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1.
J Food Sci ; 89(7): 4109-4122, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38957103

ABSTRACT

The elucidation of the interaction mechanism between phospholipids and milk proteins within emulsions is pivotal for comprehending the properties of infant formula fat globules. In this study, multispectral methods and molecular docking were employed to explore the relationship between phosphatidylcholine (PC) and whey protein isolate (WPI). Observations indicate that the binding constant, alongside thermodynamic parameters, diminishes as temperature ascends, hinting at a predominantly static quenching mechanism. Predominantly, van der Waals forces and hydrogen bonds constitute the core interactions between WPI and PC. This assertion is further substantiated by Fourier transform infrared spectroscopy, which verifies PC's influence on WPI's secondary structure. A detailed assessment of thermodynamic parameters coupled with molecular docking reveals that PC predominantly adheres to specific sites within α-lactalbumin, ß-lactoglobulin, and bovine serum albumin, propelled by a synergy of hydrophobic interactions, hydrogen bonding, and van der Waals forces, with binding energies noted at -5.59, -6.71, and -7.85 kcal/mol, respectively. An increment in PC concentration is observed to amplify the emulsification properties of WPI whilst concurrently diminishing the zeta potential. This study establishes a theoretical foundation for applying the PC-WPI interaction mechanism in food.


Subject(s)
Hydrogen Bonding , Hydrophobic and Hydrophilic Interactions , Molecular Docking Simulation , Phosphatidylcholines , Thermodynamics , Whey Proteins , Whey Proteins/chemistry , Phosphatidylcholines/chemistry , Spectroscopy, Fourier Transform Infrared/methods , Lactoglobulins/chemistry , Lactoglobulins/metabolism , Emulsions/chemistry , Lactalbumin/chemistry , Lactalbumin/metabolism , Serum Albumin, Bovine/chemistry , Infant Formula/chemistry
2.
J Food Sci ; 89(7): 4389-4402, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38957134

ABSTRACT

Previously, we showed that water extract (soymilk, except pH was increased to 8 from 6.5) of whole soybean could be used directly as a raw material for producing edible soy films by deposition of the film-forming solution (soy extract with enhancers). However, the strength of such soy films needed improvement because they were weak. The purpose of this study was to investigate how transglutaminase (TG) cross-linking reactions and film enhancers, including pectin (low- and high-methoxyl pectin), whey protein isolate (WPI), and soy protein isolate (SPI), improve the physical properties of soy films. Soy films prepared with TG had tensile strength (TS) of 3.01 MPa and puncture strength (PS) of 0.78 MPa, which were higher by as much as 51% and 30% than that of soy films without TG treatment, respectively. Pectin showed significant effects on the mechanical properties of TG-added soy films in terms of TS, PS, and % elongation. On the other hand, only TS and PS were increased by the addition of WPI or SPI. Heat curing had a significant effect on soy film's physical properties. TG treatment significantly reduced film solubility when soaked in water and various levels of acid (vinegar) and base (baking soda) solutions. Under the experimental conditions of 35 unit TG and 28 min of reaction, the degrees of cross-linking were evidenced by the disappearance of individual protein subunits, except the basic subunit of glycinin, and the reduction of 21% of lysine residues of the proteins. HIGHLIGHTS: Edible soy films were made with transglutaminase and about 21% lysine cross-linked. The mechanical strength of soy films was increased by incorporating film enhancers. Transglutaminase enhanced the mechanical properties of soy films.


Subject(s)
Pectins , Soybean Proteins , Tensile Strength , Transglutaminases , Transglutaminases/chemistry , Transglutaminases/metabolism , Pectins/chemistry , Soybean Proteins/chemistry , Solubility , Whey Proteins/chemistry , Food Packaging/methods , Cross-Linking Reagents/chemistry , Glycine max/chemistry , Edible Films , Hydrogen-Ion Concentration , Soy Milk/chemistry
3.
Food Res Int ; 190: 114562, 2024 Aug.
Article in English | MEDLINE | ID: mdl-38945563

ABSTRACT

The structural and functional properties of whey-quercetin and whey hydrolysate-quercetin conjugates synthesized using alkaline and free radical-mediated methods (AM and FRM) coupled with sonication were studied. FTIR showed new peaks at 3000-3500 cm-1 (N-H stretching regions) and the 1000-1100 cm-1 region with the conjugates. Conjugation increased the random coils and α-helix content while decreasing the ß-sheets and turns. It also increased the particle size and surface hydrophobicity which was significantly (p < 0.05) higher in AM than FRM conjugates. AM conjugates had higher radical scavenging activity but lower quercetin content than FRM conjugates. Overall, the functional properties of whey-quercetin conjugates were better than whey hydrolysate-quercetin conjugates. However, hydrolysate conjugates had significantly higher denaturation temperatures irrespective of the method of production. Sonication improved the radical scavenging activity and quercetin content of FRM conjugates while it decreased both for AM conjugates. This study suggested that whey-quercetin conjugates generally had better quality than whey hydrolysate conjugates and sonication tended to further improve these properties. This study highlights the potential for using camel whey or whey hydrolysate-quercetin conjugates to enhance the functional properties of food products in the food industry.


Subject(s)
Camelus , Hydrophobic and Hydrophilic Interactions , Quercetin , Sonication , Quercetin/chemistry , Animals , Protein Hydrolysates/chemistry , Whey/chemistry , Antioxidants/chemistry , Whey Proteins/chemistry , Free Radical Scavengers/chemistry , Spectroscopy, Fourier Transform Infrared , Free Radicals/chemistry , Particle Size , Hydrogen-Ion Concentration
4.
Food Res Int ; 190: 114621, 2024 Aug.
Article in English | MEDLINE | ID: mdl-38945576

ABSTRACT

Ageing leads to changes in the functionality of the digestive tract but the effect of age on digestion and absorption of nutrients remains unclear. The objective of this study was to investigate in vitro the digestion of two high-protein dairy products similar to cream cheese (24 % w/w proteins, 20 % w/w lipids) with opposite casein to whey protein ratios, 80:20 (WP-20), and 20:80 (WP-80). The new static digestion model adapted to the general older adult population (≥65 y.) proposed by INFOGEST was used, as well as the standard version of the protocol. Kinetics of proteolysis and lipolysis were compared between both models for each product, in the gastric and intestinal phases of digestion. In both cream cheeses, the degree of protein hydrolysis (DH-P) was significantly lower for older adults than for young adults at the end of the gastric phase (-19 % for WP-20, and -44 % for WP-80), and at the end of the intestinal phase (-16 % for WP-20, and -20 % for WP-80). The degree of lipid hydrolysis (DH-L) was also significantly lower for older adults than for young adults at the end of the digestion for WP-20 (-30 %), but interestingly it was not the case for WP-80 (similar DH-L were measured). Free fatty acids were also released faster from WP-80 than from WP-20 in both digestion conditions: after 5 min of intestinal digestion DH-L was already ≈32 % for WP-80 against 14 % for WP-20. This was attributed to the opposite casein to whey protein ratios, leading to the formation of different gel structures resulting in different patterns of deconstruction in the gastrointestinal tract. This study highlights the fact that it is essential to carefully consider the composition, structure, and digestibility of foods to develop products adapted to the specific needs of the older adult population.


Subject(s)
Caseins , Cheese , Digestion , Proteolysis , Whey Proteins , Cheese/analysis , Whey Proteins/metabolism , Whey Proteins/chemistry , Caseins/metabolism , Humans , Aged , Hydrolysis , Adult , Lipolysis , Young Adult , Age Factors , Models, Biological , Kinetics
5.
Food Res Int ; 190: 114608, 2024 Aug.
Article in English | MEDLINE | ID: mdl-38945618

ABSTRACT

In dairy products, the added sodium hyaluronate may form complexes with proteins, thereby affecting product properties. In the present study, the interaction between whey protein isolate (WPI)/ whey protein hydrolysate (WPH) and sodium hyaluronate (SH) was characterized under thermal treatment at different temperatures (25 ℃, 65 ℃, 90 ℃ and 121 ℃) after studying effects of protein/SH ratio and pH on complex formation. The addition of SH reduced the particle size of WPI/WPH and increased potential value in the system, with greater variation with increasing treatment temperature. The structural properties of complexes were studied. The binding with SH decreased the contents of free amino group and free thiol group, as well as the fluorescence intensity and surface hydrophobicity. FTIR results and browning intensity measurement demonstrated the formation of Maillard reaction products. Moreover, the attachment of SH improved the thermal stability of WPI/WPH and decreased their antigenicity.


Subject(s)
Hot Temperature , Hyaluronic Acid , Protein Hydrolysates , Whey Proteins , Whey Proteins/chemistry , Hyaluronic Acid/chemistry , Protein Hydrolysates/chemistry , Hydrogen-Ion Concentration , Maillard Reaction , Hydrophobic and Hydrophilic Interactions , Particle Size , Spectroscopy, Fourier Transform Infrared , Food Handling/methods
6.
Biomed Mater ; 19(4)2024 Jun 28.
Article in English | MEDLINE | ID: mdl-38857605

ABSTRACT

Chronic skin wounds pose a global clinical challenge, necessitating effective treatment strategies. This study explores the potential of 3D printed Poly Lactic Acid (PLA) scaffolds, enhanced with Whey Protein Concentrate (WPC) at varying concentrations (25, 35, and 50% wt), for wound healing applications. PLA's biocompatibility, biodegradability, and thermal stability make it an ideal material for medical applications. The addition of WPC aims to mimic the skin's extracellular matrix and enhance the bioactivity of the PLA scaffolds. Fourier Transform Infrared Spectroscopy results confirmed the successful loading of WPC into the 3D printed PLA-based scaffolds. Scanning Electron Microscopy (SEM) images revealed no significant differences in pore size between PLA/WPC scaffolds and pure PLA scaffolds. Mechanical strength tests showed similar tensile strength between pure PLA and PLA with 50% WPC scaffolds. However, scaffolds with lower WPC concentrations displayed reduced tensile strength. Notably, all PLA/WPC scaffolds exhibited increased strain at break compared to pure PLA. Swelling capacity was highest in PLA with 25% WPC, approximately 130% higher than pure PLA. Scaffolds with higher WPC concentrations also showed increased swelling and degradation rates. Drug release was found to be prolonged with increasing WPC concentration. After seven days of incubation, cell viability significantly increased in PLA with 50% WPC scaffolds compared to pure PLA scaffolds. This innovative approach could pave the way for personalized wound care strategies, offering tailored treatments and targeted drug delivery. However, further studies are needed to optimize the properties of these scaffolds and validate their effectiveness in clinical settings.


Subject(s)
Bandages , Biocompatible Materials , Polyesters , Printing, Three-Dimensional , Tensile Strength , Tissue Scaffolds , Whey Proteins , Wound Healing , Whey Proteins/chemistry , Polyesters/chemistry , Tissue Scaffolds/chemistry , Wound Healing/drug effects , Humans , Biocompatible Materials/chemistry , Materials Testing , Spectroscopy, Fourier Transform Infrared , Microscopy, Electron, Scanning , Cell Survival/drug effects , Porosity , Drug Liberation , Skin/metabolism
7.
Int J Biol Macromol ; 273(Pt 2): 132878, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38844277

ABSTRACT

Granular hydrogels have emerged as a new class of materials for 3D printing, tissue engineering, and food applications due to their extrudability, porosity, and modularity. This work introduces a convenient method to prepare granular hydrogel with tunable properties by modulating the interaction between gum Arabic (GA) and whey protein isolate (WPI) microgels. As the concentration of GA increased, the appearance of the hydrogel changed from fluid liquid to moldable solid, and the microstructure changed from a macro-porous structure with thin walls to a dense structure formed by the accumulation of spherical particles. At a GA concentration of 0.5 %, the hydrogels remained fluid. Granular hydrogels containing 1.0 % GA showed mechanical properties similar to those of tofu (compressive strength: 10.8 ± 0.5 kPa, Young's modulus: 16.7 ± 0.4 kPa), while granular hydrogels containing 1.5 % GA showed mechanical properties similar to those of hawthorn sticks and sausages (compressive strength: 300.4 ± 5.8 kPa; Young's modulus: 200.5 ± 3.4 kPa). The hydrogel with 2.0 % GA was similar to hawthorn sticks, with satisfactory bite resistance and elasticity. Such tunability has led to various application potentials in the food industry to meet consumer demand for healthy, nutritious, and diverse textures.


Subject(s)
Gum Arabic , Hydrogels , Microgels , Whey Proteins , Gum Arabic/chemistry , Hydrogels/chemistry , Whey Proteins/chemistry , Microgels/chemistry , Elastic Modulus , Rheology , Porosity , Compressive Strength
8.
Int J Biol Macromol ; 273(Pt 2): 133079, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38942664

ABSTRACT

Proteins impact starch digestion, but the specific mechanism under heat-moisture treatment remains unclear. This study examined how proteins from various sources-white kidney bean, soybean, casein, whey-altered corn starch's structure, physicochemical properties, and digestibility during heat-moisture treatment (HMT). HMT and protein addition could significantly reduce starch's digestibility. The kidney bean protein-starch complex under HMT had the highest resistant starch at 19.74 %. Most proteins effectively inhibit α-amylase, with kidney bean being the most significantly (IC50 = 1.712 ± 0.085 mg/mL). HMT makes starch obtain a more rigid structure, limits its swelling ability, and reduces paste viscosity and amylose leaching. At the same time, proteins also improve starch's short-range order, acting as a physical barrier to digestion. Rheological and low-field NMR analyses revealed that protein enhanced the complexes' shear stability and water-binding capacity. These findings enrich the understanding of how proteins from different sources affect starch digestion under HMT, aiding the creation of nutritious, hypoglycemic foods.


Subject(s)
Digestion , Hot Temperature , Starch , Zea mays , alpha-Amylases , Starch/chemistry , alpha-Amylases/chemistry , alpha-Amylases/metabolism , Zea mays/chemistry , Viscosity , Chemical Phenomena , Water/chemistry , Plant Proteins/chemistry , Amylose/chemistry , Rheology , Whey Proteins/chemistry
9.
Food Res Int ; 188: 114433, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38823827

ABSTRACT

Whey derived peptides have shown potential activity improving brain function in pathological condition. However, there is little information about their mechanism of action on glial cells, which have important immune functions in brain. Astrocytes and microglia are essential in inflammatory and oxidative defense that take place in neurodegenerative disease. In this work we evaluate antioxidant and anti-inflammatory potential bioactivity of whey peptide in glial cells. Peptides were formed during simulated gastrointestinal digestion (Infogest protocol), and low molecular weight (<5kDA) peptides (WPHf) attenuated reactive oxygen species (ROS) production induced by hydrogen peroxide stimulus in both cells in dose-dependent manner. WPHf induced an increase in the antioxidant glutathione (GSH) content and prevented GSH reduction induced by lipopolysaccharides (LPS) stimulus in astrocytes cells in a cell specific form. An increase in cytokine mRNA expression (TNFα and IL6) and nitric oxide secretion induced by LPS was attenuated by WPHf pre-treatment in both cells. The inflammatory pathway was dependent on NFκB activation. Bioactive peptide ranking analysis showed positive correlation with hydrophobicity and negative correlation with high molecular weights. The sequence identification revealed 19 peptides cross-referred with bioactive database. Whey peptides were rich in leucine, valine and tyrosine in the C-terminal region and lysine in the N-terminal region. The anti-inflammatory and antioxidant potential of whey peptides were assessed in glia cells and its mechanisms of action were related, such as modulation of antioxidant enzymes and anti-inflammatory pathways. Features of the peptide structure, such as molecular size, hydrophobicity and types of amino acids present in the terminal region are associated to bioactivity.


Subject(s)
Anti-Inflammatory Agents , Antioxidants , Neuroglia , Whey Proteins , Antioxidants/pharmacology , Anti-Inflammatory Agents/pharmacology , Whey Proteins/pharmacology , Whey Proteins/chemistry , Whey Proteins/metabolism , Neuroglia/drug effects , Neuroglia/metabolism , Animals , Reactive Oxygen Species/metabolism , Lipopolysaccharides/pharmacology , Glutathione/metabolism , Peptides/pharmacology , Nitric Oxide/metabolism , Astrocytes/drug effects , Astrocytes/metabolism
10.
Food Res Int ; 188: 114352, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38823826

ABSTRACT

In the ongoing quest to formulate sensory-rich, low-fat products that maintain structural integrity, this work investigated the potential of bigels, especially those created using innovative Pickering techniques. By harnessing the unique properties of whey protein isolate (WPI) and whey protein microgel (WPM) as interfacial stabilizers, WPM-based Pickering bigels exhibited a remarkable particle localization at the interface due to specific intermolecular interactions. The rise in protein concentration not only intensified particle coverage and interface stabilization but also amplified attributes like storage modulus, yield stress, and adhesiveness, owing to enhanced intermolecular forces and a compact gel matrix. Impressively, WPM-based Pickering bigels outshone in practical applications, showcasing exceptional oil retention during freeze-thaw cycles and extended flavor release-a promising indication for frozen food product applications. Furthermore, these bigels underwent a sensory evolution from a lubricious texture at lower concentrations to a stable plateau at higher ones, offering an enriched consumer experience. In a comparative digestibility assessment, WPM-based Pickering bigels demonstrated superior prowess in decelerating the release of free fatty acids, indicating slowed lipid digestion. This study demonstrates the potential to fine-tune oral sensations and digestive profiles in bigels by modulating Pickering particle concentrations.


Subject(s)
Digestion , Microgels , Taste , Whey Proteins , Whey Proteins/chemistry , Humans , Microgels/chemistry , Food Handling/methods , Gastrointestinal Tract/metabolism , Sensation
11.
Food Res Int ; 188: 114453, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38823833

ABSTRACT

In this study, whipped cream with blends of micellar casein (MCN) and whey protein (WPI) in different ratios were prepared to investigate the role of protein interfacial behavior in determining foam properties at multiple scales, using theoretical modeling, and microscopic and macroscopic analysis. Fluid force microscopy has been used for the first time as a more realistic and direct means of analyzing interfaces properties in multiphase systems. The adsorption kinetics showed that the interfacial permeability constant of WPI (4.24 × 10-4 s-1) was significantly higher than that of the MCN (2.97 × 10-4 s-1), and the WPI interfacial layer had a higher modulus of elasticity (71.38 mN/m) than that of the MCN (47.89 mN/m). This model was validated via the mechanical analysis of the fat globules in real emulsions. The WPI-stabilized fat globule was found to have a higher Young's modulus (219.67 Pa), which contributes to the integrity of its fat globule morphology. As the ratio of MCN was increased in the sample, however, both the interfacial modulus and Young's modulus decreased. Moreover, the rate of partial coalescence was found to increase, a phenomenon that decreased the stability of the emulsion and increased the rate of aeration. The mechanical analysis also revealed a higher level of adhesion between MCN-stabilized fat globule (25.16 nN), which increased fat globule aggregation and emulsion viscosity, while improving thixotropic recovery. The synergistic effect of the blended MCN and WPI provided the highest overrun, at 194.53 %. These studies elucidate the role of the interfacial behavior of proteins in determining the quality of whipped cream and provide ideas for the application of proteins in multiphase systems.


Subject(s)
Caseins , Micelles , Whey Proteins , Whey Proteins/chemistry , Caseins/chemistry , Emulsions/chemistry , Dairy Products , Lipid Droplets/chemistry , Adsorption , Kinetics , Permeability , Food Handling/methods , Glycolipids/chemistry , Elastic Modulus , Viscosity , Glycoproteins
12.
Food Res Int ; 188: 114499, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38823844

ABSTRACT

The aim of this study was to evaluate the effect of the enzymatic hydrolysis, performed using Alcalase and Protamex enzymes, on the technological functionalities and the antioxidant capacity of whey protein hydrolysates (WPHs) to identify the conditions allowing to obtain target functionality/ies. Samples were characterized for hydrolysis degree (DH), molecular weight distribution, structural properties, and food-related functionalities. Free sulfhydryl groups and surface hydrophobicity significantly decreased with the increase in DH, regardless of the used enzyme. The foaming and antioxidant properties of Alcalase WPHs were higher as compared to those of WPI, reaching the maximum value at DH = 18-20 %, while higher DH resulted in impaired functionality. Gelling properties were guaranteed when WPI was hydrolysed by Protamex at DH < 15 % while foaming and antioxidant abilities were fostered at 15 < DH < 21 %. These results were well correlated with MW distribution and were rationalized into a road map which represents a useful tool in the selection of proper hydrolysis conditions (time, DH, enzyme type) to obtain WPHs with tailored functionalities. Research outcomes highlighted the possibility to drive protein hydrolysis to optimize the desired functionality/ies.


Subject(s)
Antioxidants , Hydrophobic and Hydrophilic Interactions , Protein Hydrolysates , Whey Proteins , Antioxidants/chemistry , Whey Proteins/chemistry , Hydrolysis , Protein Hydrolysates/chemistry , Subtilisins/metabolism , Subtilisins/chemistry , Molecular Weight , Subtilisin/metabolism , Subtilisin/chemistry
13.
Food Res Int ; 188: 114341, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38823851

ABSTRACT

Spatiotemporal assessment of lipid and protein oxidation is key for understanding quality deterioration in emulsified food products containing polyunsaturated fatty acids. In this work, we first mechanistically validated the use of the lipid oxidation-sensitive fluorophore BODIPY 665/676 as a semi-quantitative marker for local peroxyl radical formation. Next, we assessed the impact of microfluidic and colloid mill emulsification (respectively producing mono- and polydisperse droplets) on local protein and lipid oxidation kinetics in whey protein isolate (WPI)-stabilized emulsions. We further used BODIPY 581/591 C11 and CAMPO-AFDye 647 as colocalisation markers for lipid and protein oxidation. The polydisperse emulsions showed an inverse relation between droplet size and lipid oxidation rate. Further, we observed less protein and lipid oxidation occurring in similar sized droplets in monodisperse emulsions. This observation was linked to more heterogeneous protein packing at the droplet surface during colloid mill emulsification, resulting in larger inter-droplet heterogeneity in both protein and lipid oxidation. Our findings indicate the critical roles of emulsification methods and droplet sizes in understanding and managing lipid oxidation.


Subject(s)
Emulsions , Oxidation-Reduction , Particle Size , Whey Proteins , Whey Proteins/chemistry , Emulsions/chemistry , Boron Compounds/chemistry , Kinetics , Peroxides/chemistry , Lipids/chemistry
14.
Nutrients ; 16(11)2024 May 25.
Article in English | MEDLINE | ID: mdl-38892554

ABSTRACT

This study examined whey protein's impact on insulin resistance in a high-fat diet-induced pediatric obesity mouse model. Pregnant mice were fed high-fat diets, and male pups continued this diet until 8 weeks old, then were split into high-fat, whey, and casein diet groups. At 12 weeks old, their body weight, fasting blood glucose (FBG), blood insulin level (IRI), homeostatic model assessment for insulin resistance (HOMA-IR), liver lipid metabolism gene expression, and liver metabolites were compared. The whey group showed significantly lower body weight than the casein group at 12 weeks old (p = 0.034). FBG was lower in the whey group compared to the high-fat diet group (p < 0.01) and casein group (p = 0.058); IRI and HOMA-IR were reduced in the whey group compared to the casein group (p = 0.02, p < 0.01, p < 0.01, respectively). The levels of peroxisome proliferator-activated receptor α and hormone-sensitive lipase were upregulated in the whey group compared to the casein group (p < 0.01, p = 0.03). Metabolomic analysis revealed that the levels of taurine and glycine, both known for their anti-inflammatory and antioxidant properties, were upregulated in the whey group in the liver tissue (p < 0.01, p < 0.01). The intake of whey protein was found to improve insulin resistance in a high-fat diet-induced pediatric obesity mouse model.


Subject(s)
Diet, High-Fat , Disease Models, Animal , Insulin Resistance , Liver , Pediatric Obesity , Whey Proteins , Animals , Whey Proteins/pharmacology , Diet, High-Fat/adverse effects , Male , Mice , Pediatric Obesity/metabolism , Liver/metabolism , Liver/drug effects , Female , Blood Glucose/metabolism , Insulin/blood , Lipid Metabolism/drug effects , Pregnancy , Mice, Inbred C57BL
15.
Nutrients ; 16(11)2024 May 30.
Article in English | MEDLINE | ID: mdl-38892645

ABSTRACT

The current state of the literature lacks a clear characterization of gastrointestinal (GI) symptoms, gut microbiota composition, and general physical and mental wellbeing in well-trained athletes. Therefore, this study aimed to characterize differences in self-reported symptoms, gut microbiota composition, and wellbeing (i.e., sleep quality, mood, and physical (PHQ) and mental wellbeing) between athletes with and without GI symptoms. In addition, we assessed the potential impact of a 3-week multi-ingredient fermented whey supplement in the GI complaints group, without a control group, on the gut microbiota and self-reported GI symptoms and wellbeing. A total of 50 athletes (24.7 ± 4.5 years) with GI issues (GI group at baseline, GI-B) and 21 athletes (25.4 ± 5.3 years) without GI issues (non-GI group, NGI) were included. At baseline, there was a significant difference in the total gastrointestinal symptom rating scale (GSRS) score (24.1 ± 8.48 vs. 30.3 ± 8.82, p = 0.008) and a trend difference in PHQ (33.9 ± 10.7 vs. 30.3 ± 8.82, p = 0.081), but no differences (p > 0.05) were seen for other outcomes, including gut microbiota metrics, between groups. After 3-week supplementation, the GI group (GI-S) showed increased Bifidobacterium relative abundance (p < 0.05), reported a lower number of severe GI complaints (from 72% to 54%, p < 0.001), and PHQ declined (p = 0.010). In conclusion, well-trained athletes with GI complaints reported more severe GI symptoms than an athletic reference group, without showing clear differences in wellbeing or microbiota composition. Future controlled research should further investigate the impact of such multi-ingredient supplements on GI complaints and the associated changes in gut health-related markers.


Subject(s)
Athletes , Dietary Supplements , Gastrointestinal Diseases , Gastrointestinal Microbiome , Mental Health , Self Report , Humans , Athletes/psychology , Male , Gastrointestinal Diseases/microbiology , Female , Adult , Young Adult , Whey Proteins/administration & dosage
16.
Molecules ; 29(11)2024 May 31.
Article in English | MEDLINE | ID: mdl-38893466

ABSTRACT

Epigallocatechin gallate (EGCG), the principal catechin in green tea, exhibits diverse therapeutic properties. However, its clinical efficacy is hindered by poor stability and low bioavailability. This study investigated solid particle-in-oil-in-water (S/O/W) emulsions stabilized by whey protein isolate (WPI) and sodium caseinate (NaCas) as carriers to enhance the bioavailability and intestinal absorption of EGCG. Molecular docking revealed binding interactions between EGCG and these macromolecules. The WPI- and NaCas-stabilized emulsions exhibited high encapsulation efficiencies (>80%) and significantly enhanced the bioaccessibility of EGCG by 64% compared to free EGCG after simulated gastrointestinal digestion. Notably, the NaCas emulsion facilitated higher intestinal permeability of EGCG across Caco-2 monolayers, attributed to the strong intermolecular interactions between caseins and EGCG. Furthermore, the emulsions protected Caco-2 cells against oxidative stress by suppressing intracellular reactive oxygen species generation. These findings demonstrate the potential of WPI- and NaCas-stabilized emulsions as effective delivery systems to improve the bioavailability, stability, and bioactivity of polyphenols like EGCG, enabling their applications in functional foods and nutraceuticals.


Subject(s)
Biological Availability , Caseins , Catechin , Emulsions , Whey Proteins , Catechin/analogs & derivatives , Catechin/chemistry , Humans , Whey Proteins/chemistry , Caseins/chemistry , Caco-2 Cells , Emulsions/chemistry , Molecular Docking Simulation , Reactive Oxygen Species/metabolism , Oxidative Stress/drug effects , Drug Carriers/chemistry , Antioxidants/pharmacology , Antioxidants/chemistry , Antioxidants/pharmacokinetics , Intestinal Absorption/drug effects
17.
Int J Mol Sci ; 25(11)2024 May 27.
Article in English | MEDLINE | ID: mdl-38892006

ABSTRACT

There is increasing evidence about the role of inflammation in sarcopenia and tumor progression; thus, its modulation would represent a valuable strategy for improving clinical outcomes in patients with cancer. Several studies have reported that whey protein has significant anti-inflammatory and antioxidant characteristics in humans. We aimed to evaluate the effects of whey protein-based oral nutritional support on circulating cytokines in patients with solid tumors undergoing systemic treatment. Forty-six patients with solid tumors of different origin and undergoing systemic treatment were evaluated. Nutritional support with two daily whey protein-based oral supplements was administered. Circulating levels of IL-6, IL-8, IL-10, MCP-1 and IP-10 were determined. Nutritional evaluation included anthropometric, instrumental and biochemical parameters. Over 63% of the evaluated patients underwent surgery, 56.5% required chemotherapy and almost 50% received combined treatment. Patients with resected primary tumor presented with lower baseline IL-6 (p < 0.05) and IP-10 (p < 0.001); after three months of nutritional support, they presented with lower IL-8 (p < 0.05) and tended to present lower IL-6 and IP-10 (p = 0.053 and 0.067, respectively). Significant positive correlations between circulating cytokines, C-reactive protein and ferritin were observed; similarly, negative correlations with anthropometric and biochemical nutritional parameters were noticed (p < 0.05). We did not observe significant changes in circulating cytokine levels (IL-6, IL-8, IL-10, MCP-1 and IP-10) in patients with cancer undergoing systemic treatment after three months of nutritional support with whey protein-based oral supplements. According to a univariate analysis in our cohort, circulating IL-8 was associated with mortality in these patients, additionally, MCP-1 and IP-10 tended to correlate; but an age- and sex-adjusted multivariate analysis revealed that only baseline MCP-1 was significantly associated with mortality (OR 1.03 (95% CI: 1.00-1.05)). In conclusion, surgery of the primary solid tumor and combination treatment allow significant reduction in circulating cytokine levels, which remained stable while patients received nutritional support with whey protein-based oral supplements over three months. The role of MCP-1 as an independent factor for mortality in these patients should be further evaluated.


Subject(s)
Cytokines , Inflammation , Neoplasms , Nutritional Support , Whey Proteins , Humans , Female , Male , Middle Aged , Aged , Inflammation/blood , Nutritional Support/methods , Cytokines/blood , Adult , Dietary Supplements , Chemokine CCL2/blood
18.
Food Res Int ; 188: 114485, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38823871

ABSTRACT

Whey protein isolate (WPI) is mainly composed of ß-lactoglobulin (ß-LG), α-lactalbumin (α-LA) and bovine serum albumin (BSA). The aim of this study was to compare and analyze the influence of WPI and its three main constituent proteins, as well as proportionally reconstituted WPI (R-WPI) on resveratrol. It was found that the storage stability of resveratrol was protected by WPI, not affected by R-WPI, but reduced by individual whey proteins at 45°C for 30 days. The rank of accelerated degradation of resveratrol by individual whey proteins was BSA > α-LA > ß-LG. The antioxidant activity, localization of resveratrol and oxidation of carrier proteins were determined by ABTS, H2O2 assay, synchronous fluorescence, carbonyl and circular dichroism. The non-covalent interactions and disulfide bonds between constituent proteins improved the antioxidant activity of the R-WPI-resveratrol complex, the oxidation stability of the carrier and the solvent shielding effect on resveratrol, which synergistically inhibited the degradation of resveratrol in R-WPI system. The results gave insight into elucidating the interaction mechanism of resveratrol with protein carriers.


Subject(s)
Antioxidants , Lactalbumin , Lactoglobulins , Oxidation-Reduction , Resveratrol , Serum Albumin, Bovine , Whey Proteins , Resveratrol/chemistry , Resveratrol/pharmacology , Whey Proteins/chemistry , Lactalbumin/chemistry , Antioxidants/chemistry , Antioxidants/pharmacology , Lactoglobulins/chemistry , Serum Albumin, Bovine/chemistry , Circular Dichroism
19.
Clin Nutr ; 43(7): 1747-1758, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38850996

ABSTRACT

BACKGROUND & AIM: Patients with an ileostomy are at increased risk of dehydration and sodium depletion. Treatments recommended may include oral rehydration solutions (ORS). We aimed to investigate if protein type or protein hydrolysation affects absorption from iso-osmolar ORS in patients with an ileostomy. METHODS: This was a randomised, double-blinded, active comparator-controlled 3 × 3 crossover intervention study. We developed three protein-based ORS with whey protein isolate, caseinate or whey protein hydrolysate. The solutions contained 40-48 g protein/L, 34-45 mmol sodium/L and had an osmolality of 248-270 mOsm/kg. The patients ingested 500 mL/d. The study consisted of three 4-week periods with a >2-week washout between each intervention. The primary outcome was wet-weight ileostomy output. Ileostomy output and urine were collected for a 24-h period before and after each intervention. Additionally, blood sampling, dietary records, muscle-strength tests, bioimpedance analyses, questionnaires and psychometric tests were conducted. RESULTS: We included 14 patients, of whom 13 completed at least one intervention. Ten patients completed all three interventions. Wet-weight ileostomy output did not change following either of the three interventions and did not differ between interventions (p = 0.38). A cluster of statistically significant improvements related to absorption was observed following the intake of whey protein isolate ORS, including decreased faecal losses of energy (-365 kJ/d, 95% confidence interval (CI), -643 to -87, p = 0.012), potassium (-7.8 mmol/L, 95%CI, -12.0 to -3.6, p = 0.001), magnesium (-4.0 mmol/L, 95%CI, -7.4 to -0.7, p = 0.020), improved plasma aldosterone (-4674 pmol/L 95%CI, -8536 to -812, p = 0.019), estimated glomerular filtration rate (eGFR) (2.8 mL/min/1.73 m2, 95%CI, 0.3 to 5.4, p = 0.03) and CO2 (1.7 mmol/L 95%CI, 0.1 to 3.3, p = 0.04). CONCLUSION: Ingestion of 500 mL/d of iso-osmolar solutions containing either whey protein isolate, caseinate or whey protein hydrolysate for four weeks resulted in unchanged and comparable ileostomy outputs in patients with an ileostomy. Following whey protein isolate ORS, we observed discrete improvements in a series of absorption proxies in both faeces and blood, indicating increased absorption. The protein-based ORS were safe and well-tolerated. Treatments should be tailored to each patient, and future studies are warranted to explore treatment-effect heterogeneity and whether different compositions or doses of ORS can improve absorption and nutritional status in patients with an ileostomy. GOV STUDY IDENTIFIER: NCT04141826.


Subject(s)
Cross-Over Studies , Fluid Therapy , Ileostomy , Rehydration Solutions , Whey Proteins , Humans , Double-Blind Method , Male , Female , Whey Proteins/administration & dosage , Middle Aged , Aged , Rehydration Solutions/administration & dosage , Fluid Therapy/methods , Dehydration/therapy , Caseins/administration & dosage , Protein Hydrolysates/administration & dosage , Adult
20.
Int J Biol Macromol ; 272(Pt 1): 132843, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38830489

ABSTRACT

The study aimed to inhibit the stimulating impact of garlic oil (GO) on the stomach and attain high release in the intestine during digestion. So, wheat porous starch (WPS) was modified with octenyl succinic acid (OSA) and malic acid (MA) to obtain esterified WPS, OWPS and MWPS, respectively. The differences in physicochemical, encapsulation, and digestive properties of two GO microcapsules, WPI/OWPS/GO and WPI/MWPS/GO microcapsules produced by using OWPS and MWPS as variant carrier materials and whey protein isolate (WPI) as the same coating agent, were compared. The results found that OWPS had greater amphiphilicity, while MWPS had better hydrophobicity and anti-digestive ability than WPS. Encapsulation efficiency of WPI/OWPS/GO (94.67 %) was significantly greater than WPI/MWPS/GO (91.44 %). The digestion inhibition and low GO release (approximately 23 %) of WPI/OWPS/GO and WPI/MWPS/GO microcapsules in the gastric phase resulted from the protective effect of WPI combined with the good adsorption and lipophilicity of OWPS and MWPS. Especially, WPI/OWPS/GO microcapsule was relatively stable in the gastric phase and had sufficient GO release (67.24 %) in the intestinal phase, which was significantly higher than WPI/MWPS/GO microcapsule (56.03 %), benefiting from the adsorption and digestive properties of OWPS, and resulting in a total cumulative GO release rate of 90.86 %.


Subject(s)
Digestion , Starch , Triticum , Whey Proteins , Whey Proteins/chemistry , Starch/chemistry , Triticum/chemistry , Porosity , Capsules , Chemical Phenomena , Plant Oils/chemistry , Hydrophobic and Hydrophilic Interactions , Drug Compounding , Garlic/chemistry
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