and digestible amino acid requirements of European catfish, which requires future validation through controlled feeding trials.

Interpreting the asymmetric interaction between yeast and acetic acid bacteria in kefir grains from a metabolic perspective.

Lipid-driven modulation of milk/soy proteins digestion in young child formulas: From in vitro gastric emptying to intestinal absorption coupled with in vivo protease activation.

Yogurt is a popular functional dairy product prized for health benefits and nutritional value, especially as a significant source of high-quality proteins. In recent years, the research on the processing-induced modification of milk protein structure to regulate its nutritional properties has attracted much attention. Although yogurt processing has been extensively studied at the physicochemical level, novel processing technologies continue to emerge. At the same time, increasing attention has been directed toward digestion-driven nutritional functionality, calling for a renewed, digestion-oriented interpretation of processing-induced protein modifications and their downstream physiological relevance. The review synthesizes current knowledge on how key yogurt processing technologies-standardization, homogenization, heat treatment, and fermentation-govern milk protein structural transformations, gel network formation, and bioactive peptide generation. Particular emphasis is placed on linking processing-induced protein changes with gastrointestinal digestion behaviors, including gastric emptying, enzymatic hydrolysis, and nutrient absorption. Precisely, processing-driven protein denaturation, aggregation, redistribution, and hydrolysis collectively determine yogurt matrix architecture and its digestive fate. Structural features of the yogurt matrix modulate gastric emptying kinetics, whereas protein conformational changes influence enzymatic accessibility and hydrolysis rates. Fermentation-associated proteolysis further alters the profile and availability of absorbable peptides and amino acids. This review may help for advancing yogurt production from standardized processing toward precision nutrition design and for developing functional yogurts with targeted digestive and health benefits.

Effects of protease-hydrolyzed cottonseed protein on growth performance, intestinal morphology, and bacterial diversity in broilers.

Ready-to-eat expanded parboiled brown rice and bean snack consumption promotes good protein quality and improves lipid and glycemic profiles and intestinal health.

Supplements are commonly used by osteoarthritis (OA) patients, and eggshell membrane (ESM) proteins are widely advertised as natural bioactive compounds for joint health. Here, we evaluated the solubility, digestibility, and immunomodulatory potential of commercial ESM supplements under physiologically relevant conditions to assess their plausibility as anti-inflammatory agents. We analyzed three commercial ESM formulations (NEM®, Torolis®, and Biova®) using standardized extraction protocols. Protein solubility was assessed in physiological saline and under simulated gastric (pH 2) and intestinal (pH 5.8) conditions with controlled temperature, agitation, and digestive enzyme exposure. We examined the role of disulfide-crosslinked proteins in insolubility using dithiothreitol (DTT) and evaluated digestibility of proteins by SDS-PAGE after treatment with pepsin, pancrelipase (Creon®), or sequential digestion. Released peptides were identified by MALDI-TOF mass spectrometry, and immunomodulatory effects were tested using human peripheral blood mononuclear cells (PBMC) by measuring cytokine release after stimulation with lipopolysaccharide or Phorbol 12-myristate 13-acetate/Ionomycin, in the presence or absence of Biova®. NEM® and Torolis® showed extremely low solubility (< 0.3%) and remained insoluble under all conditions, including after DTT treatment. Although Biova® was highly soluble (~ 90%), simulated gastrointestinal digestion produced minimal peptide generation. Only non-physiological extraction yielded sporadic trace peptides, most lacking known anti-inflammatory relevance. In PBMC assays, Biova® increased IL-6 after lipopolysaccharide stimulation, showed a non-significant TNFα reduction, and had no effect on IL-17A or granzyme B. Together, commercial ESM supplements are largely insoluble, resistant to digestion, and show no meaningful anti-inflammatory activity in human immune cells. These findings challenge the plausibility of orally administered ESM as a therapeutic intervention for osteoarthritis.

Physicochemical and digestive properties of low-sodium bread enriched with Agaricus bisporus and Pleurotus ostreatus co-products.

Structural modifications of lupin protein isolate induced by high hydrostatic pressure and their impact on in vitro digestibility and techno-functional properties.

Multiscale insights into the digestion and bioactive peptide release of Laminaria-fortified yak meat under different thermal treatments.

Degradation products of phytic acid during high-moisture extrusion and impacts on the digestion and absorption of textured protein.

Sargassum filipendula flour improves composition, digestibility, and antioxidant activity of gluten-free biscuits.

Fermentation unlocks the nutritional potential of oat milk during in vitro dynamic gastrointestinal digestion and colonic fermentation.

Gut microbiota and metabolites have been increasingly implicated in the pathogenesis of immune inflammation, which may be affected by environmental factors. This study aimed to explore the influence of co-exposure to high humidity and temperatures (low, normal or high) on biomarkers of immune inflammation and potential mechanisms. We established C57BL/6J mice models (with equal numbers of males and females) of high humidity and low temperature (HH-LT), normal temperature (HH-NT) or high temperature (HH-HT) co-exposure environments to observe the impact of high humidity and different temperature co-exposure environments for 28 and 56 consecutive days. Following exposure, results showed that all six combined exposure conditions significantly increased pro-inflammatory cytokines (TNF-α, IL-1β, IL-12p70), decreased anti-inflammatory cytokines (IL-4, IL-10) and elevated the Teff/Treg ratio in the spleen. Gut microbiota analysis revealed reduced Akkermansia and increased Desulfovibrio and Enterorhabdus. Serum metabolomics identified widespread disturbances enriched in pathways including protein digestion and absorption, lysine degradation, phenylalanine metabolism and unsaturated fatty acid biosynthesis. Pearson correlation analysis confirmed significant associations among microbial shifts, immune-inflammatory dysregulation and metabolic perturbations-suggesting that high humidity combined with different temperatures correlated with immune imbalance, likely mediated by gut dysbiosis and serum metabolic disruption.

Oncogenic viruses, such as human papillomavirus (HPV), alter the endosomal system to manipulate the proteomic content of extracellular vesicles, aiding their persistence and disease progression. HPV has emerged as a key risk factor for head and neck squamous cell carcinoma (HNSCC). However, the influence of HPV on the exosomal proteomics remains poorly understood. Label-free quantitative proteomics was employed to analyze proteins extracted from HPV16-positive (93VU147T, UDSCC2) and HPV-negative (OCT1) HNSCC cell lines and their exosomes. Data are available via ProteomeXchange with identifier PXD067001. PCA revealed distinct clustering of HPV16-positive and -negative cells and exosomes. Differential expression analysis revealed 130 and 136 DEPs in exosomes of 93VU147T and UDSCC2, respectively, and 326 and 320 DEPs in the corresponding cells. Gene Ontology enrichment showed that HPV16-positive exosomal proteins and cells were associated mainly with protein digestion and absorption, different neurodegenerative diseases, and PI3K/Akt signaling. Exosomes showed distinct profiling from that of parental cells, emphasizing selective cargo packaging. Overall, the study demonstrates that HPV modulates the exosomal content in HNSCC, suggesting potential implications in tumor progression and biomarker discovery.

Exogenous proteases can enhance protein digestion in feed. However, their precise impact on peptide release and allergenecity remains poorly understood. This study evaluated the effects of a protease blend (Protease I) and a single protease (Protease II) on soybean meal in vitro digestibility and peptide release, using the standardized INFOGEST model. Compared to the Control, Proteases I and II increased protein digestibility from 83-89% to 90-96% and 91-92%, respectively, while enhancing peptide release from typically enzyme-resistant regions. Peptide profiling showed broader sequence coverage of key soybean proteins and revealed distinct substrate specificities. Cleavage site analysis indicated that exogenous enzymes altered the proteolytic pattern. Importantly, epitope sequence comparison revealed that enzymatic hydrolysis reduced the presence of certain allergenic epitopes. These findings suggest that protease supplementation enhances digestibility and may reduce allergenic potential, offering a promising strategy to improve the nutritional quality and safety of plant-based feed proteins.

Human insulin-like growth factor-1 (hIGF-1) is a non-glycosylated polypeptide hormone that plays a crucial role in prenatal and postnatal growth. Recently, various engineered variants of hIGF-1 have been created to enhance protein stability and activity. However, challenges persist in the production process, including yield, purification, and production costs. In this study, we simultaneously expressed active TEV protease and His-tagged hIGF-1 fused with the TrxA solubility tag in SHuffle T7 Express and Rosetta-gami 2(DE3) strains to assess expression yield and in vivo digestion of the soluble TrxA-free His-tagged hIGF-1 fusion protein. Our findings revealed efficient expression of recombinant TrxA-TEVs-His.hIGF-1, with successful digestion by TEV protease to release TrxA-free His-tagged hIGF-1 in both strains. However, the SHuffle strain exhibited higher expression levels and TEV protease functionality under optimized conditions. Furthermore, bioactivity assays of the purified TrxA-free His-tagged hIGF-1 demonstrated comparable activity to a commercial hIGF-1. This study developed a simple and feasible method for producing and purifying soluble, active recombinant hIGF-1 without any solubility tag through effective in vivo cleavage. By maintaining protein activity, this method is expected to simplify downstream processing and reduce both the time and cost of protein production.