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1.
Nutrients ; 16(13)2024 Jun 26.
Article in English | MEDLINE | ID: mdl-38999765

ABSTRACT

Animal-sourced whey protein (WPr) is the most popular protein supplement among consumers and has been shown to improve muscle mass and strength. However, due to allergies, dietary restrictions/personal choices, and growing demand, alternative protein sources are warranted. Sedentary adults were randomized to pea protein (PPr) or WPr in combination with a weekly resistance training program for 84 days. Changes in whole-body muscle strength (WBMS) including handgrip, lower body, and upper body strength, body composition, and product perception were assessed. The safety outcomes included adverse events, vital signs, clinical chemistry, and hematology. There were no significant differences in the change in WBMS, muscle mass, or product perception and likability scores between the PPr and WPr groups. The participants supplemented with PPr had a 16.1% improvement in WBMS following 84 days of supplementation (p = 0.01), while those taking WPr had an improvement of 11.1% (p = 0.06). Both study products were safe and well-tolerated in the enrolled population. Eighty-four days of PPr supplementation resulted in improvements in strength and muscle mass comparable to WPr when combined with a resistance training program in a population of healthy sedentary adults. PPr may be considered as a viable alternative to animal-sourced WPr without sacrificing muscular gains and product enjoyment.


Subject(s)
Dietary Supplements , Muscle Strength , Muscle, Skeletal , Pea Proteins , Resistance Training , Sedentary Behavior , Humans , Male , Female , Adult , Pea Proteins/administration & dosage , Muscle Strength/physiology , Muscle, Skeletal/physiology , Whey Proteins/administration & dosage , Middle Aged , Young Adult , Body Composition , Hand Strength
2.
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
3.
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
4.
Food Res Int ; 191: 114622, 2024 Sep.
Article in English | MEDLINE | ID: mdl-39059896

ABSTRACT

This study was aimed to evaluate the effect of heat damage on the release of total amino acids (AA), essential AA (EAA), branched-chain AA (BCAA) and bioactive peptides following in vitro static simulated gastrointestinal digestion (SGID) of four commercial whey-protein based sports supplements. The extent of protein glycation and denaturation was evaluated through the determination of the content of furosine and soluble whey proteins. The strongest protein breakdown (41.3 %) and the highest release of AA, EAA and BCAA (36.20, 27.78, and 11.30 g/100 g protein, respectively) was observed in the sports supplement characterised by the lowest (52.5 %) level of soluble whey proteins; whereas the protein glycation had a negligible impact on the studied parameters. The SGID also led to the release of several peptides with various reported bioactivities that may be beneficial to sports activity.


Subject(s)
Amino Acids , Dietary Supplements , Digestion , Hot Temperature , Whey Proteins , Amino Acids/analysis , Amino Acids/metabolism , Gastrointestinal Tract/metabolism , Peptides , Protein Denaturation , Proteolysis , Humans , Lysine/analogs & derivatives
5.
Food Res Int ; 191: 114675, 2024 Sep.
Article in English | MEDLINE | ID: mdl-39059937

ABSTRACT

In present study, whey protein isolate fibrils and sodium alginate complexes (WPIFs-SA) were prepared and further used to stabilize Pickering emulsions for lycopene delivery. The optimal interaction between WPIFs and SA occurred at pH 3.0, with a mass ratio of 2:1. Increasing the oil fractions and the content of WPIFs-SA complexes significantly improved Pickering emulsions' stability, concurrently reducing droplet size and increasing viscoelasticity. Meanwhile, it facilitated the formation of a thicker protective layer and a compact network structure around the oil droplets, offering better protection for lycopene against thermal and photo degradation. In vitro digestion studies revealed that as the oil fractions and complex contents increased, the lipolysis degree decreased. The engineered WPIFs-SA Pickering emulsion could be used as an innovative delivery system for the protection and delivery of lycopene.


Subject(s)
Alginates , Emulsions , Lycopene , Whey Proteins , Whey Proteins/chemistry , Alginates/chemistry , Lycopene/chemistry , Hydrogen-Ion Concentration , Digestion , Viscosity , Particle Size , Carotenoids/chemistry , Lipolysis , Glucuronic Acid/chemistry , Hexuronic Acids/chemistry
6.
Ultrason Sonochem ; 108: 106983, 2024 Aug.
Article in English | MEDLINE | ID: mdl-39002225

ABSTRACT

Mulberry leaf protein (MLP) is a nutrient-rich protein, but its applicability is limited because of its poor solubility. To address this issue, this study combines MLP with whey protein isolates (WPI), known for the high nutritional value, and subsequently forms composite protein nanoparticles using the ultrasound-assisted pH shifting method. Microscopic observation and SDS-PAGE confirmed the binding between these two proteins. Fluorescence spectra and Fourier Transform infrared spectroscopy (FTIR) analysis supported the involvement of electrostatic interactions, hydrophobic attractions, and hydrogen bonding in the formation of stable complex nanoparticles. The interactions between the proteins became stronger after ultrasound-assisted pH-shifting treatment. Solubility, emulsification capacity, foaming, and antioxidant activity, among other indicators, demonstrate that the prepared composite nanoparticles exhibit favorable functional properties. The study successfully illustrates the creation of protein-based complex nanoparticles through the ultrasound-assisted pH shifting method, with potential applications in the delivery of bioactive compounds.


Subject(s)
Morus , Plant Leaves , Plant Proteins , Whey Proteins , Morus/chemistry , Plant Leaves/chemistry , Plant Proteins/chemistry , Whey Proteins/chemistry , Hydrogen-Ion Concentration , Ultrasonic Waves , Solubility , Antioxidants/chemistry , Nanoparticles/chemistry
7.
J Anim Sci ; 1022024 Jan 03.
Article in English | MEDLINE | ID: mdl-38995038

ABSTRACT

Fermentation of dietary and endogenous protein in the hindgut is generally considered detrimental to the health of pigs. We investigated the in vitro fermentation potential of porcine endogenous protein in ileal digesta and colonic mucus, using a N-free buffer with an excess of fermentable carbohydrates. Urea, whey protein isolate (WPI, positive control), WPI hydrolysate (WPIH), and combinations of the latter two were used to validate the assay. A new biphasic model, including a linear end simulation, fitted to the gas production data over a 48-h period identified the time point when substrate fermentation ended. A higher degree of hydrolysis of WPI resulted in a higher maximum gas production rate (Rmax, P < 0.01). Differences in Rmax and the time required to reach Rmax were observed among ileal digesta samples, with Rmax increasing with the insoluble protein content, and the highest Rmax occurring with colonic mucus samples (P < 0.05). The endogenous proteins entering the large intestine of pigs can ferment more rapidly compared to highly soluble and digestible protein sources, with Rmax positively correlated with decreasing solubility of endogenous nitrogenous components.


Protein fermentation in the hindgut of pigs can impact their health, affecting factors like growth rates and feed efficiency. Besides dietary protein, up to 50% of the protein entering the large intestine of growing pigs may be of endogenous origin. Therefore, we explored the fermentation potential of endogenous proteins compared to a well-known protein source, whey protein isolate (WPI). In developing and validating an in vitro gas production technique, we employed urea, WPI, WPI hydrolysate, and various combinations as substrates. The study introduces a new biphasic model for in vitro gas production, offering a detailed analysis of the fermentation process over a 48-h period. Our results revealed that porcine endogenous proteins can undergo rapid fermentation because the maximum gas production rate was higher compared to WPI. This insight is crucial for understanding the dynamics of protein fermentation in pigs. Additionally, we explored the solubility and molecular size of proteins, providing a comprehensive understanding of their fermentation characteristics. We found that endogenous proteins were less soluble compared to WPI but contained more smaller peptides. Unraveling the complexities of protein fermentation in pigs contributes to improvement of feed formulation for optimal gut health.


Subject(s)
Dietary Proteins , Fermentation , Animals , Swine , Dietary Proteins/metabolism , Digestion/physiology , Ileum/metabolism , Colon/metabolism , Colon/microbiology , Whey Proteins/metabolism , Gastrointestinal Contents/chemistry
8.
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
9.
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
10.
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
11.
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
12.
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
13.
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
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 , Insulin Resistance , Pediatric Obesity , Whey Proteins , Animals , Female , Male , Mice , Pregnancy , Blood Glucose/metabolism , Diet, High-Fat/adverse effects , Disease Models, Animal , Insulin/blood , Lipid Metabolism/drug effects , Liver/metabolism , Liver/drug effects , Mice, Inbred C57BL , Pediatric Obesity/metabolism , Whey Proteins/pharmacology
15.
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
16.
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
17.
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
18.
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
19.
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
20.
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
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