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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.)

The application of natural biopolymers to develop colloidal carriers for delivering hydrophobic bioactive molecules has become one of the hottest topics in food science. In this study, a simple pH-driven method to prepare whey protein nanofibrils stabilized zein nanoparticles was developed. The formation, structure, intermolecular interactions, rheological properties, in vitro digestion, and antioxidant activity of the nanoparticles were investigated. When the mass ratio of zein and whey protein nanofibrils was 1:0.8, the hydrodynamic diameter and zeta potential of the nanoparticles were 413 nm and - 25 mV, respectively. Transmission electron microscope photographs showed that the nanoparticles were a spherical core-shell structure. Fourier transform infrared spectroscopy and surface hydrophobicity measurements indicated that whey protein nanofibrils adsorbed to the surface of zein aggregates through hydrogen bonding and hydrophobic interactions. Differential scanning calorimetry tests confirmed the formation of nanoparticles improved the thermal stability of zein and whey protein nanofibrils. The nanoparticles exhibited less shear-thinning behavior with low apparent viscosity, and it can't be degraded in simulated gastric fluid but can be in simulated intestinal fluid. The antioxidant activity of the nanoparticles was increased by in vitro antioxidant assay when compared to whey protein nanofibrils. This new technology to develop zein-whey protein nanoparticles may be used for preparing nanoparticles of other similar hydrophobic food ingredients. And the findings of this study may provide a theoretical basis for preparation of nanoparticles as a nutrient delivery system., Competing Interests: Declaration of competing interest The authors confirm that they have no conflict of interest to declare for this publication., (Copyright © 2020. Published by Elsevier B.V.)

Cereal-based fermented products are becoming popular in the world. A millet-based yogurt-like product (MYP) using polymerized whey protein (PWP) and xanthan gum (XG) as thickeners was developed. The present study aimed to investigate the effects of PWP (0.3 to 0.5%, w/v) and XG (0 to 0.2%, w/v) on the gelation properties and microstructure of MYP. All samples were analyzed for rheological properties, textural properties, microstructure, and pH value during fermentation. The MYP Ⅲ (0.4% PWP and 0.1% XG) registered the highest elastic modulus (G') throughout the fermentation and cooling steps (P < 0.05), but MYP Ⅳ (0.35% PWP and 0.15% XG) had the highest apparent viscosity compared with the other samples. No significant differences in the pH values among the samples were observed during the fermentation process (P > 0.05). The hardness value of MYP Ⅳ reached a maximum after 4 hr and then stabilized during fermentation. Scanning electron microscopy showed a compact and uniform network for the MYP with PWP and XG. MYP Ⅳ had the best texture properties (hardness, springiness, and gumminess). Overall, PWP (0.35%, w/v) and XG (0.15%, w/v) were the best combination for MYP as a thickening system. PRACTICAL APPLICATION: Cereal-based fermented products have attracted much attention in the food industry. However, due to absence of a natural protein network, it is hard to produce a set-type millet-based yogurt with a firm texture under the studied conditions without adding any thickening agents. In this study, PWP (0.35%, w/v) and XG (0.15%, w/v) can be used for fermentation of millet-based yogurt-like products. The new cereal-based fermented product would be a promising food in the market., (© 2020 Institute of Food Technologists®.)

Background: Polymerized whey protein-sodium tripolyphosphate can be induced to gel in an acidic environment provided during fermentation. The variety of thickening agent has an influence on texture that is an essential aspect of yogurt quality affecting consumer preference. Similar to polysaccharide stabilizers, the cold gelation properties of whey proteins can improve the body texture of yogurt products. Polymerized whey protein-sodium tripolyphosphate could be a favorable and interesting thickening agent for making set yogurt., Results: The effects of whey protein isolate (WPI), heat-treated whey protein-sodium tripolyphosphate (WPI-STPP), heat-treated WPI and pectin on the storage properties and microstructure of yogurt were investigated. All samples were analyzed for syneresis, pH, titratable acidity, viscosity, texture profile and microstructure during storage. The results showed that incorporating heat-treated WPI-STPP had a significant impact on syneresis (32.22 ± 0.60), viscosity (10 956.67 ± 962.1) and hardness (209.24 ± 12.48) (p < 0.05) with uniform body texture., Conclusion: Yogurt fermented with modified WPI-STPP had higher levels of protein and better hardness compared with yogurt using pectin. The microstructure was observed to be a uniform and denser, complicated network. Heat-treated WPI-STPP may be useful for improving yogurt texture. © 2016 Society of Chemical Industry., (© 2016 Society of Chemical Industry.)

Soy isoflavones (SIF) are bioactive compounds with low bioavailability due to their poor water solubility. In this study, we utilized polymerized goat milk whey protein (PGWP) as a carrier to encapsulate SIF with encapsulation efficiency of 89%, particle size of 135.53 nm, and zeta potential of −35.16 mV. The PGWP-SIF nanoparticles were evaluated for their stability and in vitro digestion properties, and their ability to transport SIF was assessed using a Caco-2 cell monolayer model. The nanoparticles were resistant to aggregation when subjected to pH changes (pH 2.0 to 8.0), sodium chloride addition (0–200 mM), temperature fluctuations (4 °C, 25 °C, and 37 °C), and long-term storage (4 °C, 25 °C, and 37 °C for 30 days), which was mainly attributed to the repulsion generated by steric hindrance effects. During gastric digestion, only 5.93% of encapsulated SIF was released, highlighting the nanoparticles' resistance to enzymatic digestion in the stomach. However, a significant increase in SIF release to 56.61% was observed during intestinal digestion, indicating the efficient transport of SIF into the small intestine for absorption. Cytotoxicity assessments via the MTT assay showed no adverse effects on Caco-2 cell lines after encapsulation. The PGWP-stabilized SIF nanoparticles improved the apparent permeability coefficient (Papp) of Caco-2 cells for SIF by 11.8-fold. The results indicated that using PGWP to encapsulate SIF was an effective approach for delivering SIF, while enhancing its bioavailability and transcellular transport. [ABSTRACT FROM AUTHOR]

Panax notoginseng saponins (PNSs) have been used as a nutritional supplement for many years, but their bitter taste limits their application in food formulations. The effects of PNS (groups B, C, and D contained 0.8, 1.0 and 1.2 mg/mL of free PNS, respectively) or Panax notoginseng saponin-polymerized whey protein (PNS-PWP) nanoparticles (groups E, F, and G contained 26.68, 33.35 and 40.03 mg/mL of PNS-PWP nanoparticles, respectively) on the rheological, textural properties and bitterness of yogurt were investigated. Group G yogurt showed a shorter gelation time (23.53 min), the highest elastic modulus (7135 Pa), higher hardness (506 g), higher apparent viscosity, and the lowest syneresis (6.93%) than other groups, which indicated that the yogurt formed a stronger gel structure. The results of the electronic tongue indicated that the bitterness values of group E (−6.12), F (−6.56), and G (−6.27) yogurts were lower than those of group B (−5.12), C (−4.31), and D (−3.79), respectively, which might be attributed to PNS being encapsulated by PWP. The results indicated that PWP-encapsulated PNS could cover the bitterness of PNS and improve the quality of yogurt containing PNS. [ABSTRACT FROM AUTHOR]

Goat milk whey protein products are a hard-to-source commodity. Whey protein concentrate was directly prepared from fresh goat milk. The effects of the heating temperature (69–78 °C), time (15–30 min), and pH (7.5–7.9) on the physicochemical and functional properties of the goat milk whey protein were investigated. The results showed that the particle size of the samples significantly increased (p < 0.05) after heat treatment. The zeta potential of polymerized goat milk whey protein (PGWP) was lower than that of native goat milk whey protein. The content of the free sulfhydryl groups of PGWP decreased with increasing heating temperature and time, while an increase in surface hydrophobicity and apparent viscosity of PGWP were observed after heat treatment. Fourier Transform Infrared Spectroscopy analysis indicated that heat treatment and pH had considerable impacts on the secondary structure of goat milk whey protein. Transmission electron microscope images revealed that heat induced the formation of a large and uniform protein network. Additionally, the changes in the physicochemical and structural properties contributed to the improvement of the emulsifying and foaming properties of goat milk whey protein after heat treatment. The results may provide a theoretical basis for the applications of polymerized goat milk whey protein in related products. [ABSTRACT FROM AUTHOR]

Goat milk whey protein concentrates were manufactured by microfiltration (MF) and ultrafiltration (UF). When MF retentate blended with cream, which could be used as a starting material in yogurt making. The objective of this study was to prepare goat milk whey protein concentrates by membrane separation technology and to investigate the effects of polymerized goat milk whey protein (PGWP) on the physicochemical properties and microstructure of recombined goat milk yogurt. A 3-stage MF study was conducted to separate whey protein from casein in skim milk with 0.1-µm ceramic membrane. The MF permeate was ultrafiltered using a 10 kDa cut-off membrane to 10-fold, followed by 3 step diafiltration. The ultrafiltration-diafiltration-treated whey was electrodialyzed to remove 85% of salt, and to obtain goat milk whey protein concentrates with 80.99% protein content (wt/wt, dry basis). Recombined goat milk yogurt was prepared by mixing cream and MF retentate, and PGWP was used as main thickening agent. Compared with the recombined goat milk yogurt without PGWP, the yogurt with 0.50% PGWP had desirable viscosity and low level of syneresis. There was no significant difference in chemical composition and pH between the recombined goat milk yogurt with PGWP and control (without PGWP). Viscosity of all the yogurt samples decreased during the study. There was a slight but not significant decrease in pH during storage. Bifidobacterium and Lactobacillus acidophilus in yogurt samples remained above 106 cfu/g during 8-wk storage. Scanning electron microscopy of the recombined goat milk yogurt with PGWP displayed a compact protein network. Results indicated that PGWP prepared directly from raw milk may be a novel protein-based thickening agent for authentic goat milk yogurt making. [ABSTRACT FROM AUTHOR]

Thermal treatment has been utilized to improve the functional properties of proteins for many years. In this study, we aimed to investigate the effect of sodium triphosphate (Na5P3O10) on particle size and size distribution of heat‐induced whey protein concentrate (WPC) aggregates under different processing conditions. The results showed that high Na5P3O10 level (>0.5%, w/w), long heating time (>15 min), and alkaline condition (pH 8–8.5) facilitated formation of large particles (>10 μm). The WPC aggregates with small‐to‐medium particle size (1–3 μm) that are suitable to be applied as a fat replacer were obtained by heating the WPC solution (8%, w/v) containing 0.4% (w/w) Na5P3O10 at 85°C for 5 min. We conclude that thermal treatment of whey protein concentrate added with Na5P3O10 can obtain whey protein products with different particle sizes for certain applications. It is possible to prepare different sizes of WPC aggregates by manipulating the processing conditions such as protein content and Na5P3O10 level, pH, heating temperature, and time. Thermal treatment at controlled conditions can produce the majority of the aggregates as spherical particles of 1–3 μm in diameter that is suitable for use as a fat replacer in non‐ or low‐fat dairy product formulations. [ABSTRACT FROM AUTHOR]

Proteins were removed from soybean whey wastewater using the chitosan flocculation technique, and this method was compared with lime flocculation, and transglutaminase polymerization. Compared with other flocculation methods, chitosan flocculation exhibited higher saccharide levels ( p < 0.05), lower protein movement ( p < 0.05) through the membrane and lower ultrafiltration membrane pollution levels and could be[0] useful for the development of industrial flocculation processes. The chitosan flocculation procedure was optimized by an L18(37) orthogonal array experimental design (OAD) with four factors at three levels. Optimum variables were a chitosan dosage of 0.8 g/L and a standing pH, time and temperature of 5.5, 60 min and 30C, respectively. Under these conditions, the experimental rate of protein removal was 61.21%, which was consistent with the predicted value (58.85%). These results showed that chitosan flocculation alleviated membrane fouling to a large extent. Practical Applications This study demonstrated the differences in the protein removal properties due to the different processes, i.e., lime flocculation, transglutaminase polymerization and chitosan flocculation technique, in the purification soybean whey wastewater. The information on chitosan combined with ultrafiltration would help in understanding their influences on soybean whey wastewater. Chitosan-ultrafiltration process will facilitate the subsequent recovery of soybean polysaccharides and can be used as an environmentally friendly means for soy whey wastewater purification. [ABSTRACT FROM AUTHOR]

Panax Notoginseng Saponins (PNS) may be beneficial to human health due to their bioactive function. The application of PNS in functional foods was limited due to the bitter taste and low oral bioavailability. PNS were encapsulated by polymerized whey protein (PWP) nanoparticles. The physicochemical, digestive, and sensory properties of the nanoparticles were investigated. Results showed that the nanoparticles had a particle size of 55 nm, the zeta potential of −28 mV, and high PNS encapsulation efficiency (92.94%) when the mass ratio of PNS to PWP was 1:30. Differential Scanning Calorimetry (DSC) results revealed that PNS were successfully encapsulated by PWP. The mainly intermolecular forces between PNS and PWP were hydrogen bonding and electrostatic attraction confirmed by Fourier Transform Infrared Spectroscopy (FTIR). Results of simulated gastrointestinal digestion indicated that the PNS-PWP (1:30) nanoparticles had smaller average particle size (36 nm) after treatment with gastric fluids and increased particle size (75 nm) after treatment with intestinal fluids. Transmission Electron Microscopy (TEM) micrographs reflected that the nanoparticles had irregular spherical structures. The encapsulated PNS exhibited significantly (p < 0.05) decreased bitterness compared to the non-encapsulated PNS confirmed by the electronic tongue. The results indicated that encapsulation of PNS with PWP could facilitate their application in functional foods. [ABSTRACT FROM AUTHOR]

Soy isoflavones (SIF) are a group of polyphenolic compounds with health benefits. However, application of SIF in functional foods is limited due to its poor aqueous solubility. SIF nanoparticles with different concentrations were prepared using polymerized goat milk whey protein (PGWP) as wall material. The goat milk whey protein was prepared from raw milk by membrane processing technology. The encapsulation efficiencies of all the nanoparticles were found to be greater than 70%. The nanoparticles showed larger particle size and lower zeta potential compared with the PGWP. Fourier Transform Infrared Spectroscopy indicated that the secondary structure of goat milk whey protein was changed after interacting with SIF, with transformation of α-helix and β-sheet to disordered structures. Fluorescence data indicated that interactions between SIF and PGWP decreased the fluorescence intensity. All nanoparticles had spherical microstructure revealed by Transmission Electron Microscope. Data indicated that PGWP may be a good carrier material for the delivery of SIF to improve its applications in functional foods. [ABSTRACT FROM AUTHOR]

Abstract Whey proteins (WP) have many nutritional and beneficial therapeutic properties. Whey proteins isolate (WPI) and whey protein concentrate (WPC) are the two major forms of WP, which are indispensable for the functional and nutritional properties of foods. The core aim of this research work was to study the effect of heat treatment on physicochemical and emulsifying properties of polymerized whey protein concentrate and polymerized whey protein isolate. Whey protein solutions (8, 10, 12 w/v %) were heated at temperatures (80, 85, 90 °C) for 30 min, and the physicochemical, emulsification and stability indices properties of WPC and WPI thermal polymers were scrutinized. Results revealed that the content of free sulfhydryl groups, zeta potential and the EAI of polymerized whey protein (PWP) were lower than those of native whey protein (WP) under the same conditions. Meanwhile, the viscosity of PWP was increased with increase in temperature and protein concentration. Additionally, both EAI and ESI of polymerized whey protein isolate (PWPI) were higher than those of polymerized whey protein concentrate (PWPC). TEM and SDS-PAGE results clearly demonstrated that heating induced the formation of large protein aggregates. Conclusively, PWPI network was more homogeneous, stable and denser than that of PWPC. Highlights • In this study, whey protein physicochemical and emulsifying properties were investigated. • Physico-chemical characteristics of polymerized WPI and WPC have been compared. • Interestingly, increase of temperature and protein concentration increase PWP viscosity. • In addition, EAI and ESI of PWPI were higher than PWPC. • Taken together, PWPI network was more homogeneous and denser than that of PWPC. [ABSTRACT FROM AUTHOR]

In this study, gum arabic (GA) and pH modulation were used to change the structural and emulsion properties of soy whey protein (SWP). The interaction mode and binding site of SWP and GA were analyzed by structural characterization and molecular modeling techniques. The microscopic morphological, emulsifying, interfacial, and rheological properties of emulsions formed by SWP–GA complexes were characterized. The ζ-potential results showed that pH has a significant effect on the electrostatic interaction between SWP and GA. Fluorescence spectra and surface hydrophobicity (H 0) illustrated that the H 0 of SWP–GA complexes significantly decreased. Fourier transform infrared spectroscopy (FTIR) showed that GA provided the basis for the formation of ordered structures and that the β-sheet content of SWP–GA complexes reached the maximum value (44.68%) at pH 6.0. Molecular docking results further verified that SWP–GA interaction occurred through hydrogen bond and hydrophobic interaction. Compared with SWP emulsions, droplets of SWP–GA emulsions were uniformly distributed and formed a dense network structure. The emulsifying activity index and emulsifying stability index significantly improved, especially at pH 6.0, which were 902.78 ± 4.44 m2/g and 4648.27 ± 203.59%, respectively. SWP–GA complexes facilitated adsorption at the oil–water interface and reduced the interfacial tension. GA significantly improved the rheological properties of SWP–GA emulsion. Furthermore, statistical analysis indicated that the structural properties of SWP–GA complexes were significantly correlated with the emulsifying and interfacial properties of SWP–GA emulsions. This study would provide theoretical guidance for the preparation of the stable emulsion system of protein–polysaccharide complexes. [Display omitted] • Electrostatic, hydrogen bonding, and hydrophobic interactions were the main forces of SWP and GA. • The properties of SWP emulsion were advanced by pH adjustment and GA addition. • SWP-GA complexes enhanced interfacial and rheological properties of emulsions. [ABSTRACT FROM AUTHOR]

Modification of food proteins by interactions with polyphenols has been used to improve the functional properties of proteins. In this study, soy isoflavones-whey protein complexes were prepared via non-covalent complexation. Solubility of soy isoflavones and changes in conformation and functionality of whey proteins were investigated. The results showed that the solubility of soy isoflavones was significantly increased by the complexation with whey proteins (p < 0.05). Soy isoflavones induced decreased α-helix and increased β-sheet of whey protein but increased α-helix and decreased β-sheet of polymerized whey protein. The solubility, foaming properties, and emulsifying activity of whey proteins were enhanced. The thermal stability of whey protein was decreased, but the thermal stability of polymerized whey protein was increased. The thermal gelation behavior of whey protein was enhanced. This study demonstrated that the conformation and functionality of whey proteins could be modified by interaction with soy isoflavones. There were some different changes in the functionalities of whey protein and polymerized whey protein due to the diverse conformation changes. The current study may provide useful information for the modification of whey proteins by polyphenols complexation. [Display omitted] • Interactions between whey proteins and soy isoflavones occurred. • The conformation and functional properties of whey proteins were modified. • Changes in the functional properties of whey proteins can be utilized in food applications. [ABSTRACT FROM AUTHOR]

Whey proteins of Saanen goat milk samples from 3 provinces in China (Guangdong, GD; Inner Mongolia, IM; Shaanxi, SX) were characterized and compared using data-independent acquisition quantitative proteomics technique. A total of 550 proteins were quantified in all 3 samples. There were 44, 44, and 33 differentially expressed proteins (DEP) for GD versus IM, GD versus SX, and IM versus SX, respectively. Gene ontology annotation analysis showed that the largest number of DEP for the 3 comparisons were as follows: for biological processes: response to progesterone, glyceraldehyde-3-phosphate metabolic process, and negative regulation of megakaryocyte differentiation; for molecular functions: antioxidant activity, binding, and peroxiredoxin activity; and for cellular components: the same category of extracellular regions for the 3 comparisons, respectively. Pathways for the DEP of 3 comparisons were (1) disease; (2) synthesis and metabolism; and (3) synthesis, degradation, and metabolism. Protein–protein interaction network analysis showed that DEP for GD versus SX had the most interactions. [ABSTRACT FROM AUTHOR]

Milk proteins are well known to produce aerated food due to the amphiphilicity. However, milk proteins are commonly added in blends for the desirable properties in food industry. In this study, the foaming properties of milk protein mixtures (MPM), a mixtures of whey protein isolated (WPI) and milk protein concentrate (MPC), was studied through foaming capacity (FC), foam stability (FS), and foam morphology at pH 3.0–9.0. Physiochemical, structural, surface properties, and Pearson correlation analysis were measured to gain insight into foaming behavior. Results indicated that MPM showed excellent FC (113.0–114.3 %) and FS (90.7–93.0 %) at pH 6.0–9.0, and foam displayed a smaller size and uniform distribution. MPM solutions showed smaller particles, higher solubility, and lower apparent viscosity at pH 6.0–9.0, which resulted in an increase in surface pressure and adsorption rate (K diff), facilitating more protein absorbed to interface. To further investigate structural changes, various spectral methods were used, in which the structure of MPM was changed with pH. Correlation analysis further suggests that K diff and solubility positively affect the formation of foam, while free sulfhydryl and β -sheet contributed to stabilizing foams. These findings provide valuable information on MPM as ingredients for aerated foods under acidic, neutral, and alkaline conditions. • Foaming properties of milk proteins mixtures were varied at different pH values. • Milk proteins mixtures showed higher foaming properties at pH 6.0–9.0. • Milk proteins mixtures showed the lowest FC and FS at pH 5.0 and 3.0. • FC was positively correlated with K diff , solubility, and H 0. • FS was highly related to protein structure and interaction between proteins. [ABSTRACT FROM AUTHOR]

The investigation explores the structural changes and gel properties of heat-unfolded whey protein isolate (PWPI) with mogrosides (MFE) through the simultaneous rheological and fourier transform infrared (FTIR) techniques. The PWPI/MFE complexes potential application in non-fat yogurt were also detected. The results showed that MFE significantly increased the average particle size of the PWPI/MFE complexes and decrease the absolute zeta potential (P < 0.05). Complex formation was evidenced by protein structural changes when PWPI was bound to MFE. Multi-spectral analysis indicated that different MFE concentrations caused protein unfolding and the increase of a disordered structure. The simultaneous rheological and FTIR techniques indicated that the gel properties of PWPI/MFE complexes were much higher than that of PWPI. After addition of MFE, the bands at 2961, 1525, 1351, 1392, 1236 cm−1 occurred simultaneously. The microstructure of the PWPI added with 5 mg/mL MFE exhibited a higher degree of interconnectivity and a denser network than that of PWPI. In addition, the addition of 60 mL 10% PWPI/MFE complexes could significantly improve the syneresis, rheological properties and microstructure of non-fat yogurt. This study provides a theoretical basis for applying PWPI/MFE complexes as a food additive in developing the non-fat dairy foods. [Display omitted] • The addition of MFE affected the structural changes and gel properties of PWPI. • PWPIM structure was investigated by the simultaneous rheology and FTIR technology. • MFE mainly promoted the intermolecular hydrogen bonded β-sheet structures of PWPI. • The PWPIM improved the syneresis, rheology and microstructure of non-fat yogurt. • The PWPIM could be used as food additive in the non-fat dairy foods. [ABSTRACT FROM AUTHOR]

Soy isoflavones are widely used as a dietary supplement. However, the bioavailability of soy isoflavones is low due to the poor water solubility. Whey protein is an excellent biopolymer to encapsulate functional ingredients. In this study, soy isoflavones loaded whey protein nanoparticles were prepared using a pH-driven method. The physicochemical properties and in vitro digestion properties of the nanoparticles were investigated. The results showed that the physicochemical properties of nanoparticles were regulated by the mass ratios of soy isoflavones to whey proteins. Hydrogen bonding and hydrophobic interactions were confirmed in generating soy isoflavones loaded nanoparticles, which modified the thermal stability and secondary structure of whey proteins. The nanoparticles could pass through simulated gastric digestion to deliver soy isoflavones into the intestinal tract, responsible for the increased digestion stability and bioaccessibility of soy isoflavones. Moreover, the controlled release of soy isoflavones from nanoparticles can be achieved with a mechanism of non-Fickian diffusion. This study may provide useful information about the utilization of soy isoflavones loaded whey protein nanoparticles to develop functional foods. [Display omitted] • Soy isoflavones loaded whey protein nanoparticles were prepared using a pH-driven method. • Nanoparticles showed high encapsulation efficiency and loading capacity to soy isoflavones. • Thermal stability and secondary structure of whey proteins were modified by soy isoflavones. • Nanoparticles could target delivering soy isoflavones into the intestinal tract. • Digestion stability and bioaccessibility of soy isoflavones were improved by encapsulation. [ABSTRACT FROM AUTHOR]

Coenzyme Q10 (CoQ10) is one of the most popular dietary supplements in the United States of America. However, the bioavailability of CoQ10 is limited due to its poor water solubility and chemical form. In this study, CoQ10-loaded whey protein nanoparticles were prepared to improve the antioxidant activity and bioaccessibility of CoQ10. The results showed that the nanoparticle size depended on the whey protein-to-CoQ10 mass ratio and ranged from 50 to 200 nm. The zeta potential was relatively high, and the encapsulation efficiency of CoQ10 was over 98%. Analysis of differential scanning calorimetry and Fourier transform infrared spectra demonstrated that amorphous CoQ10 was associated with whey protein mainly by hydrogen bonding and hydrophobic interactions in the nanoparticles. Encapsulation improved the in vitro antioxidant activity of CoQ10 (p < 0.05) and its bioaccessibility (p < 0.05) during simulated gastrointestinal digestion. This encapsulation technology may be useful for encapsulating similar functional ingredients. [Display omitted] • ●Coenzyme Q10 (CoQ10) was encapsulated in whey protein nanoparticles. • ●Nanoparticles have high encapsulation efficiency of CoQ10. • ●The antioxidant activity of CoQ10 was improved by encapsulation. • ●CoQ10 was delivered into the intestine with improved bioaccessibility. [ABSTRACT FROM AUTHOR]

Abstract: The objective of this study was to formulate and evaluate a novel liquid paper glue based on a renewable material, polymerized whey proteins (PWP), and a synthetic polymer, polyvinylpyrrolidone (PVP) K90. Both PWP and PVP separately and/or cumulatively played important roles in the viscosity and bonding strength of the glue. Two optimized formulations (prototype A and prototype B) were analyzed for physicochemical and adhesive properties, microstructure and storage stability. A commercial product was used as a reference for comparison. Both prototypes had comparable bonding strength with the control, showed full substrate failure in the lap-shear strength tests, and exhibited faster setting property than the control. Viscosity of the prototypes was lower than that of the control, but they were still easy for application and spread. Scanning electron microscope (SEM) analysis showed that combined PVP and PWP formed more compact networks compared with those formed by PWP alone. Not only did they have desirable adhesive properties, both prototypes with addition of an antimicrobial agent also had stable shelf lives. Neither significant changes of bonding strength, viscosity or appearance, nor growth of microbes was observed during storage at 23°C or 40°C for 12 months. In conclusion, the whey protein based paper glue has comparable functional properties to the commercial product. [Copyright &y& Elsevier]