Effect of Steam Flash-Explosion on Physicochemical Properties and Structure of High-Temperature Denatured Defatted Rice Bran Protein Isolate.

The effects of Steam Flash-Explosion (SFE) on the physicochemical properties and molecular structure of high-temperature denatured defatted rice bran protein isolate (RBPI) were investigated. The mechanism of SFE treatment on high-temperature denatured defatted RBPI was revealed. The analysis of the physical and chemical properties of RBPI showed that the surface hydrophobicity, characteristic viscosity, and thermal stability of rice bran protein isolate were significantly affected by the pressure of saturated steam and pressure holding time. Under the conditions of 2.1 MPa and 210 s, the surface hydrophobicity index decreased significantly from 137.5 to 17.5, and the characteristic viscosity increased significantly. The peak temperature of denaturation decreases from 114.2 to 106.7 °C, and the enthalpy of denaturation decreases from 356.3 to 231.4 J/g. The higher structure (circular dichroic spectrum and endogenous fluorescence spectrum) of rice bran protein isolate was analyzed by volume rejection chromatography (SEC). The results showed that steam flash treatment could depolymerize and aggregate RBPI, and the relative molecular weight distribution changed greatly. The decrease in small molecules with poor solubility was accompanied by the increase in macromolecules (>550 kDa) soluble aggregates, which were the products of a Maillard reaction. The contents of free sulfhydryl and disulfide bonds in high-temperature rice bran meal protein isolate were significantly increased, which resulted in the increase in soluble aggregates containing disulfide bonds. Circular dichroism (CD) analysis showed that the α-helix content of the isolated protein was significantly decreased, the random curl content was increased, and the secondary structure of the isolated protein changed from order to disorder. The results of endogenous fluorescence spectroscopy showed that the high-temperature rice bran meal protein isolate was more extended, tryptophan was in a more hydrophilic microenvironment, the fluorescence intensity was reduced, and the tertiary structure was changed. In addition, the mean particle size and net surface charge of protein isolate increased in the aqueous solution, which was conducive to the development of the functional properties of the protein.

A novel strategy for preparation of rice bran protein oleogels based on high internal phase emulsion template.

BACKGROUND: Oleogels have been extensively explored as fat substitutes with no trans fatty acids and low saturated fatty acids in recent years as a result of increased health problems found to be related to the intake of trans and saturated fatty acids. RESULTS: Herein, high internal phase emulsion (HIPE) stabilized by rice bran protein (RBP) was prepared and further utilized as a template for preparation of RBP oleogels. RBP HIPE with the strongest rheological properties was obtained at pH 5.0 as a result of appropriate structural deformation, surface charge and a high three-phase contact angle at this pH. However, RBP oleogels prepared at pH 9.0 exhibited the highest yield stress after drying process. At this pH, RBP showed higher resistance to deformation caused by water evaporation. This highlighted the importance of structural stability of protein network on rheological properties of the resultant oleogels. Furthermore, with an increase in drying temperature, RBP oleogels exhibited higher yield stress and gel strength because water was better removed as a result of an enhanced capability to overcome the capillary pressure of emulsion. CONCLUSION: The present study further revealed the structure-activity relationship between protein, HIPE and oleogel, and also provided theoretical support for the development of protein-based oleogel. © 2023 Society of Chemical Industry.

Pyrazine yield and functional properties of rice bran protein hydrolysate formed by the Maillard reaction at varying pH.

Interest in plant-based protein sources has grown rapidly. Rice bran contains excellent quality protein, but it is still rare in the market, due to its poor functional properties and undesirable odors. Therefore, we studied the Maillard reaction at different pHs on the formation of pyrazines and improved functional properties of rice bran protein hydrolysate. Protein from rice bran was extracted and hydrolyzed, using alcalase, at 55 °C for 4 h. Fructose was added, and the pH of the hydrolysate was adjusted to pHs between 7.0 and 10.0, before spray drying. Five pyrazines were detected in the hydrolysate powder, with the highest yield at pH 9 ( p < 0.05). The highest odor active value came from 2-ethyl-3,5-dimethylpyrazine (26.26), which contributed coffee, nutty and caramel aromas, followed by 2,5-dimethylpyrazine (9.2) and 2-ethyl-5-methylpyrazine (5.0). Increased pH led to a darker color (L* = 58.5) and redder (a* = 11.7) and yellower (b* = 13.8) powder. Key functional properties-solubility, water and oil binding capacity and emulsion stability index and foaming capacity-were increased with pH ( p < 0.05). The optimum pH for pyrazine formation and improved properties of enzymatic rice bran protein hydrolysate was pH 9.0.

Effect of protein aggregates on properties and structure of rice bran protein-based film at different pH.

Rice bran protein (RBP) aggregates were prepared by heating of RBP solution at 90 °C for 4 h at pH 2, 7, or 11 and used for preparing of packaging films. The structure and properties of RBP aggregates and RBP-based films were characterized with sodium dodecyl sulfate-polyacrylamide gel electrophoresis, transmission electron microscopy, scanning electron microscope, differential scanning calorimetry, Fourier transform infrared spectroscopy and circular dichroism. The results showed formation of fibrillar, globular, and large molecular protein aggregates during the heating at pH 2, 7 and 11. The heat-aggregated RBP-based films exhibited lower opacity, moisture content, water solubility, and water vapor permeability than those of untreated RBP-based films. Also, improved mechanical and thermal properties were found for the heat-aggregated RBP-based films. In addition, the heat-aggregated RBP-based film at pH 11 showed homogenous and smooth surface as well as compact appearance compared with the untreated RBP-based films or heat-aggregated RBP-based film at pH 2 or 7. Furthermore, the secondary structure of heat-aggregated RBP film exhibited an increase in ß-sheet content and molecular interactions through non-covalent bonds. The obtained results indicated that formation of protein aggregates could improve physical, mechanical, and thermal properties of RBP-based film, especially at pH 11.

Rice bran protein hydrolysates reduce arterial stiffening, vascular remodeling and oxidative stress in rats fed a high-carbohydrate and high-fat diet.

PURPOSE: Rice bran protein hydrolysates (RBPH) contain highly nutritional proteins and antioxidant compounds which show benefits against metabolic syndrome (MetS). Increased arterial stiffness and the components of MetS have been shown to be associated with an increased risk of cardiovascular disease. This study aimed to investigate whether RBPH could alleviate the metabolic disorders, arterial stiffening, vascular remodeling, and oxidative stress in rats fed a high-carbohydrate and high-fat (HCHF) diet. METHODS: Male Sprague-Dawley rats were fed either a standard chow and tap water or a HCHF diet and 15 % fructose solution for 16 weeks. HCHF rats were treated orally with RBPH (250 or 500 mg/kg/day) for the final 6 weeks of the experimental period. RESULTS: Rats fed with HCHF diet had hyperglycemia, insulin resistance, dyslipidemia, hypertension, increased aortic pulse wave velocity, aortic wall hypertrophy and vascular remodeling with increased MMP-2 and MMP-9 expression. RBPH supplementation significantly alleviated these alterations (P < 0.05). Moreover, RBPH reduced the levels of angiotensin-converting enzyme (ACE) and tumor necrosis factor-alpha in plasma. Oxidative stress was also alleviated after RBPH treatment by decreasing plasma malondialdehyde, reducing superoxide production and suppressing p47phox NADPH oxidase expression in the vascular tissues of HCHF rats. RBPH increased plasma nitrate/nitrite level and up-regulated eNOS expression in the aortas of HCHF-diet-fed rats, indicating that RBPH increased NO production. CONCLUSION: RBPH mitigate the deleterious effects of HCHF through potential mechanisms involving enhanced NO bioavailability, anti-ACE, anti-inflammatory and antioxidant properties. RBPH could be used as dietary supplements to minimize oxidative stress and vascular alterations triggered by MetS.

Preparation, aroma characteristics and volatile compounds of flavorings from enzymatic hydrolyzed rice bran protein concentrate.

BACKGROUND: Rice bran is a by-product obtained from the rice milling industry. The aims of this research were to add value to rice bran by preparation of enzymatic hydrolyzed rice bran protein concentrate (HRPC) as a flavoring agent and the flavoring which was produced by HRPC has not been investigated. Different drying methods (freeze-drying and spray-drying) and fructose additions were studied for improvement of rice bran protein sensorial aroma characteristics. RESULTS: The most abundant amino acids in liquid HRPC (LH) were glutamic acid, arginine, aspartic acid and leucine. The intensity of desirable aromas, such as cereal-like, nut-like, milk-powder-like, sweet, and cocoa-like aroma, were higher in spray-dried HRPC powder (SHP) than in LH and freeze-dried HRPC. Volatile compounds, such as aldehydes, pyrazines and ketones, were significantly increased in HRPC powders in which fructose was added before spray-drying (SHP-F). Higher amounts of 2-methylbutanal, 3-methylbutanal, phenylacetaldehyde, 2,5-dimethylpyrazine, vanillin, 2-acetylpyrrole and maltol were detected in SHP-F. Moreover, these compounds had high odor active values, which accounted for the cocoa-like, sweet, nut-like, and milk-powder-like characteristics of SHP-F. CONCLUSIONS: These findings could lead to the creation of desirable aroma characteristics of rice bran protein concentrate by different preparation methods. © 2018 Society of Chemical Industry.

Identification of the active protein in rice bran protein having an inhibitory activity of cholesterol micellar solubility.

In our previous study, rice bran protein (RBP) inhibited cholesterol micellar solubility in vitro and decreased serum cholesterol level in rats. In the present study, RBP was separated and purified by size-exclusion chromatography and reversed-phase chromatography. The active protein of RBP related to cholesterol micellar solubility was identified as lectin and non-specific lipid-transfer protein 1 using MALDI-TOF mass spectrometry analysis.

Rheology and microstructure of binary mixed gel of rice bran protein-whey: effect of heating rate and whey addition.

BACKGROUND: Rice bran protein (RBP) is a valuable plant protein which has unique nutritional and hypoallergenic properties. Whey proteins have wide applications in the food industry, such as in dairy, meat and bakery products. RESULTS: Whey protein concentrate (WPC), RBP and their mixtures at different ratios (1:1, 1:2, 1:5 and 1:10 w/w) were heated from 20 to 90 °C at different heating rates (0.5, 1, 5 and 10 °C min(-1) ). The storage modulus (G') and gelling point (Tgel ) of WPC were higher than those of RBP, indicating the good ability of WPC to develop stiffer networks. By increasing the proportion of WPC in mixed systems, G' was increased and Tgel was reduced. Nevertheless, the elasticity of all binary mixtures was lower than that of WPC alone. Tgel and the final G' of RBP-WPC blends were increased by raising the heating rate. The RBP-WPC mixtures developed more elastic gels than RBP alone at different heating rates. RBP had a fibrillar and lentil-like structure whose fibril assembly had smaller structures than those of WPC. CONCLUSION: The gelling structure of the mixed gel of WPC-RBP was improved by adding WPC. Indeed, by adding WPC, gels tended to show syneresis and had lower water-holding capacity. Furthermore, the gel structure was produced by adding WPC to the non-gelling RBP, which is compatible with whey and can be applied as a functional food for infants and/or adults. © 2015 Society of Chemical Industry.

Comparison the effect of three commercial enzymes for enzymatic hydrolysis of two substrates (rice bran protein concentrate and soy-been protein) with SDS-PAGE.

In this research enzymatic hydrolysis of rice bran protein concentrate (RBPC) and soybean Protein (SBP) as control were studied with 3 commercial enzymes (Alcalase®, Papain and acommercial 3-enzyme cocktail containing of 1.6 mg ml(-1) Trypsin, 3.1 mg ml(-1) Chymotrypsin, 1.3 mg ml(-1)Aminopeptidase (SIGMA P7500) and 7.95 mg ml(-1)pronase type XIV (SIGMA P5147) by the pH stat method. The hydrolysis was carried out at temperature of 28 C, 60 min and pH 8.00. Results were showed that RBPC, and SBP had higher Degree hydrolysis (DH %) with Alcalase® enzyme. Alcalase®had stronger capability for hydrolysis compared to the other tested enzymes. After 60 minute of hydrolysis time, the DH% of Alcalase® for RBPC and SBP was 12.69 and 12.50 %, respectively. In contrast, papain enzyme was showed lowest DH% in three substrates that 1.56 and 1.24 % were for SBP and RBPC, respectively.The hydrolysis of the protein fraction performed the three enzymes on the two substrates was followed in SDS-PAGE. RBPC and SBP showed almost complete digestion with Alcalase® enzyme after 60 minutes. 3-enzyme cocktail enzyme hydrolyzed better the RBPC than the SBP. Papain enzyme had less effect on the two substrates than other 2 enzymes. It was found that Alcalase® has highest capability for hydrolysis compared to other enzyme preparations. The high value protein hydrolysates prepared by Alcalase® can be used as value added ingredients in many food formulations. They are also suitable for a broad range of industrial food applications and also for cosmetic and personal care products.

Cholesterol-lowering effect of rice bran protein containing bile acid-binding proteins.

Dietary plant protein is well known to reduce serum cholesterol levels. Rice bran is a by-product of rice milling and is a good source of protein. The present study examined whether feeding rats a high-cholesterol diet containing 10% rice bran protein (RBP) for 10 d affected cholesterol metabolism. Rats fed dietary RBP had lower serum total cholesterol levels and increased excretion of fecal steroids, such as cholesterol and bile acids, than those fed dietary casein. In vitro assays showed that RBP strongly bound to taurocholate, and inhibited the micellar solubility of cholesterol, compared with casein. Moreover, the bile acid-binding proteins of the RBP were eluted by a chromatographic column conjugated with cholic acid, and one of them was identified as hypothetical protein OsJ_13801 (NCBI accession No. EAZ29742) using MALDI-TOF mass spectrometry analysis. These results suggest that the hypocholesterolemic action of the RBP may be caused by the bile acid-binding proteins.

Antioxidant activities of rice bran protein hydrolysates in bulk oil and oil-in-water emulsion.

BACKGROUND: Recently, utilization of natural antioxidants in food processing has been of growing interest, owing to the concerns of health hazards of synthetic agents. Protein hydrolysates are a potent candidate for this purpose. In this work, rice bran protein hydrolysates (RBPH) with various degrees of hydrolysis (DH) were prepared, and their antioxidant activities in soybean oil and oil-in-water (O/W) emulsion were examined. RESULTS: With increasing DH, RBPH showed increasing antioxidant activities, as evidenced by the increases in DPPH radical scavenging activity, reducing power and ferrous chelating activity (P < 0.05). The improved activity was associated with increasing surface hydrophobicity (SoANS). After hydrolysis for 60 min, the content of hydrophobic amino acids was increased. When RBPH with various DH were incorporated into bulk soybean oil and O/W emulsion stored at 37 °C for up to 15 days, lipid oxidation was successfully retarded, especially when DH increased. The efficiency in prevention of oxidation was dose dependent (0-10 g L(-1)), as indicated by the lower peroxide value and thiobarbituric reactive substances. CONCLUSION: The present work suggests that RBPH might be potently employed as a natural antioxidant in both bulk oil and emulsion models.

Sensory aroma characteristics of alcalase hydrolyzed rice bran protein concentrate as affected by spray drying and sugar addition.

The sensory aroma characteristics of alcalase hydrolyzed rice bran protein concentrate as affected by spray drying and sugar addition were investigated. Rice bran protein concentrate (RBPC) was hydrolyzed by alcalase. Sucrose, glucose or fructose was added to the liquid rice bran protein hydrolysate (LRBPH) and subsequently spray dried. The sensory aroma intensities of the hydrolysates were evaluated. Results showed that after spray drying, the rice bran protein concentrate powder (RBPC-P) had higher sweet and cocoa-like aroma intensities than RBPC (p ≤ 0.05) and hydrolyzed rice bran protein powder (HRBPP) had higher milk powder-like aroma intensities than LRBPH (p ≤ 0.05). The sweet, cocoa-like and milk powder-like aroma intensities in hydrolyzed rice bran protein powder with fructose addition (HRBPP-F) were significantly higher (p ≤ 0.05) than those of hydrolyzed rice bran protein powder with sucrose or glucose addition (HRBPP-S or HRBPP-G). HRBPP-F had the highest overall aroma liking score. These results also indicate that spray drying and sugar addition could improve the sensory aroma characteristics of alcalase hydrolyzed RBPC.

Preparation of Transglutaminase-Catalyzed Rice Bran Protein Emulsion Gels as a Curcumin Vehicle.

Protein-based emulsion gels have tunable viscoelasticity that can be applied to improve the stability of bioactive ingredients. As the by-product of rice processing, rice bran protein (RBP) has high nutritional value and good digestibility, exhibiting unique value in the development of hypoallergenic formula. In this study, the effect of transglutaminase (TGase) cross-linking on the physicochemical properties of RBP emulsion gels was investigated. To improve the stability of curcumin against environmental stress, the entrapment efficiency and stability of curcumin in the emulsion gel systems were also evaluated. The results indicated that TGase increased the viscoelastic modulus of RBP emulsion gels, resulting in a solid-like structure. Moreover, the entrapment efficiency of curcumin was increased to 93.73% after adding TGase. The thermal stability and photo-stability of curcumin were enhanced to 79.54% and 85.87%, respectively, compared with the sample without TGase addition. The FTIR results showed that TGase induced the cross-linking of protein molecules and the secondary structure change in RBP. Additionally, SEM observation confirmed that the incorporation of TGase promoted the formation of a compact network structure. This study demonstrated the potential of RBP emulsion gels in protecting curcumin and might provide an alternative strategy to stabilize functional ingredients.

Self-assembly embedding of curcumin by alkylated rice bran protein.

Lysine-rich rice bran protein (RBP) can be used as raw material for alkylation modification to improve the self-assembly performance of protein. The results of 1H NMR, degree of alkylation, and DSC analysis showed that the alkyl chain was successfully attached to the RBP. The surface hydrophobicity and absolute ζ-potential increased. The three-dimensional structure of the alkylated RBP (ARBP) become more porous and ARBP-2 was selected as the material for embedding curcumin. The XRD results revealed that curcumin induced self-aggregation of ARBP-2 and the inclusion of curcumin was attained. The maximum encapsulation efficiency of curcumin was 82.67 % and the maximum loading amount was 171.37 g/100 g RBP. The results of atomic force microscopy (AFM), particle size, and polydispersity index (PDI) analyses revealed that the particles in the system were aggregated after curcumin was added. Curcumin was well protected by encapsulation in the self-assembled particles. Thus, this study provides a new strategy for the embedding and delivery of curcumin.

Effect of Rice Bran Protein on the Foaming Properties and Foaming Characteristics of Rice Bran Protein-Sodium Caseinate and Rice Bran Protein Nanoparticles-Sodium Caseinate.

Rice bran, a byproduct of rice milling, comprises 12-14% protein. The foaming properties and associated mechanisms of the composite rice bran protein system were not well studied. In this study, a composite protein system composed of rice bran protein (RBP)-sodium caseinate (NaCas) and rice bran protein nanoparticles (RBPNs)-sodium caseinate (NaCas) was investigated. The results showed that the synergistic effect of RBP and NaCas increased the foaming stability of the composite solution up to 83.77 ± 2.75%. Moreover, the foaming capacity and foaming stability of the RBPNs-NaCas composite solution were up to 177.50 ± 3.53% and 80.28 ± 0.39%, respectively. The physicochemical properties results revealed that the particle size volume peaks of RBP-NaCas and RBPNs-NaCas were mainly concentrated at 55.7 nm and 197.1 nm, and RBPNs-NaCas showed a wider single peak particle size distribution. The ζ-potential values of RBP-NaCas and RBPNs-NaCas were changed to -35.5 ± 0.07 mV and -27.2 ± 0.28 mV after complexation. The apparent viscosity and consistency factor of RBP-NaCas decreased by 31.1% compared to RBP, while RBPNs-NaCas displayed similar parameters to the single proteins. The interfacial rheological test showed that RBP and RBPNs can significantly improve the interfacial properties of NaCas by enhancing the interfacial interaction and the interfacial viscoelastic modulus of composite proteins, which is conducive to the stability of the foam system. The outcome of the study provided a theoretical basis for RBP and RBPNs to partially replace NaCas in the processing of foamed food.

The synergistic effects of rice bran rancidity and dephenolization on digestive properties of rice bran protein.

Both rice bran (RB) rancidity and dephenolization could affect the structural characteristics and phenolics composition of rice bran protein (RBP), thereby affecting RBP digestibility. The synergistic effects of RB rancidity and dephenolization on RBP digestibility were investigated. Excessive RB rancidity (RB stored for 10 d) and non-dephenolization reduced RBP digestibility, while moderate RB rancidity (RB stored for 1 d) combined with dephenolization improved RBP digestibility to a maximum of 74.19%. Dephenolization reduced the antioxidant capacities of RBP digestive products. The digestibility of non-dephenolized RBP (NDRBP) was significantly (P < 0.05) related with its carbonyl content, surface hydrophobicity, and ζ-potential. The digestibility of dephenolized RBP (DRBP) was significantly related with its ß-sheet structure content, surface hydrophobicity, ζ-potential, and average particle size. Overall, moderate RB rancidity combined with dephenolization enhanced RBP digestibility by reducing the non-competitive inhibition of endogenous phenolics on protease and regulating the spatial structural characteristics of RBP.

Effect of ultrasonic pretreatment on the emulsion rheological properties and interface protein structure of epigallocatechin-3-gallate and rice bran protein complex.

The effect of ultrasonic pretreatment on the emulsion rheological properties and the structural characteristics of interface-adsorbed protein (IAP) and interface-unabsorbed protein (IUP) of rice bran protein and epigallocatechin-3-gallate complex (RBP-EGCG) were studied. Compared to RBP-EGCG without ultrasonic pretreatment, appropriate ultrasonic pretreatment (ultrasonic power was 425 W) enhanced the IAP trypsin sensitivity (from 3.20 to 3.73), increased the IUP surface hydrophobicity (from 12.59 to 20.87), and decreased the ζ-potential (from -24.93 mV to -36.88 mV) and particle size (from 567.30 nm to 273.13 nm) of IUP, thereby increasing the viscosity and viscoelasticity of emulsion. Compared to appropriate ultrasonic pretreatment, high-power ultrasonic pretreatment (ultrasonic power was 500 W) attenuated the IAP trypsin sensitivity, and increased the ζ-potential and particle size of IUP, thereby decreasing the viscosity and viscoelasticity of emulsion. Overall, ultrasonic pretreatment changed the EGCG-RBP emulsion viscoelasticity by regulating spatial structural characteristics and flexibility of interface protein.

Protein oxidation affected the encapsulation properties of rice bran protein fibril-high internal phase pickering emulsions: Enhanced stability and bioaccessibility of ß-carotene.

Rice bran protein fibril (RBPF)-high internal phase Pickering emulsions (HIPPEs) loaded with ß-carotene (CE) were constructed to enhance stability and bioavailability of CE. Rice bran (RB) protein with varying oxidation degrees was extracted from RB with varying storage period (0-10 days) to prepare RBPF by acid-heating (90 °C, 2-12 h) to stabilize HIPPEs. The influence of protein oxidation on the encapsulation properties of RBPF-HIPPEs was studied. The results showed that CE-HIPPEs could be stably stored for 56 days at 25 °C. When RB storage time was the same, the average particle size, lipid hydroperoxide content, and malondialdehyde content of CE-HIPPEs and the CE degradation rate initially fell, and then grew as the acid-heating time prolonged, while the ζ-potential value, viscosity, viscoelasticity, free fatty acid (FFA) release rate, and bioaccessibility first rose, and subsequently fell. When acid-heating time of RBPF was the same, the average particle size, lipid hydroperoxide content, and malondialdehyde content of CE-HIPPEs initially fell, and subsequently increased with RB storage time extended, while the ζ-potential value, viscosity, viscoelasticity, FFA release rate, and bioaccessibility initially increased, and then decreased. Overall, Moderate oxidation and moderate acid-heating enhanced the stability as well as rheological properties of CE-HIPPEs, thus improving the stability and bioaccessibility of CE. This study offered a new insight into the delivery of bioactive substances by protein fibril aggregates-based HIPPEs.

Effects of rice bran rancidity on the interfacial adsorption properties of rice bran protein fibril aggregates and stability of high internal phase Pickering emulsions.

The effects of rice bran rancidity-induced protein oxidation and heating time on the stability of rice bran protein fibril aggregates (RBPFA)-high internal phase Pickering emulsions (HIPPEs) were investigated. The optimal conditions for RBPFA-HIPPEs were 8 mg/mL RBPFA with an oil phase volume fraction of 75 %. Moderate oxidation (rice bran stored for 3 d) and moderate heating (8 h) enhanced the wettability, flexibility, diffusion rate, and adsorption rate of RBPFA, meanwhile, the rheological properties of RBPFA-HIPPEs increased. RBPFA-HIPPEs could be stably stored for 50 d at 25 °C. Moderate oxidized and moderate heated RBPFA-stabilized HIPPEs could remain stable after heat treatment and could be re-prepared after freeze-thaw (3 cycles). Additionally, the stability of RBPFA-HIPPEs was significantly related to the structural characteristics and interfacial properties of RBPFA. Overall, moderate oxidation and moderate heating enhanced the storage, thermal, and freeze-thaw stability of RBPFA-HIPPEs by improving the interfacial properties of RBPFA.

Effect of epigallocatechin-3-gallate modification on the structure and emulsion stability of rice bran protein in the presence of soybean protein isolate.

For improving the emulsion stability of rice bran protein (RBP), RBP was modified by different concentrations of epigallocatechin-3-gallate (EGCG) in the presence of soybean protein isolate (SPI), and RBP-EGCG-SPI conjugate was prepared by alkaline pH-shifting. The results showed that the addition of EGCG led to an increase in the bound phenol content and the flexibility of the secondary structure, a decrease in the free sulfhydryl and disulfide bond content of the RBP-EGCG-SPI conjugate. EGCG covalently bound to RBP and SPI through non-disulfide bonds. When the concentration of EGCG was 10 % (w/v), the emulsifying activity index and emulsion stability index of conjugate reached the maximum value (36.61 m2/g and 255.61 min, respectively), and the conjugate had the best emulsion stability. However, an EGCG concentration above 10 % (w/v) negatively affected the emulsion stability, with increasing particle size due to protein aggregation. Summarily, the modification of EGCG improved the emulsion stability of conjugate by regulating the spatial structure of RBP-EGCG-SPI conjugate. The work provided an important guide to further improve the emulsion stability of RBP.