Mung bean protein is an emerging source of pulse proteins with good foaming properties. The relation among its physicochemical properties, foamability and interfacial behavior of individual protein fractions (albumins-rich fraction (ALB) and globulins-rich fraction (GLO)) and their mixtures (0.1 %, w/w) at distinct mass ratios (AG14, AG23, AG32, and AG41) has not elucidated in depth and was investigated in this study. ALB demonstrated significantly higher foaming capacity than GLO, attributable to its smaller particle size, lower surface charge, and enhanced hydrophobicity, facilitating rapid interfacial adsorption. ALB-GLO mixtures (AG14, AG23, AG32, and AG41) exhibited comparable foam capacity with ALB. Nevertheless, ALB-stabilized foams had substantially inferior stability compared to GLO systems. GLO dominated the foaming properties of MPI due to its status as the primary constituent. Synergistic effects in both interfacial strength and foam stability at the interface were explored through ALB-GLO mixture at varying ratios. AG14 exhibited the highest interfacial strength among mixed samples, implying the occurrence of synergistic effect between ALB and GLO. The highest foam stability was found for GLO, which was primarily due to the formation of stiff interfacial layers and probably also pinning of the lamellae in the foams by GLO. Overall, mung bean albumins exhibited substantially higher foaming capacity than the globulins, and these outcomes highlight that mung bean protein mixture at certain mass ratio possesses great potential for a plant-resourced foam-based food ingredient.

The air-water interfacial and foaming properties of three mung bean protein fractions (albumin (ALB), globulin (GLO) and mung bean protein isolate (MPI)) as a function of pH values (3.0, 5.0, 7.0, and 9.0) and ion strengths (10, 100, 500, and 1000 mM) were investigated here. We used interfacial dilatational rheology, characterized the physicochemical properties, and linked the outcomes to the foaming properties of three mung bean protein fractions. At neutral pH (7.0), the mean particle diameter was in the following order: MPI > GLO > ALB. Mean particle size was highly dependent on the pH value. Under identical pH conditions, the surface hydrophobicity of various mung bean protein fractions followed the order: GLO > MPI > ALB. For GLO and MPI, surface hydrophobicity progressively increased with rising ionic strength from 10 to 1000 mM. Proteins at pH values close to their isoelectric point (IEP) can provide the highest surface pressure during the initial adsorption stage (0-10 s). The elastic modulus initially decreased and then increased with rising pH, reaching its minimum at pH 5.0. Foamability was in the following order: ALB > MPI > GLO, varied remarkably with pH, with the effect being more pronounced for GLO. The foamability of both MPI and GLO at pH 5.0 was significantly higher than that at pH 7.0. Compared to GLO, ALB exhibited relatively lower foam stability, likely due to weak interfacial interactions, which failed to prevent particle coalescence. Rising pH from 3.0 to 9.0 continuously reduced the foam stability of ALB, due to enhanced electrostatic repulsion between protein molecules and potential excessive unfolding. The findings gained from this study may provide some useful information to expand the application of mung bean proteins as effective air-water interfacial and foaming stabilizers.

The EGCG/PPN composite, prepared by combining pea protein nanofibrils (PPNs) with epigallocatechin gallate (EGCG), could be used as a multifunctional nanocarrier. Compared to pea protein isolate (PPI), EGCG/PPN composites exhibited remarkably higher turbidity and zeta potential, along with similar UV spectra. Intrinsic fluorescence spectroscopy, ThT fluorescence spectroscopy, and surface hydrophobicity analysis suggested that the interactions between EGCG and PPN were primarily driven by hydrophobic forces. UV spectra indicated that the microenvironment of amino acid residues in the tertiary structure of the protein changes upon complexation, and circular dichroism (CD) revealed that the incorporation of EGCG increases the β-sheet content in the protein’s secondary structure. Analyses of DPPH and ABTS radical scavenging activity, as well as reducing power, demonstrated that the synergistic effect between EGCG and PPN did not hinder the inherent antioxidant properties of EGCG but rather enhanced them significantly. Transmission electron microscopy (TEM) images showed that the addition of EGCG reconstructed the fibril morphology, thereby affecting the properties of PPNs. Overall, the composite fabricated through the interaction between PPN and EGCG shows great potential as a nanocarrier in the processing of functional foods.

Pea protein nano-micelles gained with partial hydrolysis by a proteolytic enzyme (Protamex) were employed as nanocarriers to encapsulate and stabilize liable and hydrophobic curcumin (CUR) with two various methods (pHdriven method (PDM) and ethanol-induced method (EIM)). Both CUR-loaded pea protein hydrolysates (PPHs) nano-micelles by PDM and EIM exhibited spherical shapes, and uniform particle size distributions. Highest CUR loading amount (3.21 %) was gained with PPHs by PDM. The interaction between PPHs nano-micelles and curcumin was comprehensively examined with optical spectroscopy. These outcomes obviously demonstrated the water solubility, storage stability against UV light and heating, bioaccessibility and in vitro antioxidant activity of CUR can be pronouncedly enhanced with PPHs-based nanocarriers. Interestingly, PPHs-CUR nano-micelles fabricated with PDM have higher loading amount, light stability, and better bioaccessibility as well as antioxidant activity than those by EIM. These results clearly show that PDM may be a better method than EIM and provide useful information in nutraceuticals encapsulation with vegetable proteins-based delivery systems.

In this study, PPN-Cur/EGCG hydrogels were fabricated through EGCG-induced PPN gelation for Cur encapsulation. WHC of PPN-Cur/EGCG and PPN/EGCG hydrogels was both higher than 80 %. At [E]/[P] = 0.15, PPN-Cur/EGCG hydrogel exhibited the highest EE (76.70 %), and LA (15.30 μg/mg). Interaction forces assay illustrated hydrophobic interactions, hydrogen bonding, and ionic bonding dominated the formation of PPN-Cur/EGCG hydrogel. SEM revealed wrinkled porous architectures of PPN-Cur/EGCG hydrogel. Optimal [E]/[P] ratio (0.15, w/w) yielded dense homogeneous networks, whereas excessive EGCG caused surface coarsening and hyper-crosslinking. PPN-Cur/EGCG hydrogels at [E]/[P] (0.15, w/w) exhibited the highest UV stability (78.71 %) after 180 min UV light exposure. PPN-Cur/EGCG hydrogel possessed exceptional antibacterial activity against S. aureus and E. coli. Compared to Cur (free), the bioaccessibility of Cur (30 %) was increased by almost 3-fold. The information found here provides valuable insights into the forming mechanisms PPN-Cur/EGCG hydrogels mediated by EGCG, and broadens the potential applications in food systems of PPNs.

The purpose was to apply metal ions to induce the formation of alpha-lactalbumin fibril-based hydrogel to create a versatile nano-carrier for effective quercetin encapsulation and delivery. Quercetin could be successfully embedded into the hydrogel primarily through hydrogen bonding and hydrophobic interaction, as demonstrated by FTIR and XRD. Quercetin encapsulation effectiveness in alpha-lactalbumin fibril-based hydrogel via metal ions was up to 91.82 %, 7.41-fold higher than that with alpha-lactalbumin directly. Rheological results revealed elasticity was the dominant behavior of these hydrogels and quercetin addition could lead to a slight decrease of both G ' and G '', presumably due to the formation of soluble macroparticle aggregates and insoluble aggregates caused by polyphenol like quercetin. Quercetin bioaccessibility was increased to 32.62 % by 2.82-fold with this hydrogel. Additionally, the hydrogel demonstrated strong UV stability, antioxidant activity, and water retention. This research could provide practical and theoretical support to widen the development of new alpha-lactalbumin-derived food products.

Background Probiotics, often referred to as beneficial microorganisms, and prebiotics, non-digestible food ingredients that promote the growth of beneficial bacteria, have garnered significant attention in the food industry due to their health benefits. The co-encapsulation of probiotics with prebiotics has emerged as a promising approach to enhance the effectiveness and stability of probiotics with prebiotics in food products. Scope and Approach This review examines the classification and health benefits of probiotics and explores various co-encapsulation techniques such as freeze drying, spray drying, electro-hydrodynamic atomization, complex coacervation, and emulsification/internal gelation. It also delves into how encapsulation techniques and biopolymers enhance solubility and bioavailability, mask undesirable smells or flavors, improve stability and food preservation, prevent degradation during storage or absorption, increase viability, and improve tolerance to detrimental conditions in the gastrointestinal tract. Key Findings Co-encapsulation of probiotics with prebiotics enhances stability, increases encapsulation efficiency, and improves sensory attributes. This approach also promotes synergistic health benefits, enhances bioavailability, and facilitates the development of appealing, functional dairy and non-dairy foods, making them increasingly attractive to health-conscious consumers in the food industry. Conclusion Co-encapsulation of probiotics with prebiotics presents a viable strategy to maximize the health benefits of functional foods. By leveraging advanced encapsulation techniques, the industry can improve the delivery and efficacy of these bioactive compounds, leading to more stable, effective, and consumer-appealing food products. This approach holds substantial potential for developing new and innovative health-promoting products that meet the growing consumer demand for functional and fortified foods.

The effects of different valence metal ions on the formation of hydrogels with alpha-lactalbumin fibrils (ALAF) were comprehensively examined in this study. The properties of hydrogel were generally characterized with water holding capacity (WHC), rheology, texture, DSC and ICP tests. Except FeCl3, it was shown that KCl, NaCl, CaCl2, MgCl2, NiCl2, and AlCl3 at 90 mM could induce the formation of hydrogels with ALAF (40 mg/mL), and hydrogels formed by high valence metal salts had more good properties (viscoelasticity, WHC, and thermal stability), and the amounts of metal ions released from hydrogels with high valence salts after immersion in deionized water for 90 min were all below 10 %. Among them, the hydrogels fabricated with Mg2+ owned a maximum hardness of 35 g, up to 90 % WHC, and marvelous thermal stability. Overall, the finding about ALAFderived hydrogels may provide some new insights for the utilization of amyloid-like fibrils in food industry.

With heightened health awareness and regulatory guidelines, consumer preferences have shifted towards low/no saturated fat food products. Bigel has emerged as a viable solution for replacing saturated fat. In this study, a system based on bigel was developed using a potato starch-based hydrogel and a walnut oil/candelilla wax-based oleogel, and its quality characteristics including sensory properties, texture, rheology, crystal structure, solid fat content (SFC), and distribution uniformity of bigel were evaluated. The results indicated that the optimum ratio of oleogel (oil/wax = 25) to hydrogel (distilled water/starch = 30) for the prepared bigel-based margarine was 2:1 (w/w). The melting point of the bigel-based margarine ranged from 36.23 +/- 1.966 degrees C to 44.53 +/- 0.503 degrees C, with good plasticity, hardness, good thixotropy recovery and viscosity properties. The content of SFC was lower than 4%, the major crystal types were beta and beta ' polycrystalline and possessed a good homogeneity. Generally, the preparation of nutritious and healthy margarine based on bigel is practicable. This research may provide a theoretical basis and also focus on the practical development and application of novel lower-temperature spreadable margarines.

Curcumin, a natural polyphenolic compound, has many health benefits: instabilities and poor solubility limit curcumin's industrial applications. The encapsulation of curcumin in Pickering emulsion can enhance its bioavailability. Developing an efficient and simple method for fabricating a natural emulsifier for Pickering emulsion remains a significant challenge. Chitosan has gained attention for its nontoxicity and excellent emulsifying properties. The purpose of this study was to prepare four different types of self-aggregated chitosan particles using a pH-responsive self-assembling method. The aggregated particle properties are tuned by pH, degree of deacetylation (DDA), and molecular weight (MW) through control of surface charge, size (nano, micro, and floc), and contact angle. Pickering emulsions were prepared using different types of aggregated particles. As MW and pH increase and DDA decreases, aggregated particles networked structures formed, resulting in highly elastic gels more resistant to the breakdown of Pickering emulsion at ambient temperature. When ramped up to higher temperatures, the kinetic energy of aggregated particles increases, disrupting hydrogen bonds and potentially changing the systems from fluids to gels. The aggregated particles-based Pickering emulsion was used as the carrier for curcumin encapsulation. MW and DDA regulate drug loading, encapsulation efficiency, and release profile. It found that DDA and MW were responsible for tuning the properties of Pickering emulsion. This research provides a new perspective on selecting suitable chitosan for controlling the release of bioactive compounds in Pickering emulsions, considering factors such as adjustable rheological properties, microstructure, and macrostructure.

It is assumed that the stability and bioaccessibility of iron ions in iron–pea protein fibril (Fe-Fib PP) nanocomposite can be remarkably enhanced, and Fe-Fib PP exhibits great potential as an effective iron fortificant. Fe-Fib PP, a stable and effective iron supplement, was fabricated based on the reducing property of pea protein fibrils, derived from pea protein through thermal treatment at pH 2.0. The results demonstrated that the reducing power of iron was remarkably affected by fibril concentration and fibrillization degree. The reducing power of pea protein fibrils gradually enhanced from 0.31 to 0.92 with the increase in incubation time from 0 to 48 h. Compared with iron nanoparticles (Fe–Nano), Fe-Fib PP possessed much higher dispersibility. Additionally, the stability of iron in Fe-Fib PP was significantly higher than that in Fe–Nano under different storage conditions. X-ray photoelectron spectroscopy (XPS) outcomes revealed Fe (II) content in Fe-Fib PP (70.75 ± 0.65%) was remarkably higher than that of Fe–Nano (56.05 ± 0.50%). In addition, the bioaccessibility of Fe (II) dramatically improved from 42.7% to 62.8% using PP fibrils as carriers. The findings suggest that Fe-Fib PP is an effective iron nutrition enhancer.

The influences of laccase-catalyzed crosslinking on the structural, emulsifying and gelling properties of pea protein with chlorogenic acid were intensively probed. Molecular weight analysis illustrated the formation of pea protein aggregates by laccase-induced polymerization in the presence of chlorogenic acid and the increase of incubation time facilitated the aggregation. Particle size of pea protein-laccase-chlorogenic acid progressively enhanced increasing incubation time. Laccase-induced polymerization possessed remarkable impacts on the secondary and tertiary structure of pea protein, confirmed by circular dichroism, and fluorescence spectroscopy. Surface hydrophobicity of pea protein appreciably enhanced with laccase-induced crosslinking due to the exposure of interior hydrophobic amino acid residues. Emulsifying activity, emulsifying capacity, gel strength, and water-holding capacity of pea protein can be considerably enhanced with laccase-catalyzed crosslinking with chlorogenic acid, suggesting excellent functionalities for pea protein were accomplished after being modified by laccase with chlorogenic acid. The obtained information will widen pea protein's application in food systems.

Natural cross-linkers are extensively employed due to their low toxicity and biocompatibility benefits. Genipin acts as a precursor for producing blue colorants. The formation of these colorants involves the cross-linking reaction between genipin and primary amines present in amino acids, peptides, and proteins. Genipin is extracted from Gardenia jasminoides and Genipa americana. This article explains the cross-linking mechanism of genipin with proteins/polysaccharides to provide an overall understanding of its properties. Furthermore, it explores new sources of genipin and innovative methodologies to make the genipin recovery process efficient. Genipin increases food products' texture, gel strength, stability, and shelf life. The antibacterial, antiinflammatory, and antioxidant properties of chitosan, gelatin, alginate, and hyaluronic acid increased after genipin cross-linking. Lastly, drawbacks, toxicity, and directions regarding the genipin cross-linking have also been addressed. The review article covers how to recover and cross-link genipin with biopolymers for industrial applications.

Background The demand for high-quality protein is increasing globally due to population growth and a preference for plant-based food. Potato protein is a promising solution as it contains essential amino acids and can be used in food (dairy, meat) and pharmaceutical applications. However, a lack of comprehensive research on potato protein necessitates an updated review to assess its value and potential applications. Scope and approach This review aims to provide an updated review of potato protein, focusing on its bioactive and functional properties and potential uses. The review also explores the impact of different processing methods on the quality and functionality of potato protein, including extraction, isolation, and purification techniques. Key findings Potato protein is a rich and sustainable source of essential amino acids with a high nutritional profile. Potato protein's bioactivity and technological properties present significant interest in various industries such as food and pharmaceutical. These applications can potentially enhance the overall value and reduce the environmental impact associated with potato cultivation.In conclusion, Potato proteins are high-quality and allergen-free, offering numerous nutritional and functional benefits. However, further research is needed to improve extraction methods, increase protein content, and overcome application limitations. As demand for sustainable and plant-based sources grows, potato protein holds excellent promise as a valuable and versatile resource. Its utilization can help meet the world's increasing protein needs and support sustainable food production practices.

Food protein-based amyloid-like fibrils have been utilized recently to stabilize, encapsulate and increase the water solubility, chemical stability and bioaccessibility of labile and hydrophobic nutrients because of their unique structure (high aspect ratio and nanoscale size) endowing exceptional performance. In this study, formation mechanism of alpha-lactalbumin fibrils with acid-heat treatment was assessed with such as sodium dodecyl sulfate polyacrylamide gel electrophoresis, thioflavin T fluorescence spectroscopy, and Congo red UV-vis spectroscopy. Mature alpha-lactalbumin fibrils with a width of 10-15 nm and a length of 0.5-2.0 mu m were attained with a 24 h acid-heat treatment (pH 2.0, 85 degrees C). alpha-Lactalbumin self-assembled into alpha-lactalbumin fibrils mainly through hydrophobic interactions and hydrogen bonding. Compared with alpha-lactalbumin (native), the water solubility of quercetin in alpha-lactalbumin fibrils nanocomposites was markedly enhanced. Ultrasound further increased its water solubility. Quercetin-loaded alpha-lactalbumin fibrils with ultrasonication exhibited the highest antioxidant activity probably due to the highest loading amount of quercetin. Compared with quercetin (free), the bioaccessibility of quercetin in alpha-lactalbumin fibrils with ultrasound was increased to 24.85% (a 2.16-fold increase). The incorporation of quercetin-loaded alpha-lactalbumin fibrils nanocomposites exhibited no pronounced impacts on the stability of yogurt and remarkably enhanced the perception score of overall assessment, as illustrated with sensory evaluation. The finding demonstrates that quercetin-loaded alpha-lactalbumin fibrils nanocomposites can be used as functional supplements in food system.

Bovine serum albumin nanofibrils (BSNs) were fabricated under thermal treatment (85 degrees C) at acidic condition (pH 2.0) and the incubation time on the structural, and physicochemical characteristics were probed. The formation and development of BSNs have been detected and confirmed by Thioflavin T (ThT) fluorescence and circular dichroism (CD) measurements. The structural alterations of bovine serum albumin (BSA) have also been investigated using intrinsic fluorescence and Congo red (CGR) UV -vis spectroscopy. Atomic force microscopy (AFM) outcomes displayed the morphologies of BSNs at varied time, with a diameter of about 3 nm and a contour length of about 200 nm at 24 h. The apparent viscosities of BSNs at three different pH were in the following order: pH 3.0 > pH 5.0 > pH 7.0. Emulsifying and foaming properties of BSA were pronouncedly enhanced through fibrillation, which was highly correlated with the interfacial properties and structural characteristics. Highest EAI 54.2 m(2)/g was attained at 48 h and no pronounced alterations were observed for EAI at 24 h and 48 h. Maximum value of FC was obtained at 48 h for BSA. This study will provide some useful information in understanding the formation of BSNs and broaden their application in food systems as functional food ingredients.