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The glycomacropeptide (GMP) present in the cheese whey byproduct can be an excellent antifreezing agent due to its unique molecular structure. The objective of this study was to concentrate this peptide and investigate its ice recrystallization inhibition (IRI) ability. Heat denaturation of the non-GMP proteins and preparative liquid chromatography were used to create fraction 1 (F1) and fraction 2 (F2) and these were tested using the splat assay and a modified sucrose sandwich assay to investigate their IRI activity. Both F1 and F2 showed moderate IRI activity, but this activity was strongest under low salt and low pH conditions as indicated by the regression trends. F1 demonstrated an ice shaping ability similar to that of antifreeze glycoproteins. Molecular dynamic simulations of GMP, de-glycosylated GMP, and alpha-lactalbumin were performed and confirmed substantial differences of GMP when compared to the others in its high degree of conformational diversity and flexibility, as shown by the combination of radius of gyration, solvent accessible surface area, secondary structure, and hydrogen-bonding measurements together. Thus, GMP was shown for the first time as an effective IRI agent and its concentrate can be feasibly obtained from dairy processing byproduct., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

This study employed spectroscopic methods to investigate the interactions between whey protein isolate/polysaccharide (WPI/PS) complexes and curcumin. The UV-visible absorption spectra and fluorescence spectra indicated effective binding of curcumin to WPI and its complexes with chitosan (CS), carrageenan (CAR) and carboxymethylcellulose (CMC). This binding significantly increased the UV-visible absorption intensity of curcumin, with its maximum fluorescence emission peak shifting from 552 nm to 510 nm. Fluorescence kinetics analysis suggested that the binding constant between curcumin and WPI/CS complexes reached a maximum of 4.0794 × 10 5  L/mol. Circular dichroism and infrared spectroscopy indicated that the higher binding constant was attributed to the binding of CS, which reduced the α-helix structure and exposed hydrophobic groups of WPI. Curcumin entrapped by WPI/CS complexes showed the highest DPPH radical scavenging activities, UV and thermal stability. In summary, the WPI/CS complexes effectively protect curcumin against various environmental stresses and maintain its antioxidant properties., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Glycation elicits diverse effects on the digestion of caseins and whey proteins in a goat protein model system (40 % casein,60 % whey proteins). Caseins generated longer peptides in the digesta of heated vs unheated samples. The further cleavage of casein peptides was hindered by dry heating, which might be induced by glycated modification. This reduced cleavage of casein peptides may also explain the decreased intensity of casein-derived bioactive peptides. Moreover, dry heating for 72 h significantly decreased the total intensity and number of whey protein-derived peptides. Whey protein-derived peptides in heated samples were shorter than those in unheated samples, and the cleavage sites of whey proteins were notably influenced. Dry heating increased the intensity of whey protein-derived bioactive peptides. These changes also affected the predicted bioactivity of peptides in the digesta, which may influence infant health. This study offers insights into the infant digestion of milk proteins into peptides., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

The intricate interactions between stevioside (STE) and milk protein (mixtures of whey protein isolate and sodium caseinate, WPI/SC) as well as interfacial stabilization mechanisms were investigated. At the molecular scale, it was observed that the incorporation of the steviol hydrophobic skeleton enhanced the surface hydrophobicity of WPI/SC (from 1560.73 to 2175.63), favoring the reduction of the energy barrier for adsorption. At the mesoscopic scale, the analysis of adsorption kinetics and interfacial dilatational rheological response revealed that STE and WPI/SC had a synergistic effect on the attenuation of oil-water interfacial tension, with the lowest value of interfacial tension of 9.46 mN/m. Meanwhile, at low concentrations of STE, the WPI/SC-STE complexes unfolded and self-assembled at the interface to form a spring-like interfacial layer that relaxed in response to external deformation. In contrast, at high concentrations of STE, it gradually replaced WPI/SC-STE complexes at the interface and destabilized the interfacial layer., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The effects and mechanisms of four exogenous proteins, soy protein isolate (SPI), pea protein isolate (PPI), egg white protein (EWP), and whey protein isolate (WPI), on the gelation of Meretrix meretrix (MM) surimi were investigated. The exogenous protein addition significantly increased the G* of samples to 1.36-1.60 folds compared to the MM group, and the MM/EWP sample presented a better time-stable structure. Furthermore, the incorporation of SPI and EWP reduced expressible water content by 17.51 % and 21.61 % in MM gel, respectively. Moreover, SPI and PPI interacted with water to act as fillers within the MM matrix, where SPI formed larger self-aggregations than PPI. A double cross-linked network was generated by EWP and MM protein, and WPI increased the interaction with MM protein as a binder. This research could provide a theoretical basis for the processing and utilization of exogenous proteins in MM., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Herein, we prepared a new aerogel-based preservation pad using soy hull nanocellulose (SHNC), polyvinyl alcohol (PVA), whey protein isolate (WPI), and cinnamon essential oil (CEO) as raw materials. The physicochemicals of the aerogel preservation pads were studied, and their effects on beef preservation were evaluated. The results showed that the aerogel monomers were crosslinked by hydrogen, ester bonds, and electrostatic interactions in the aerogels, and there were three-dimensional pores in the aerogels. Meanwhile, SHNC/PVA/WPI/CEO-3 (aerogel prepared using 2 g of SHNC) exhibited excellent mechanical properties (elongation: 251 %; tensile strength: 33.97 MPa) and super-high absorption performance. Additionally, the aerogel displayed excellent antioxidant and antibacterial properties (83.74 %). The preservation experiment showed that, at 4 °C, the aerogel preservation pad inhibited the growth and reproduction of bacteria on the surface of beef, inhibited lipid oxidation, effectively preserved the color of beef, and extended the shelf life of beef from 4 to 12 days., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Bovine whey contains bioactive proteins that could benefit consumer health, but their intact bioactivity depends on their ability to survive the digestive process and remain intact to their sites of action. Our study assessed whey protein degradation in the adult human jejunum after whey protein isolate ingestion and during static in vitro gastric and intestinal digestions, using LC-MS/MS-based proteomics and SDS-PAGE. We found that 53 % of the protein counts identified in the gastric digesta, including β-lactoglobulin and lactoferrin were stable under simulated gastric conditions. However, most proteins were degraded during both in vitro and in vivo intestinal digestion. The intact protein survival profiles were closely aligned between in vitro and in vivo digestion samples. Understanding the survival of specific whey proteins during digestion will help determine their biological relevancy in their intact forms within the gastrointestinal tract and may inspire strategies to enhance their stability for specific functions., Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: David Dallas reports financial support was provided by BUILD Dairy. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Authors. Published by Elsevier Ltd.. All rights reserved.)

The strong polyelectrolyte dextran sulfate (DS) is an anionic polysaccharide with a high negative charge, characterized by high stability and pH independence. DS and whey protein isolate (WPI) were selected to study the specific effects of highly negatively charged polysaccharides on the phase behavior and interaction of WPI/DS complexes (1 % w/v) under varying external conditions (pH, WPI:DS ratio, and salt addition). The phase diagrams, zeta potential, and laser confocal scanning microscopy measurements indicated that the WPI/DS complexes did not dissociate even at pH 1 due to the pH independence of DS. The exclusion volume effect of DS promoted WPI self-aggregation at high salt concentrations, which inhibited acidification-induced dissociation. Isothermal titration calorimetry indicated that the WPI/DS interaction is a spontaneous exothermic reaction driven by both enthalpy and entropy changes due to electrostatic interactions. This study provides valuable information on the interactions between highly negatively charged polysaccharides and proteins., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Soft gels based on protein-polysaccharide composite systems play a crucial role in the dietary management of people with dysphagia. The effect of chia seed gum (CSG) on the gelling and swallowing properties of heat-induced whey protein isolate (WPI) gels (3.125-75 mg/mL) was investigated. The results showed that adding CSG reduced the gelation concentration of WPI and weak gels could form at 12.5 mg/mL WPI concentration. In addition, the viscoelasticity and water-binding capacity of the WPI/CSG composite gels were gradually enhanced with increasing WPI concentrations. The WPI/CSG composite systems can be classified as level 2-5 dysphagia-oriented foods according to the International Dysphagia Diet Standardization Initiative (IDDSI) framework. The incorporation of CSG promoted the cross-linking of protein aggregates and the formation of compact and continuous network structures, resulting in improved gelling properties of composite systems. This study contributes to the development of novel soft gel-type dysphagia foods with better textural characteristics., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Polymerised whey is widely used in dairy products and can affect digestibility when its high-molecular-weight aggregates and gel structure are modified. This study investigated the digestibility, peptide profiles and satiety of modified whey protein isolate (MWPI) pre-heated with transglutaminase. Results showed that 43.06 % of MWPI was digested during the 4-h in vitro digestion, indicating a slow digestion rate. Compared with whey protein isolate (WPI), MWPI yielded 103 peptides with higher abundance following in vitro digestion, including 17 angiotensin-converting enzyme inhibitors and 1 dipeptidyl peptidase-4 inhibitor. Visual analytics indicated differential peptides located at distinct α-helix and β-sheet of β-lactoglobulin, α-lactalbumin and bovine serum albumin. MWPI gavage extended stomach retention time, decreased intestinal propulsion rate from 75.60 % (WPI group) to 33.72 % in 30 min and enhanced satiety within 120 min compared with WPI. Overall, whey polymerisation modulates protein-enzyme interactions, releasing different peptides and enhancing satiety., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Two whey protein isolate amyloid fibrils (WPIF) with different structure were prepared, and the effects of these structures on binding of β-carotene (BC) and in vitro digestibility were evaluated. Whey protein isolate (WPI) in water (80 °C, pH 2.0) self-assembled into elongated WPIF (E-WPIF), whereas WPI formed to worm-like WPIF (W-WPIF) in trifluoroethanol. Compared to E-WPIF, W-WPIF showed higher surface hydrophobicity, indicating exposure of more hydrophobic residues. The encapsulation efficiency and loading capacity of BC in W-WPIF were higher than that of E-WPIF. The hydrophobic interaction were the main driving forces of WPIF/BC. During gastric digestion, WPIF lost intact fibrils structures, resulting in unordered small aggregates and most BC still bound to them. Then they were destroyed in the following intestinal digestion, leading to the release of BC. Compared with W-WPIF/BC, E-WPIF/BC had higher release of BC in gastrointestinal digestion due to weaker binding of BC and better digestibility of E-WPIF., Competing Interests: Declaration of competing interest The authors confirm that they had no conflicts of interest with respect to the work described in this manuscript., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The phenolic compounds (PC) present in the pulp flour of Cantaloupe melon (Cucumis melo L.) were encapsulated in whey protein isolate (EPWI), whey protein concentrate (EPWC), and soy protein isolate (EPSP) by nanoprecipitation to evaluate the effect on the antioxidant potential in vitro. The crude extract was evaluated for the content and profile of PC, presenting 750 ± 60.73 mg EAG/100 g and ten different types with emphasis on procyanidin B1 (213.9 ± 33.23 mg/kg) and fumaric acid (181.6 ± 30.55 mg/kg). The characterization indicated the incorporation efficiency of PC in the range of 74.10 ± 0.28-90.60 ± 6.52 %, formation of spherical particles with smooth surfaces, average diameters between 74.90 ± 10.78-96.57 ± 10.17 nm, amorphous structure, and chemical interactions between the materials, justifying the potentiation of the antioxidant activity of the crude extract by up to six times (p < 0.05). Therefore, nanoencapsulation using protein materials and the nanoprecipitation technique is a promising strategy to promote the encapsulation of PC from Cantaloupe melon., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Whey protein isolate (WPI) was reacted with 20, 120, and 240 μmol/g gallic acid (GA) or epigallocatechin gallate (EGCG) at 21 °C. Equilibrium dialysis testing indicated a stronger binding capacity of whey proteins with EGCG compared to GA. Both phenolics, especially EGCG, tended to reduce the adsorption of WPI at the oil-water interface and decreased the elasticity modulus (E d ) of the interfacial film. Yet, binding with 20 μmol/g of EGCG and GA (less so) resulted in significantly improved emulsifying activity of WPI, but the emulsion stability was decreased at all phenolic concentrations (except at 240 μmol/g). There was an overall improvement of pepsinolysis of both α-lactalbumin and β-lactoglobulin. In comparison with GA, EGCG yielded more pronounced effects on WPI interfacial adsorption, dilatational rheology, and peptic digestion., Competing Interests: Declaration of competing interest There are no conflicts to declare., (Copyright © 2024. Published by Elsevier Ltd.)

Physicochemical, structural properties and application in lycopene-loaded emulsions of blends of whey protein isolate (WPI) and pea protein isolate (PPI) at varying mass ratios (100/0, 75/25, 50/50, 25/75, 0/100) were investigated. Data indicated that the mass ratios affected the physical, chemical and storage stability of the emulsion by influencing the particle size, zeta-potential, surface hydrophobicity, free sulfhydryl content, and secondary structure of the blends. Particularly, emulsion with a mixing ratio of 75/25 exhibited superior physical stability against salt concentrations (200 and 500 mM), better chemical stability against UV light and heat, and maintained stability over a 30-day storage period. Emulsions stabilized by blends of different ratios exhibited similar digestion behavior, with no significant differences observed in lycopene's transformation stability and bio-accessibility. Data indicated that substitution of whey protein by pea protein is effective in term of emulsifier application and replacement ratio is an important factor need to be considered., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Protein-polysaccharide interactions are crucial for food system structure and stability. This study investigates the interaction of Lycium barbarum polysaccharide (LBP) at 0-2.00 % concentrations with whey protein isolate (WPI), focusing on functionality and structural changes. LBP covalently grafted onto WPI, as confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), forming WPI-LBP complexes with a maximum degree of grafting (DG) of 44.58 % at 2.00 % LBP. This grafting reduced WPI's surface hydrophobicity (H 0 ) and improved solubility, emulsifying properties, and digestibility under certain conditions, with optimal antioxidant activity at 1.00 % LBP. Multispectral analysis and microscopy showed LBP grafting alters WPI's secondary, tertiary, crystalline, and micro/nanostructures. The comprehensive analysis indicates that the interaction between LBP and WPI involves covalent bonding, hydrogen bonding, hydrophobic interactions, and electrostatic forces, as supported by zeta potential and chemical forces results. These findings suggest LBP-protein complexes as promising food materials for enhancing functionality and stability in the food industry., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

To improve the stability and bioavailabilityhe of polyphenolics in Lycium barbarum leaf, this study encapsulated L. barbarum leaf extracts (LLE) within whey protein isolate (WPI) and bovine serum albumin (BSA) nanoparticles (NPs) via self-assembly to enhance polyphenol distribution. The physicochemical properties of nanoparticles were characterized using transmission electron microscopy (TEM), Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), differential scanning calorimetry (DSC) and thermogravimetric (TG), respectively. The nanoparticles also showed good physical stability at various temperatures, different pH and NaCl concentrations. Compared with BSA-LLE NPs, WPI-LLE NPs exhibited strong physical stability with encapsulation efficiency of 70.6 %. The polyphenol nanoparticles demonstrated enhanced stability in the presence of stomach acid during in vitro simulated digestion. Additionally, the nanoparticles enhanced polyphenol stability during simulated gastrointestinal digestion. Following intestinal digestion, compared with LLE, the bioaccessibility of total phenolic increased by 53.67 % (WPI-LLE NPs), with specific enhancement in compounds like kaempferol, rutin, and chlorogenic acid., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

This work aims to verify the feasibility of improving protein function by regulating its hydrophobicity and reveal the relationship between structure and function. Whey protein (WP) and zein were the source of hydrophilic and hydrophobic polypeptide chains to prepare complex proteins (CPs) with much different structure and function. The results showed that the water- and oil-holding capacities, emulsifying properties and gel properties of CPs can be significantly improved via changing WP-zein ratio. All these can be attributed to the changes in protein hydrophobicity, which not only regulated the binding strength of protein to water and oil, but also modified their molecular structure (surface characteristics, availability of free thiols, α-helix, β-sheet, random coil and the formation of disulfide bonds). Notably, optimal protein hydrophobicity varies greatly among different functional properties. Overall, the techno-functional properties of protein can be improved via tuning its hydrophobicity, which may provide novel sights in protein modification., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The rising demand for sustainable proteins leads to increased interest in plant proteins like hemp protein (HP). However, commercial HP's poor functionality, including heat aggregation, limit its use. This study explored the heat-induced interactions of hemp protein particles (HPPs) with milk proteins, specifically whey proteins and caseins. Using various analysis techniques-static light scattering, TEM, SDS electrophoresis, surface hydrophobicity, and free sulfhydryl content-results showed that co-heating HPPs with whey protein isolate (WPI) or sodium caseinate (NaCN) at 95 °C for 20 min reduced HPPs aggregation. HPPs/WPI particles had a d 4,3 of ∼3.8 μm, while HPPs/NaCN were ∼1.9 μm, compared to ∼27.5 μm for HPPs alone. SDS-PAGE indicated that whey proteins irreversibly bound to HPPs, through disulfide bonds, whereas casein bound reversibly, possibly involving the chaperone-like property of casein. This study proposes possible mechanisms by which HPPs interact with milk proteins and impact protein aggregation. This may provide opportunities for developing hybrid protein microparticles., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

A pH-sensitive film was prepared from pectin (P) and whey protein (W), incorporating anthocyanin-rich purple sweet potato extract (PPE) as the pH indicator. The effect of PPE content on the structure and properties of the films and the pH indicating function were determined and evaluated for shrimp freshness and grape preservation. The solubility (60.23 ± 7.36 %) and water vapor permeability (0.15 ± 0.04 × 10 -11  g·cm/(cm 2 ·s·Pa)) of the pectin/whey protein/PPE (PW-PPE) film with 500 mg/100 mL PPE were the lowest of the films tested and much lower than PW films without PPE. PW-PPE films were non-cytotoxic and had excellent biodegradability in soil. Grapes coated with PW-PPE film had reduced weight loss from water evaporation, and decay during storage was inhibited. The total color change (ΔE) of the PW-PPE films had a strong linear correlation with the pH of shrimps during storage. PW-PPE films have application potential to monitor the real-time freshness of meat and extend the shelf life of fruit., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Fortification of human milk (HM) is often necessary to meet the nutritional requirements of preterm infants. The present experiment aimed to establish whether the supplementation of HM with either an experimental donkey milk-derived fortifier containing whole donkey milk proteins, or with a commercial bovine milk-derived fortifier containing hydrolyzed bovine whey proteins, affects peptide release differently during digestion. The experiment was conducted using an in vitro dynamic system designed to simulate the preterm infant's digestion followed by digesta analysis by means of LC-MS-MS. The different fortifiers did not appear to influence the cumulative intensity of HM peptides. Fortification had a differential impact on the release of either donkey or bovine bioactive peptides. Donkey milk peptides showed antioxidant/ACE inhibitory activities, while bovine peptides showed opioid, dipeptil- and propyl endo- peptidase inhibitory and antimicrobial activity. A slight delay in peptide release from human lactoferrin and α-lactalbumin was observed when HM was supplemented with donkey milk-derived fortifier., Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Laura Cavallarin has patent #Food Composition - EP 3057450 B1 issued to n.a. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Protein-polyphenol and polysaccharide complexes have gained ample research interest as natural emulsifiers. Covalent camel whey protein-quercetin (WQ) conjugates and their non-covalent complexes (WQS) with starch would enhance the stabilization of micron (ME) and nano-size emulsions (NE). Fabrication of WQ conjugates and WQS complexes was followed by their characterization using spectroscopic and electrophoretic techniques. Emulsions stabilized by these compounds were evaluated through microscopy, droplet size analysis, rheology, and oxidative stability assays. Production method and WQS incorporation were considered as variables in the experimental design. Results showed that WQ-conjugate-stabilized emulsions exhibited superior stability compared to control, regardless of the production method. WQS incorporation improved stability, especially in nano emulsions. Covalent-WQ-conjugates outperformed WQS in stabilizing micron emulsions. Starch concentration influenced oxidative stability, with higher concentrations in ternary complexes correlating with decreased stability. These findings underscore the potential of WQ covalent conjugates and WQS ternary complexes to enhance camel whey proteins' emulsifying properties for functional foods., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2025 The Author(s). Published by Elsevier Ltd.. All rights reserved.)

Protein fibrillation complex mechanisms led to an emerging trend in research for years. The mechanisms behind whey protein isolate (WPI) fibrillation driven by divalent cations remained still a matter of speculation. All cations (Ca 2+ , Fe 2+ , Mg 2+ , and Zn 2+ ) enhanced the microenvironment polarity through π-π stacking, and the amide I and II shifts confirmed the fibrillation. The Fe 2+ followed the nucleation-growth mechanism attested by spider-like microstructure, maximum fibril length (654.96 nm) and β-sheets. The hydrophobic forces were mainly involved while disulfide bonds had no key role. The Ca 2+ and Mg 2+ followed the nucleated conformational conversion and electrostatic shielding which induced mature multilayer fibrils. The Zn 2+ induced worm-like fibrils probably showing the low conversion rate regarding the high binding affinity toward WPI which stabilized the structure, so simple nucleated polymerization conducted the fibrillation. More ionic strength improved the exposure of hydrophobic amino acids in the surface, accelerating the growth phase by increased number of nuclei., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Baked milk is subjected to prolonged high-temperature processing, which often undermines its dispersion stability. While carrageenan is known to inhibit milk demixing, its role in stabilizing heat-induced protein aggregates remains inadequately understood. In this study, we isolated casein micelles (CM), whey protein-casein aggregates (WPCA), and whey protein aggregates (WPA) from baked milk through centrifugation. LC-MS/MS analysis revealed that the addition of 0.02% carrageenan prior to baking significantly reduced whey protein aggregation, markedly reducing WPA and WPCA. We quantitatively assessed the adsorption patterns of carrageenans of varying molecular weights and types. Results suggested that λC were predominantly nonadsorbing, enhancing system stability through thickening. Conversely, ιC demonstrated non-selective adsorption onto both CM and WPCA, while κC primarily targeted WPCA. Furthermore, longer chains of carrageenan might inhibit the formation of insoluble complexes with WPCA. This research provides valuable insights for understanding the stabilization mechanisms of carrageenans in real processing within milk systems., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2025 Elsevier Ltd. All rights reserved.)

This study aimed to develop a quercetin-loaded whey protein complex using pH-induced co-assembly for the intestinal-targeted delivery of quercetin. The investigation focused on quercetin loading capacity, formation mechanism, stability, antioxidant activity, and in vitro digestive properties of the complex. The results indicated that the stable complex was obtained at a quercetin-to-protein mass ratio of 1:20, exhibiting a high encapsulation efficiency (96.4 %) and loading capacity (4.6 %). Interaction studies revealed that quercetin binds to whey protein via hydrophobic interactions and hydrogen bonding, forming an irregular layered structure. Stability analysis demonstrated that the complex possesses high ionic and thermal stability. The antioxidant capacity of quercetin was significantly enhanced by complex encapsulation. In vitro digestion studies showed that the complex could pass through the gastrointestinal tract smoothly and effectively improve the bio-accessibility of quercetin. These findings provide a theoretical basis for the application of whey protein-based quercetin delivery systems in the functional food field., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2025 Elsevier Ltd. All rights reserved.)

Synergistic influence of extrusion conditions and whey protein isolate (WPI) incorporation on glycemic response and physicochemical characteristics of rice starch was studied. Box-Behnken Design was used to evaluate effect of process variables (rice starch:WPI ratio; feed moisture and barrel temperature) on quality characteristics of resistant starch-rich, low GI extruded snacks (RSLG-E). Optimum conditions for development of RSLG-E were WPI:18.30 %, feed moisture:20 % and barrel temperature:120 °C. FTIR spectroscopy showed maximum peaks at 1615 cm -1 and 1540 cm -1 corresponding to presence of amide group; however, such band was absent in control. Thermal analysis indicated significantly higher transition temperatures in RSLG-E than control. Expansion ratio (3.79 ± 0.17) and overall acceptability (4.48 ± 0.05) were found to be significantly lower in RSLG-E. In vitro digestibility indicated significantly lower very rapidly digestible starch (2.08 ± 0.03 %) and rapidly digestible starch (68.49 ± 1.07 %) in RSLG-E than control. Digestible starch (86.85 ± 0.97 %), starch hydrolysis rate (58.72 ± 0.97 %) and slowly digestible starch (72.61 ± 0.82 %) were lower in control., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

This work elucidated the digestion behavior of low-oil phase Pickering emulsion gel (LOPPEG) stabilized by whey protein isolate (WPI) -γ-Oryzanol (γO) aggregated particles and interfacial adsorption properties of its simulated digestion products. Initially, following simulated digestion, WPI-γO LOPPEG exhibited lower free fatty acid release and protein digestibility compared to WPI LOPPEG. WPI-γO LOPPEG maintained lower interfacial tension and higher interfacial thickness than WPI LOPPEG. The quartz crystal microbalance results further demonstrated that the viscoelasticity and oil-water interfacial adsorption quality of WPI-γO LOPPEG were higher than those of WPI LOPPEG. Ultimately, WPI-γO/pH 7.5 LOPPEG showed the best interfacial adsorption characteristics and anti-digestive properties. This work could provide the theoretical guidance for the development of the slow-digestive foods., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

This study investigated the oleogelation of cellulose bead dispersions in a sunflower oil oleogel made with solvent-transferred whey protein isolate. The microstructure and rheology of the mixed gels depended on the ratio of hydrated cellulose beads to proteins (9:1, 8:2, 7:3, and 1:1). Two gel stabilization mechanisms were identified. In gels dominated by cellulose beads, capillary bridging and the avoidance of the continuous oil phase dominated network formation. With increasing protein content, the cellulose beads became covered by a layer of aggregated protein, leading to a protein-dominated network. All mixed gels displayed similar elastic behaviour. Oil release was greater in the gels at the highest cellulose bead to protein ratio, which aligned with the presence of void spaces in the network visible under the microscope. These findings serve as the foundation to explore other particle-filled oleogels for use in food-related applications., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Authors. Published by Elsevier Ltd.. All rights reserved.)

The aim of this study was to fabricate novel transglutaminase (TGase)-mediated glycosylated whey protein isolate (WPI) nanoparticles for the encapsulation and delivery of curcumin. The influences of glycosylation on the physiochemical properties, stability, bioavailability, and antioxidant properties of WPI nanoparticles loaded with curcumin were investigated. Composite nanoparticles exhibited uniform distribution and small particle sizes. The main driving forces for the formation of curcumin nanoparticles were electrostatic interactions, hydrogen bonding, and hydrophobic interactions. The encapsulation and loading efficiency of curcumin after TGase-type glycosylation were significantly increased in comparison to WPI-curcumin nanoparticles. Glycosylated WPI-curcumin nanoparticles had stronger antioxidant properties and stability to resist external environmental changes than WPI-curcumin nanoparticles. In addition, glycosylated WPI-curcumin nanoparticles showed a controlled release and enhanced curcumin bioavailability in vitro gastrointestinal digestion. This study provides novel insights for self-assembled glycosylated protein nanoparticles as delivery systems for protecting hydrophobic nutrients., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

This study aimed to reveal the change patterns of the phosphorylation modification status of yak whey phosphoproteins during lactation and their physiological effects. Herein, we comprehensively characterized whey phosphoproteome in yak colostrum and mature milk using an ultra-high throughput phosphoproteomics approach incorporating trapped ion mobility technology. A total of 344 phosphorylation sites from 206 phosphoproteins were identified, with individual site modification predominating. Notably, 117 significantly different phosphorylation sites were distributed on 89 whey phosphoproteins. Gene ontology analysis indicated that these significantly different whey phosphoproteins (SDWPPs) were mainly annotated to carbohydrate metabolic process, membrane, extracellular region and calcium ion binding. Metabolic pathway enrichment analysis demonstrated that SDWPPs were critically involved in protein processing in endoplasmic reticulum, NOD-like receptor signaling pathway and N-glycan biosynthesis. Our results elucidate the phosphorylation profiles of yak whey phosphoproteins at different lactations and their adaptive regulatory role in meeting the nutritional requirements of yak calves during development., Competing Interests: Declaration of competing interest All authors ensure the absence of known conflicts of interest or personal relationships that could bias the research work presented in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The quality of surimi, widely used in processed seafood, is compromised by freeze-thaw cycles, leading to protein denaturation and oxidative degradation. The objective of this study is to explore the effects of adding natural whey peptide hydrolysate (WPH) on the myofibrillar proteins of repeatedly freeze-thawed surimi. Results indicated surimi treated with 15% WPH exhibited only a 128% increase in surface hydrophobicity and a maximum peroxide value of 7.84 μg/kg, significantly lower than the control group. Additionally, salt-soluble protein content, emulsification activity, and stability decreased with the increase in freeze-thaw cycles. With a 15% WPH offering the most significant protective effect, evidenced by reductions of only 25.02%, 42.52% and 37.02% in salt-soluble protein content, emulsification activity, and stability, respectively. These outcomes demonstrate that WPH effectively reduces protein denaturation during repeated freeze-thaw processes. Future research should explore the molecular mechanisms underlying WPH's protective effects and evaluate their applicability in other food systems., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Whey protein (WP) is often used as a delivery carrier due to its superior biological activity and nutritional value. Covalent binding of WP to epigallocatechin gallate (EGCG) can significantly improve the performance of WP in encapsulated materials. Nevertheless, the preparation of WP-EGCG covalent complexes still suffers from low grafting rates. Studies have shown that calcium ions (Ca 2+ ) can modify the structure of proteins. We therefore explored the effect of calcium chloride (CaCl 2 ) on the free radical grafting of EGCG and WP. The experimental results showed that the grafting rate of free radicals increased by 17.89% after adding Ca 2+ . Furthermore, the impact of WP-EGCG-Ca 2+ covalent complex on the entrapment efficiency of apigenin (AP) was further examined, and the results revealed that the entrapment rate could reach 93.66% at an apigenin concentration of 0.2 mg/mL. Simulated gastrointestinal digestion showed that WP-EGCG-Ca 2+ covalent complex could significantly improve the bioavailability of AP. The study provides new ideas to broaden the application of WP as a carrier for delivering bioactive substances., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Microorganisms, proteins, and lipids play crucial and intricate roles in the aroma generation of aquatic products. To explore the impact of the interaction between microorganisms and proteins on the volatile compounds (VOCs) in grouper, this study employed whey protein isolate (WPI) to inhibit lipid oxidation and reduce mutual interference. Changes in bacterial profiles, metabolites, and VOCs were detected. Eighteen key VOCs associated with the overall flavor of grouper were identified, and the potential relationships among microorganisms, proteins, and VOCs were explored using a correlation network. Five microorganisms (Vibrio, Vagococcus, Pseudomonas, Psychrobacter, and Shewanella) closely related to characteristic flavor compounds were identified. Additionally, 30 differential metabolites related to proteins and six metabolic pathways were screened. Therefore, this study unveils the potential interaction between microorganisms and proteins in flavor formation and provides new insights into the relationships among microorganisms, proteins, and VOCs., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Personalized three-dimensional (3D) printed foods rich in probiotics were investigated. Lactiplantibacillus plantarum (Lp), as a representative of probiotics, was used to investigate the 3D printing of probiotic-rich dysphagia foods. Here, whey protein isolate nanofibrils (WPNFs) were coated and anchored on bacterial surfaces via biointerfacial supramolecular self-assembly, providing protection against environmental stress and the 3D printing process. The optimized composite gels consisting of High acyl gellan gum (0.25 g), whey protein isolate (1.25 g), fructooligosaccharides (0.75 g), Lp-WPNFs-Glyceryl tributyrate emulsion (Φ = 40%, 3.75 mL) can realize 3D printing, and exhibit high resolution, and stable shape. The viable cell count is higher than 8.0 log CFU/g. They are particularly suitable for people with dysphagia and are classified as level 5-minced & moist in the international dysphagia diet standardization initiative framework. The results provide new insights into the development of WPNFs-coating on bacterial surfaces to deliver probiotics and 3D printed food rich in probiotics., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Vitamin B is easily degraded by light and heat during storage, which results in nutritional loss of food. Whey protein is expected to protect vitamin B by forming complexes through secondary bonds. The properties of the complexes and protective effects of whey protein on vitamins B 1 , B 2 , B 3 and B 6 were characterized. The percentage losses of vitamin B were decreased by more than 60% with the protection of whey protein. FTIR, fluorescence spectroscopy, thermodynamic analysis and molecular docking were used to investigate the binding interaction between vitamin B and whey protein. Vitamin B quenched the intrinsic fluorescence of whey protein, mainly with a static nature (Kq > 2.0 × 10 10  L/(mol·s)). The interactions between whey protein and vitamin B were mostly mediated by hydrogen bonds and van der Waals forces, as demonstrated by the thermodynamic parameters and molecular docking., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Texture-modified, multi-nutrient composite foods are essential in clinical treatment for dysphagia individuals. Herein, fibrous whey protein-stabilized emulsion and different crystalline starches (wheat, corn, rice, potato, sweet potato, cassava, mung bean and pea) were used to structure composite emulsion gels (CEGs). These CEGs then underwent 3D printing to explore the feasibility of developing a dysphagia diet. The network of molded CEGs was mainly maintained by hydrophobic interactions and hydrogen bonds. Rice and cassava starches were better suited for structuring soft-textured CEGs. Compared with molded CEGs, 3D printing decreased hydrogen bonds and the compactness of the nano-aggregate structure within the gel system, forming a looser gel network and softening the CEGs. Interestingly, these effects were more pronounced for the CEGs with high initial hardness. This study provided new strategy to fabricate CEGs as dysphagia diet using fibrous whey protein and starch, and to design texture-modified foods for patients using 3D printing., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

In the present study, we investigated the mechanisms associated with the stabilizing effects of whey protein concentrate-80 (WPC80) and L-ascorbyl 6-palmitate (LAP) on folic acid (FA). Multispectral techniques show that WPC80 binds to FA and LAP mainly through hydrophobic interactions, and that energy is transferred from WPC80 to FA and LAP in a nonradiative form (FA/LAP); The combination of FA/LAP resulted in a change in the conformation and secondary structure content of WPC80, an increase in the absolute zeta potential of the system, and a shift in the particle size distribution towards smaller sizes. The compound system exhibits strengthened antioxidant properties and favorable binding properties. Besides, WPC80 improves the storage stability of FA under different conditions. These results demonstrated that the ternary complex formed by FA co-binding with WPC80 and LAP is an effective way to improve the stability against of FA., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Gelatin (GEL), pectin (PEC), carboxymethyl cellulose (CMC), and whey protein isolate (WPI) were employed to formulate hydrogels for stabilizing N-Acetylneuraminic Acid (NeuAc). GEL/WPI-NeuAc hydrogels, irrespective of the ratio, exhibited a flexible and smooth surface with a continuous three-dimensional network structure internally. Porosity of the three types of hydrogels increased from 3.69% to 86.92% (GEL/WPI), 41.67% (PEC/WPI), and 87.62% (CMC/WPI), rendering them suitable as carriers for NeuAc encapsulation. The dynamic swelling behavior of all hydrogels followed Schott's second-order kinetics model. The degradation performance of GEL, PEC, and CMC/WPI-NeuAc hydrogels was optimal at a 5: 5 ratio, with degradation rates of 80.39 ± 1.26%, 82.38 ± 1.96%, and 81.39 ± 1.57%, respectively. GEL, PEC, CMC/WPI-NeuAc hydrogels demonstrated decreased release rates of 44.56%, 31.04%, and 41.26%, respectively, compared to free NeuAc, post gastric digestion. The present investigation suggests the potential of GEL/WPI hydrogels as effective carriers for delivering NeuAc encapsulation., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

A novel curcumin (CUR) delivery system was developed using soybean whey protein (SWP)-based emulsions, enhanced by pH-adjustment and gum arabic (GA) modification. Modulating electrostatic interactions between SWP and GA at oil/water interface, pH provides favorable charging conditions for stable distribution between droplets. GA facilitated the SWP form a stable interfacial layer that significantly enhanced the emulsifying properties and CUR encapsulation efficiency of the system at pH 6.0, which were 90.15 ± 0.67%, 870.53 ± 3.22 m 2 /g and 2157.62 ± 115.31%, respectively. Duncan's test revealed significant improvements in thermal, UV, oxidative, and storage stabilities of CUR (P < 0.05). At pH 6.0, GA effectively protected CUR by inhibiting SWP degradation during gastric digestion and promoting the release of CUR by decreasing steric hindrance with oil droplets during intestinal digestion, achieving the highest CUR bioaccessibility (69.12% ± 0.28%) based on Duncan's test. The SWP-GA-CUR emulsion delivery system would be a novel carrier for nutrients., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Malondialdehyde (MDA) can induce lipoxidation in whey protein isolate (WPI). The physicochemical changes in this reaction with or without the presence of a phenolic compound epicatechin (EC) were characterized in this study. Results suggested the content of MDA was significantly reduced during co-incubation of MDA and EC. The addition of EC dose-dependently alleviated MDA-induced protein carbonylation, Schiff base formation and loss of tryptophan fluorescence. The interruption of MDA-binding to WPI was directly visualized by immunoblotting analysis. Observation of the surface microstructure of WPI showed that MDA-induced protein aggregation was partially restored by EC. Meanwhile, EC was found to promote loss of both protein sulfhydryls and surface hydrophobicity due to possible phenol-protein interactions. These observations suggested the potential of EC in the relief of MDA-mediated protein lipoxidation., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The Glycerol monolaurate (GML) oleogel was induced using Camellia oil by slowly raising the temp to the melting point (MP) of GML. Whey protein isolate (WPI) solution with different ratios was composited with GML oleogel by emulsion template methods, forming dense spines and honeycomb-like networks and impressed with an adjustable composite structure. Textural results showed that compared with single GML-based oleogels, the GML/WPI composite oleogels had the advantages of high hardness and molding, and structural stability. The composite oleogels had moderate thermal stability and maximal oil binding (96.36%). In particular, as up to 6 wt% GML/WPI, its modulus apparent viscosity was significantly increased in rheology and similar to commercial fats. Moreover, it achieved the highest release of FFA (64.07%) and the synergy provided a lipase substrate and reduced the body's burden. The resulting composite oleogel also showed intermolecular hydrogen bonding and van der Waals force interactions. These findings further enlarge the application in the plant and animal-based combined of fat substitutes, delivery of bioactive molecules, etc., with the desired physical and functional properties according to different proportions., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The purpose of this study was to prepare Pickering emulsion with synergistic antibacterial effect using whey protein isolated-citral (WPI-Cit) nanoparticles with eugenol for grape preservation. In this emulsion, eugenol was encapsulated in oil phase. The particle size, ζ-potential, and antibacterial mechanism of the nanoparticles were characterized. The rheological properties, antibacterial effects and preservation effects of WPI-Cit Pickering emulsion were measured. The results showed that the optimal preparation condition was performed at WPI/Cit mass ratio of 1:1, WPI-Cit nanoparticles were found to damage the cell wall and membrane of bacteria and showed more effective inhibition against S. aureus. Pickering emulsion prepared with WPI-Cit nanoparticles exhibited a better antibacterial effect after eugenol was encapsulated in it, which extended the shelf life of grapes when the Pickering emulsion was applied as a coating. It demonstrated that the Pickering emulsion prepared in this study provides a new way to extend the shelf life., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Wall material types influence the efficacy of nanocarriers in oral delivery systems. We utilized three food biomacromolecules (whey protein isolate, oxidized starch, lipids) to prepare three types of nanocarriers. Our aim was to investigate their performance in digestion, cellular absorption, mucus penetration, intestinal retention, and bioavailability of the encapsulated anthocyanins (Ant). The release rate of protein nanocarriers (Pro-NCs) was twice that of starch nanocarriers (Sta-NCs) and four times that of lipid nanocarriers (Lip-NCs) in simulated gastrointestinal fluid. Additionally, Pro-NCs demonstrated superior transmembrane transport capacity and over three times cellular internalization efficiency than Sta-NCs and Lip-NCs. Sta-NCs exhibited the highest mucus-penetrating capacity, while Pro-NCs displayed the strongest mucoadhesion, resulting in extended gastrointestinal retention time for Pro-NCs. Sta-NCs significantly enhanced the in vivo bioavailability of Ant, nearly twice that of free Ant. Our results demonstrate the critical role of wall material types in optimizing nanocarriers for the specific delivery of bioactive compounds., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper Declaration of interests The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The poor thermal stability and ion tolerance of whey protein hydrolysates (WPH) restrict its application in emulsions, while glycosylation shows potential benefits in improving WPH stability. However, the relationship between saccharides with different Mw and the glycosylation behavior of WPH rich in short peptides is unclear. In response, the effect of different saccharides on glycosylated WPH rich in short peptides and its emulsion stability were investigated. Grafted small Mw saccharides were more beneficial to the emulsion stability of WPH. Specifically, grafting xylose effectively inhibited 121 °C sterilization and 5 mM CaCl 2 -induced coalescence of WPH emulsion (687.50 nm) by comprehensively enhancing steric hindrance, conformational flexibility and electrostatic repulsion, and dissociating large aggregates into small aggregates. Conversely, grafting maltodextrin (30,590 Da) reduced thermal stability of WPH emulsion (4791.80 nm) by steric shielding and bridging flocculation. These findings provide new sights into glycosylation mechanism for WPH and achieving its application in nutritional emulsions., Competing Interests: Declaration of competing interest We declare that no support, financial or otherwise, has been received from any organization that may have an interest in the submitted work, and there is no any other conflict of interest for this manuscript entitled “Investigating the Thermal Stability and Calcium Resistance of O/W Emulsions Prepared with Glycosylated Whey Protein Hydrolysates Modified by Different Saccharides”. The authors have declared no conflicts of interest., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

High internal phase Pickering emulsions (HIPPEs) prepared from natural polymers have attracted much attention in the food manufactures. However, single zein-stabilized HIPPEs are poorly stable and prone to flocculation near the isoelectric point. To address this issue, in this study, zein and whey protein nanofibrils (WPN) complex nanoparticles (ZWNPs) were successfully prepared using a pH-driven method, and ZWNPs were further used as HIPPEs stabilizers. The results showed that zein and WPN were combined together through hydrogen bonding and hydrophobic interaction to form ZWNPs, and the HIPPEs stabilized by ZWNPs had excellent stability, which could effectively protect the internally encapsulated lycopene and improve the bioaccessibility of lycopene. In conclusion, this study provides a new strategy for the preparation of stable hydrophobic protein-based HIPPEs, represented by zein., Competing Interests: Declaration of competing interest The authors declared that they have no conflicts of interest to this work., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Iron is an important micronutrient that cannot be added directly into food products due to potential reactions with the food matrix, impact on color, and taste. Complexed biopolymeric nanocarriers can overcome these challenges particularly for oral delivery of iron, but selecting appropriate biopolymers, their ratio and pH of complexation is very important. In this study, whey protein concentrate (WPC)-pectin nanocomplexes were prepared at different concentrations (WPC 4, 6 and 8%; pectin 0.5, 0.75 and 1%), and pH (3, 6 and 9) to encapsulate iron. The smallest carriers were observed at pH 3; higher pH led to higher zeta potential (zero to -32.5 mV). Encapsulation efficiency of iron in nanocarriers formulated at pH = 3, 6 and 9 were 87.83, 75.92 and 20%, respectively. Scanning electron microscopy revealed the spherical particles at pH 3. To conclude, a WPC to pectin ratio of 4: 1 at pH 3 was the best conditions for loading iron., Competing Interests: Declaration of competing interest All authors declare that there is no conflict of interest., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

In this study, a combination of whey protein (hydrophilic coating) and polydopamine (crosslinking agent) was used to improve the stability and functionality of quercetin-loaded zein nanoparticles. There are two key benefits of the core-shell nanoparticles formed. First, the ability of the polydopamine to bind to both zein and whey protein facilitates the formation of a stable core-shell structure, thereby protecting quercetin from any pro-oxidants in the aqueous surroundings. Second, neutral and hydrophilic whey proteins were used for the surface coating of the nanoparticles to further enhance the sustained and slow release of quercetin, facilitating its sustained release into the body at a slow and steady rate. The results of this study will promote the innovative development of precise nutritional delivery systems for zein and provide a theoretical basis for the design and development of dietary supplements based on hydrophobic food nutrient molecules., Competing Interests: Declaration of competing interest No conflicts of interest are declared for any of the authors., (Copyright © 2023. Published by Elsevier Ltd.)

The instability and discoloration of (-)-epigallocatechin-3-gallate (EGCG) constrain its application in functional dairy products. Concurrently, challenges persist in the separation and utilization of whey in the dairy industry. By harnessing the interactions between polyphenols and whey proteins or their hydrolysates, this study proposed a method that involved limited enzymatic hydrolysis followed by the addition of EGCG and pH adjustment around the isoelectric point to obtain whey protein hydrolysates (WPH)-EGCG. Over 92 % of protein-EGCG complexes recovered from whey while ensuring the preservation of α-lactalbumin. The combination between EGCG and WPH depended on hydrogen bonding and hydrophobic interactions, significantly enhanced the thermal stability and storage stability of EGCG. Besides, the intestinal phase retention rate of EGCG in WPH-EGCG complex was significantly increased by 23.67 % compared to free EGCG. This work represents an exploratory endeavor in the improvement of EGCG stability and expanding the utilization approaches of whey., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

This research compared the effects of dry heating on the digestion of goat milk proteins with different casein-to-whey ratios (40% casein, C40 and 80% casein, C80). The glycation markers of heated samples were determined by LC-MS. Heating at 60 °C for 8 h induced early glycation while heating at 60 °C for 72 h induced advanced glycation. Unheated C80 samples showed a higher digestibility than unheated C40 samples, which may be due to their higher protein solubility. After dry heating for 72 h, no significant difference in digestibility was observed between C80 and C40 samples. Heating for 72 h decreased the digestibility of C40 samples compared to unheated samples, probably due to glycation, while protein aggregation was the main reason for the reduced digestibility of heated C80 samples. Overall, this study showed that dry heating for 72 h induced a lower digestibility of C80 and C40 samples, although with different underlying mechanisms., Competing Interests: Declaration of competing interest The authors state that they do not possess any known conflicting financial interests or personal associations that might have influenced the findings reported in this paper., (Copyright © 2023. Published by Elsevier Ltd.)

Casein microparticles from milk are important carrier materials for bioactive substances with stability and swelling properties that can be influenced by heat treatment. Microparticles produced by depletion flocculation and film drying remain stable in acidic media but swell and disintegrate under slightly alkaline conditions. Heat treatment after formation can stabilize the microparticles via a disulfide bridge network and newly formed hydrophobic contacts. Temperatures >60 °C are required so that denatured whey protein initiate formation of disulfide bridges via thiol exchange reactions. The particles then swell in a two-step process and exhibit an overshooting effect. If formation of disulphide bridges is prevented during heat treatment by adding N-methylmaleimide, overshooting swelling disappears and microparticles continue to expand instead. The analysis with parallel system dynamics models is based on the swelling of uncross-linked caseins, which is limited by the expansion capacity of cross-linked caseins., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Authors. Published by Elsevier Ltd.. All rights reserved.)

There are numerous studies on the application of soybean whey protein in three-dimensional (3D) printing. In this study, the effects of soybean meal particles (5%, 6%, 7%, 8%, 9%, and 10%) and oil-phase concentrations (70%, 72%, 74%, 76%, and 78%) on the stability and 3D-printing performance of a soybean-meal-based high-internal-phase emulsion were investigated. The results showed that the particle size of the emulsion decreased with increasing soybean meal particle concentration, and that increasing the concentration of the oil phase improved the viscoelasticity of the emulsion. Rheological tests further showed that the higher storage modulus of the emulsion indicated better support and stability. The emulsion with 8% soybean meal-particles and 76% oil-phase concentration exhibited the best printing effect. This study provides an effective solution for the preparation of stabilized high-internal-phase emulsions of soybean meal particles suitable for 3D printing., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)