Hemp seed oil bodies (HOB) is a natural lipid delivery system with exceptional nutritional value and interfacial properties. However, its environmental instability and limited interfacial functionality restrict its practical application in food systems. This study aimed to investigate the effects of chitosan (CS) with pH-dependent electrostatic interactions on the interfacial assembly behavior of HOB complexes and how structural evolution influences HOB stability. The results showed that at a CS pH = 3.5, strong electrostatic complexation occurred with HOB, with an average particle size of 415.75 +/- 5.65 nm and a potential of 41.46 +/- 1.57 mV. Multispectral analysis revealed that the-NH3+ of CS formed electrostatic complexes with the phospholipid PO2- and protein-COO-groups on the HOB surface, as well as hydrophobic interactions and hydrogen bonds, thereby inducing an ordered conformational rearrangement of the interfacial proteins. The effective coating of CS formed a core-shell structure, significantly reducing surface hydrophobicity and contact angle, optimizing the interfacial behavior of the HOB emulsion. Phase separation during storage was reduced, enhancing the stability of HOB. In vitro digestive simulations prevented the adsorption of lipases, achieving a delayed release of free fatty acids. But at neutral pH, bridge-linked flocculation caused phase separation to occur early in CS-HOB, weakening the protective effect on HOB. This research provided a theoretical basis for the development of novel polysaccharide-HOB systems and the exploration of their mechanisms.

This study systematically investigated the effects of ohmic heating on the structure and Pickering emulsion stability of whey protein fibrils, formed through multiround induction. Whey protein fibrils with varying induction cycles (F0-F6) were constructed via self-assembly and multiround induction, followed by ohmic heating treatment to analyze changes in their structure, molecular properties, and emulsifying behavior. The electric field environment was found to promote the lateral growth of fibrils. Concurrently, it disrupted the structure of the cross-beta-sheet. This disruption resulted in a looser fibril architecture, increased periodicity, reduced antiparallel beta-sheet content, and concomitantly decreased surface hydrophobicity and charge. With increasing induction cycles, the fibril content first increased and then decreased, reaching its maximum at F2. Peptide segment analysis further revealed that under electric field induction, fibril aggregation became more disordered, the release of hydrophobic peptide segments was reduced, and molecular flexibility declined. Emulsion stability results indicated that the Pickering emulsion stabilized by F2 fibrils exhibited the highest stability, with a 6.12% improvement compared to the F0 Pickering emulsion. The fractured fibrils and branched structures facilitated interfacial adsorption and crosslinking between oil droplets, forming a three-dimensional network that significantly reduced the flocculation index. The synergistic regulation of ohmic heating and multiround induction modulated the assembly pathway and structural characteristics of protein fibrils, providing a new strategy for constructing highly stable Pickering emulsions.

This study elucidated the mechanistic role of cold plasma (CP) treatment in modulating the structure of rice bran protein (RBP) to enhance the performance of vegetable oil-based whipped cream, which was crucial for its quality and include its overrun, textural, rheological, and stability characteristics. Through a systematic analysis of CP-induced alterations in the molecular conformation of RBP-specifically examining free sulfhydryl content, secondary structure, and tertiary structure-as well as its functional properties, including solubility, emulsifying activity index (EAI), and foaming capacity (FC). We identified an optimal CP treatment duration of 2-6 min, which effectively balanced protein unfolding with oxidative aggregation. Extended CP exposure beyond 6 min resulted in excessive oxidation, leading to protein reaggregation and reduced functionality. Key findings revealed that moderate CP treatment (4-6 min) disrupted RBP's disulfide bonds, resulted in a reduction of alpha-helix and beta-sheet contents by 17.24 % and 31.21 %, respectively, while increasing beta-turn and random coil contents. These structural changes enhanced RBP's EAI by (55.03 f 1.25 m2/g) and improved FC by 126.3 f 3.34 % compared to native RBP. When applied to whipped cream formulations, the optimized CP-RBP significantly improved whipping efficiency, reduced the time to 413.33 f 3.05 s, and increased overrun to 194.08 % f 2.16 %. Additionally, it conferred superior storage stability and microstructural homogeneity, as demonstrated by fluorescence microscopy and rheological assessments. This work provides a structure-function rationale for CPmediated protein engineering, offering a green strategy to tailor plant-based proteins for high-performance dairy alternatives.

Active sites for microwave plasma interaction with rice bran protein (RBP) were identified through fractionation into albumin, globulin, and glutelin components. Spatial unfolding patterns were analyzed alongside amino acid composition changes and side-chain oxidative modifications to elucidate correlations between oxidation extent and RBP conformational alterations. The results indicated that albumin exhibited 105.75% increase in surface hydrophobicity, 65.66% increase in free sulfhydryl content, 26.60% increase in solubility, and 1.11-fold and 1.47-fold increases in emulsifying activity index and emulsifying stability index under the optimal conditions of 160 W power and 3 min treatment time. Globulin demonstrated maximal structural expansion at 160 W for 5 min, with 109.34% increase in surface hydrophobicity, 74.77% increase in free sulfhydryl groups, 20.40% enhancement in solubility, and 1.72-fold and 1.59-fold improvements in emulsifying activity and stability index. Glutelin achieved optimal modification at 180 W for 7 min, showing 61.17% increase in surface hydrophobicity, 11.49% increase in free sulfhydryl content, 18.30% increase in solubility, and 2.11-fold and 2.03-fold enhancements in emulsifying activity and stability index. Amino acid content changes, oxidation kinetics, and highresolution mass spectrometry results indicated that amino acids such as cysteine, methionine, lysine, arginine, and tryptophan exhibited high oxidative reactivity. Furthermore, sulfur-containing amino acid residues underwent oxidation, trioxidation, and nitrosation with stage-dependent oxidation patterns. Aromatic residues exhibited oxidation, trioxidation, and kynurenine formation. Basic residues displayed oxidation, alpha-aminoadipic semialdehyde, and alpha-aminoadipic acid formation. Based on these findings, the cleavage of hydrogen bonds and disulfide bonds caused by microwave plasma oxidation of amino acid side chains was the primary factor in the unfolding of RBP spatial structure, thereby clarifying the correlation mechanism between the degree of oxidation and RBP spatial conformational changes. The results of this study provide theoretical support for precise protein modification and technical support for converting plant protein from low-value byproducts to high-value food ingredients.

To clarify the regulatory effect of microwave pretreatment on the stability of rice bran oil body (RBOB) and its practical value, this study systematically investigated the impact of different microwave power pretreatments on the yield rate, rheological behavior, microstructure and multispectral structure of RBOB. It also systematically explored the regulatory mechanism of this pretreatment strategy on the RBOB stability. The results showed that microwave pretreatment significantly affected the extraction efficiency and physicochemical properties of RBOB. Among them, 300 W was confirmed as the optimal microwave power. Under this power, the yield rate (76.42%) of RBOB significantly enhanced, the rheological behavior exhibited typical shear thinning characteristics and the viscoelasticity was ascended. The microscopic structure presented that oil body (OB) particles were uniformly dispersed and the interface was clear and intact. The multi-spectral characteristics revealed that the interface protein conformation was moderately stretched and relaxed, forming an interface protein membrane with both mechanical flexibility and molecular looseness, thereby effectively improving the physical stability and dispersibility of OB. Based on RBOB pretreated with optimal microwave power, a comprehensive evaluation was conducted on the encapsulation performance, oxidative stability and in vitro release behavior of nobiletin. The results revealed that this approach significantly enhanced the encapsulation efficiency (80.75%) and loading capacity (4.0373 mg/g) of nobiletin, effectively delayed its oxidative degradation, and regulated its in vitro release rate (20.53%) to achieve sustained-release properties and significantly improve its bioaccessibility. Furthermore, it offers a theoretical basis and technical support for the resource utilisation of RBOB and the development of functional products.

In this study, a novel heat treatment method ohmic heating treatment was employed to improve the rigid structure of whey protein fibrils and enhance the stability of Pickering emulsions. Unlike conventional heating treatment, the electric field generated by ohmic heating treatment resulted in shorter and looser fibril structures. Although the overall yield of fibrils decreased, their surface hydrophobicity increased. The intersheet of the cross-beta-sheet structure in mature fibrils formed by ohmic heating treatment increased from 9.954 & Aring; under conventional heating to 10.987 & Aring;, accompanied by larger diameters and more pronounced periodic structures. The Pickering emulsion stabilized by mature fibrils formed through ohmic heating treatment exhibited a 9.16% increase in emulsion stability and a 40.88% reduction in the flocculation index. The difference in Pickering emulsion stability was attributed to structural variations in the mature fibrils. The higher surface hydrophobicity of the mature fibrils produced by ohmic heating treatment facilitated their faster adsorption onto the oil droplet interface. Moreover, the fractured fibril structures enhanced molecular flexibility and promoted cross-linking between oil droplets, leading to the formation of a three-dimensional network structure that further improved the stability of the Pickering emulsion. The fibrils prepared via ohmic heating treatment possessed unique properties, which may hold significant potential for protein fibrillation processes and the production of stable food-grade Pickering emulsions.

As previously demonstrated in our studies, microwave plasma oxidation could effectively induce structural unfolding and enhance functional properties of rice bran protein (RBP). This study continuously investigated the mechanism by which this technology improved RBP interface behavior and emulsion characteristics. The results showed that the RBP sample treated at 160 W for 5 min (ORBP) diffused, adsorbed, and reoriented more rapidly; its diffusion rate, permeation rate, and rearrangement rate were 0.6790 mN m-1 & sdot;s-1/2,-2.4068 x 10-4s-1, and-15.76 x 10-4s-1. Compared to RBP, ORBP exhibited an increased interfacial dilatational modulus E; the slope of the curve between E and interfacial pressure pi increased from 2.1578 to 3.5561; the near-equivalent values of ORBP's elastic dilatational modulus E ' to E, indicating a denser interfacial membrane formation. In emulsions, ORBP significantly reduced droplet size and improved uniformity; the D4,3 value, polydispersity index, centrifugal stability constant, and creaming index decreased to 0.84 mu m, 0.427, 80.87 %, and 18.89 %. After 5 h of standing, the flocculation index decreased by 28.43 %. The absolute Zeta potential increased to 19.93 mV, and the percentage of adsorbed proteins rose by 22.76 %. Microwave plasma treatment oxidized plant protein, inducing structural unfolding, disulfide bond reorganization, and surface charge modification, which enhanced the solubility, interfacial activity, and emulsion stability of plant proteins. This study provides reference for understanding oil-water interfacial behavior of plant proteins and regulating the performance of plant protein-based emulsions.

This study employed chitosan (CS) for the electrostatic immobilization of Rhizomucor miehei lipase (RML). The immobilized lipase exhibited an activity retention of 95.43% and formed a stable oil-in-water (O/W) Pickering emulsion with a particle size of 400 nm. With tripalmitin (PPP) as the substrate, ethanol was introduced to react with the enzymatically hydrolyzed palmitic acid (PA), forming ethyl palmitate and consequently enhancing 2-MAG generation. Furthermore, Al(OH)₃ was incorporated into the aqueous phase effectively inhibiting acyl migration. Following separation and purification, a high 2-MAG content of 96.24% was achieved. Subsequently, using 2-MAG and oleic acid (OA) as substrates for esterification, the yield of 1,3-dioleoyl-2-palmitoylglycerol (OPO) reached 82.53%. Notably, the enzyme maintained 80.91% of its activity after 17 reuse cycles in the esterification reaction. This method offers a novel approach for the efficient synthesis of OPO.

: In this study, sodium tetraborate (Na2B4O7) was used as an inhibitor to exploit the electron-withdrawing capability of boron atoms, it locks the activated lone pair electrons of hydroxyl oxygen and blocks the formation of the first intermediate, thereby inhibiting acyl migration. Under the optimized conditions of pH 6.0, temperature 60 °C, enzyme addition 0.02%, Na2B4O7 addition 0.8%, and reaction time of 4 h, the phosphorus content in crude soybean oil was reduced to 12.1 mg/kg, while the FFA content increased to 1.05 g/100g. Compared to conventional enzymatic degumming, the FFA content was reduced by 0.19 g/100g, and the acyl migration rate was decreased by 17.0%. Liquid chromatography analysis confirmed that the addition of the inhibitor achieved moderate enzymatic degumming of crude soybean oil.

Rice bran protein (RBP) exhibits weak interfacial adsorption capacity due to its dense natural conformation. As a green non-thermal technology, microwave cold plasma can induce moderate oxidation and structural unfolding of RBP. Combined with the non-covalent interactions of polyphenols, the solubility and emulsifying properties of RBP can be further improved. In the study, oxidized RBP (ORBP) was used as the substrate to construct non-covalent complexes by regulating polyphenol phloridzin (PHL) addition levels, and the effect of complex structure changes on the interfacial properties of emulsion was investigated. The results indicated that PHL acted as a hydrogen donor, forming hydrogen bonds with ORBP. Compared to ORBP, the ORBP-PHL complex exhibited a trend of reduced α-helix and β-sheet, along with increased β-turn and random coil. PHL quenched the fluorescence of ORBP in an enthalpy-driven exothermic reaction, with ΔH = -67.288 kJ·mol-1 and ΔS = -172.154 J·K-1·mol-1. When the concentration of PHL was 1 mg/mL, the complex exhibited minimal average particle size, PDI value, and turbidity, alongside maximum solubility. At this concentration, the interaction between PHL and ORBP further induced the ORBP structure to become flexible, and the attenuation rate of surface tension increased. The value of diffusion rate (Kdiff) increased to 0.9038 mN·m-1·s-1/2, whilst the value of permeation rate (Kp) decreased to -2.6794 × 10-4 s-1. The exposure of more hydrophobic groups enhanced the affinity of ORBP to the oil phase, forming an interface membrane with stronger elasticity. At a PHL concentration of 1 mg/mL, the emulsion stabilized by the binary complex exhibited the smallest D4,3 value and CI value, reaching 0.52 μm and 10.01% respectively. While the absolute zeta-potential, apparent viscosity, storage modulus, and loss modulus reached their maximum values. The emulsion with high storage stability and thermal stability was formed by the non-covalent interaction between PHL and ORBP. These findings provide a theoretical foundation and scientific rationale for expanding the application scope of RBP, as well as advancing its high-value and resource-efficient utilization.

The purpose of this paper is to reduce the acid value of rice bran crude oil and make a new rice bran oil (RBO) with conjugated linoleic acid (CLA). Linoleic acid isomerase from Bifidobacterium breve was immobilized on a magnetic nanoflower carrier of Fe3O4-SiO2-NFs. Molecular docking simulations were performed to investigate the interaction and binding mode conformation between isomerase and linoleic acid (LA) molecules by using computer software. This isomerase was used in isomerization reaction of high acid value RBO. Under the optimal enzymatic isomerization conditions, the conversion rate of LA was 62.13 %. The content of c9-CLA and t11-CLA in the product of enzymatic isomerization reaction was 23.50 ± 0.25 %. After six repeated uses, the relative activity of the immobilized enzyme remained above 70 %. Esterification reaction was performed from monoacylglycerol and RBO with CLA under the catalysis of magnetic immobilized lipase. The CLA glyceride content was 14.09 ± 0.53 % in new RBO product. The acid value of RBO decreased to 0.31 ± 0.15 mgKOH/g, and the peroxide value was 1.03 ± 0.14 mmol/kg. It may provide a sustainable pathway for RBO refining that combines deacidification with CLA-functionalization.

To investigate the effects of microwave plasma treatment on rice bran protein (RBP), various power levels (150, 160, 170, 180, and 190 W) and processing times (1, 3, 5, 7, and 9 min) were examined for their impact on the conformation, physicochemical properties, and functional properties. The results showed that high-energy active particles generated by microwave plasma could oxidize modify the spatial structure of RBP, thus affecting its functional characteristics. The primary structure of RBP, as revealed by SDS-PAGE, remained unchanged. While the content of beta-sheet structures initially decreased and then increased, the random coil content first increased and then decreased, the spatial structure first unfolded and then folded again. The intrinsic fluorescence spectrum showed that hydrophobic amino acids buried within the protein's interior were initially exposed but later reburied. The disulfide bond was first broken to sulfhydryl group and then reformed due to excessive oxidation, which promoted the intermolecular aggregation of RBP. Compared with its natural counterpart, the average particle size decreased from 519.6 nm to 186.7 nm at a power of 160 W and a treatment time of 5 min. Consequently, the emulsification activity index and the stability index increased by factors of 2.18 and 1.40, respectively. The foaming capacity index and foam stability index reached maximum values of 73.07% and 43.34%, respectively. These results provide theoretical evidence for the application of microwave plasma technology to modify plant proteins.

Soybean is regarded as a high-quality protein source for gout patients to replace meat products, but it is classified as medium-purine foods. This study developed the Poly-alizarin red S/β-cyclodextrin/multi-walled carbon nanotubes/indium tin oxide electrode (PARS/β-CD/MWCNTs/ITO) for the simultaneous detection of guanine (G) and adenine (A) in soybean. The electrode was fabricated via electropolymerization and characterized by SEM, TEM, FT-IR, and XRD. Cyclic voltammetry and electrochemical impedance spectroscopy confirmed its enhanced active surface area and charge transfer efficiency. The sensor demonstrated wide linear ranges of 1.0-500 μM for G and 0.1-500 μM for A, with detection limits of 0.01 μM and 0.02 μM, respectively. The peak separation between G and A was 420 mV, enabling simultaneous quantification. Applied to soybean samples, the sensor achieved recoveries of 98.6-100.2 %, validating its accuracy and potential for real-time monitoring of purine content in soybean products.

Soybean oil body (SOB) emulsion was combined with carboxymethyl chitosan (CMCS) to improve the stability of the oil body system, and the influence on the characteristics of SOB emulsion was explored. It was found that the particle size of SOB emulsion without CMCS was the smallest, 422.7 nm. After the addition of CMCS, the particle size of all samples increased, and the particle size of SOB-CMCS emulsion was the smallest (480.0 nm) when the amount of CMCS was 0.4 %. At this time, the surface hydrophobicity (H0) of the sample is 230.5, and the emulsification stability is 69.83 min. The results of interfacial stability show that adding appropriate concentration of CMCS can reduce the interfacial tension of the sample. The results of rheological model fitting showed that the consistency coefficient of SOB-CMCS samples with 0.8 % CMCS addition was 3.75, which was the highest among all groups. The environmental stability test of SOB-CMCS emulsion showed that the particle size of SOB-CMCS emulsion with 0.4 % CMCS content was 944.0 nm after heating at 90 °C for 30 min, and the particle size of SOB-CMCS emulsion was 979.8 nm at 300 mmol/L salt ion concentration, which showed the smallest change compared with other groups.

Conjugated linoleic acid (CLA) has good physiological functions and broad application prospects, but it also has the disadvantages of being easily oxidized and uncontrolled release. In this study, high-amylose corn starch (ACS), waxy corn starch (WCS), and normal corn starch (NCS) were complexed with CLA using the solvent method. The results showed that starch-CLA complexes of ACS-CLA, WCS-CLA, and NCS-CLA were prepared with combination rates of 7.43 %, 3.31 %, and 4.33 %, respectively. ACS-CLA complex had the strongest protective effect on CLA, and the peroxide value was 2.71 mmol/kg on the 10th day of accelerated oxidation. The ACS-CLA complex had the highest stability with a CLA release rate of 7.6 % in simulated gastric fluid. The release rate of CLA in 12 h was 24.32 % in the simulated intestinal fluid. The starch-CLA complex improved the oxidative stability of CLA, and the release amount of CLA was well controlled.

This work investigated the binding interaction between (+)-catechin (CC) and rice bran protein isolate (RBPI) by determining the structure and function. The binding methods were covalent and non-covalent with different CC concentrations (0.05, 0.15, and 0.25

In this study, magnetic Fe3O4 nanoparticles were modified with sodium alginate to prepare a magnetic composite carrier (Fe3O4-SA). Partial glyceride lipase was immobilized onto this carrier (Fe3O4-SA-GS50), and enzymatic deacidification of high-acid rice bran oil was conducted using ethanol as an acyl acceptor. The results showed that Fe3O4-SA particles exhibited a spherical structure with a specific surface area of 101.57 m2/g and an average diameter of 116.60 nm. After immobilization, the average diameter of Fe3O4-SA-GS50 particles increased to 141.50 nm. The immobilized lipase exhibited optimal activity at 40 degrees C and pH 7.0, with an immobilization efficiency of 91.1 %. Under conditions of 2:1 ethanol-to-free fatty acid molar ratio, 30 U/g enzyme dosage, 40 degrees C, and 6 h reaction time, the acid value of rice bran oil was reduced to 2.04 mg KOH/g. The deacidified oil retained 90.3 mg/100 g vitamin E, 1.50 % gamma-oryzanol, 1020.5 mg/kg phytosterols, 59.55 % triglycerides, 0.96 % diglycerides, and 0.05 % monoglycerides.

This study aims to prepare soybean protein isolate (SPI)-arbutin (AR) non-covalent complexes and treat them using cavitation jets at different pressures. Fourier transform infrared and ultraviolet spectroscopies confirmed the successful cross-linking of SPI with AR. The secondary structure of SPI was transformed from a disordered to an ordered state. Endogenous fluorescence spectroscopy showed that the introduction of AR and subsequent cavitation jet treatment altered the tertiary structure of the complex, exposing more tryptophan residues and leading to the fluorescence burst phenomenon in SPI. Molecular docking simulations further demonstrated the non-covalent binding interactions between SPI and AR, identifying potential binding sites of AR and SPI. Cavitation jet treatment significantly enhanced the emulsifying properties and interfacial adsorption characteristics of the SPI-AR non-covalent complexes. Atomic force and confocal laser scanning microscopies, at a treatment pressure of 12 MPa, demonstrated significant changes in the microstructure of the complexes, characterised by smaller particle sizes and without aggregation. The solubility of the protein increased to 74.4%, surface hydrophobicity increased to 17361.3, the diffusion rate value of the sample was 0.6374, and the contact angle was 47.15 degrees. These findings offer theoretical support for the wider application of SPI in the food industry.

The contents and ratios of 7S and 11S globulins are crucial for the nutritional value and functional properties of soybean proteins. Typically sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is used to detect 7S and 11S globulin in soybeans however this method involves slow analysis procedures and high costs. Near-infrared (NIR) spectroscopy technology has emerged for detecting soybean protein content, enabling rapid non-destructive testing with advantages of convenient measurement, minimal sample processing requirements, and simultaneous determination of multiple components. To resolve the issue of shared quantitative prediction models between NIR spectroscopy-based 7S and 11S protein content predictions for various soybean seed and soybean powders, a transfer method of standard-free model based on transfer learning (TL) was proposed. Firstly, the NIR data of different forms of soybean samples were collected, and the near-infrared prediction models of 7S and 11S protein content were established. Secondly, the direct standardization (DS) and piecewise direct standardization (PDS) algorithms were improved to propose a DS-PDS-based model transfer method, with the influence of the sequence of preprocessing and model transfer algorithm on overall model transfer scheme was explored. Then, IRM is used to force the model to learn invariant features with causal relationship with labels by constraining the optimal classifier consistency of the model in different environments. Finally, aiming at standard sample sets corresponding to master-slave spectra required by traditional model transfer methods, the model transfer effect was investigated using a model transfer method based on standard-free migration learning. Results showed that the model transfer method based on without standard transfer learning was more suitable for 7S and 11S globulin content modeling between soybean seeds and soybean powders. It is intended to provide efficient and accurate 7S and 11S protein content detection methods for soybean processing enterprises and support quality control of soybean protein products and production of functional products.

Developing efficient and cost-effective electrocatalysts for the urea oxidation reaction (UOR) presents a challenge. Here, we constructed a RuO2 nanoparticle (NPs)-modified NiSx/C3N4 nanoarray heterostructure (Ru/NiSx/ C3N4) on a nickel foam (NF) substrate using a combination of impregnation and chemical vapor deposition (CVD) processes. This catalyst achieves a current density of 10 mA & sdot;cm- 2 at an ultralow potential of 1.27 VRHE in alkaline UOR. The Ru/NiSx/C3N4 exhibits lower overpotential and electrochemical impedance spectroscopy (EIS) than the pristine NiSx/C3N4 array, indicating its superior kinetic performance. Combined in situ spectroscopy and density functional theory (DFT) calculations reveal that in situ generated Ni3+ (NiOOH) is the actual active site for UOR, while the high-valence Ru delta+ serves as an adsorption center for OH- ions, preventing competitive adsorption between OH- and urea molecules at the NiOOH site on the surface of the pristine NiSx/ C3N4 array structure, thereby reducing the adsorption Gibbs free energy (Delta G) of UOR intermediates. These insights provide new avenues for the development and understanding of electrocatalysts designed for the electrochemical degradation of urea-rich wastewater and the electro-oxidation of other organic molecules.