Rice proteins - Gum arabic coacervates: Effect of pH and polysaccharide concentration in oil-in-water emulsion stability.

In the context of replacing animal proteins in food matrices, rice proteins (RP) become promised because they come from an abundant plant source, are hypoallergenic, and have high digestibility and nutritional value. However, commercial protein isolates obtained by spray drying have low solubility and poor functionality, especially in their isoelectric point. One way to modify these properties is through interaction with polysaccharides, such as gum arabic (GA). Therefore, this work aims to evaluate the effects of pH and GA concentration on the interaction and emulsifying activity of RP:GA coacervates. First, the effects of pH (2.5 to 7.0) and GA concentrations (0.2 to 1.0 wt%, giving rise to RP:GA mass ratios of 1:0.2 to 1:1.0) in RP:GA blends were evaluated. The results demonstrated that biopolymers present opposite net charges at pH between 2.5 and 4.0. At pH 3.0, insoluble coacervates with complete charge neutralization were formed by electrostatic interactions, while at pH 5.0 it was observed that the presence of GA prevented the RP massive aggregation. Second, selected blends with 0.4 or 1.0 wt% of GA (RP:GA mass ratios of 1:0.4 or 1:1.0) at pH 3.0 or 5.0 were tested for their ability to stabilize oil-in-water emulsions. The emulsions were characterized for 21 days. It was observed that the GA increased the stability of RP emulsions, regardless of the pH and polysaccharide concentration. Taken together, our results show that it is possible to combine RP and GA to improve the emulsifying properties of these plant proteins at pH conditions close to their isoelectric point, expanding the possibility of implementation in food systems.

Optimization of emulsification conditions with rice bran concentrates for the preliminary formulation of potential vegan dressings and their characterization.

A fraction of rice bran (RB), generated during the brown rice polishing, is utilized to extract oil, resulting in defatted RB (DRB). The aim of this study was to optimize the emulsification conditions to enhance the value of this byproduct by formulating potential vegan dressings and characterizing them. Enzymatic hydrolysis of the starch present in DRB yields the DRB concentrate (DRBC). A central composite design was applied and the results were analyzed using response surface methodology to select optimal conditions for an oil-in-water emulsion formula. Two formulations were chosen: one corresponds to the optimal conditions, with 26.5% of oil and 73.5% of DRBC dispersion (eoptimal), and the other one with 21.7% of oil and 78.3% of dispersion (eED8). The eoptimal formulation exhibited significantly lower mean De Brouckere diameter (D4,3) value and higher viscosity when compared with eED8. For both emulsions, the particle size distribution and D4,3 remained unchanged during storage, whereas viscosity decreased, and backscattering (BS) increased. Initially, both emulsions exhibited solid viscoelastic behavior, which was partially lost during quiescent storage. The increase in BS was attributed to particle disaggregation, ultimately leading to the aforementioned change in rheological behavior. In conclusion, although the designed emulsions underwent microstructural changes, they were stable against gravitational separation. To improve stability during quiescent storage, it is suggested to incorporate a thickening agent. Hence, it is propose to procced with the development of a vegan dressing based on the eoptimal emulsion, as it exhibits superior physicochemical properties.

Acid emulsions stabilized by soy whey concentrates and soluble soybean polysaccharides: Role of biopolymer interaction strategies on stability against environmental stresses.

This article focuses on the evaluation of different interaction strategies between soy whey concentrates (SWC) and soluble soybean polysaccharides (SSPS) at pH 3.0 on the emulsion stability against freeze-thawing and mechanical stirring. Emulsions were prepared from aqueous dispersions of both biopolymers (3.0% w/w SSPS and SWC, 1:1 mass ratio) and sunflower oil (10% w/w) by aqueous phase complexation (APC), interfacial complexation (IC) and interfacial complexation and sonication (ICS). SWC control emulsion was a poor emulsifying ability; SSPS addition, through the APC and ICS strategies, noticeably improved the SWC emulsifying properties. ICS emulsions showed the highest stability to environmental stresses, due a combination of low initial particle size, flocculation degree and steric hindrance promoted by the presence of SSPS chains at the interface. This study provides valuable information forthe utilization of whey soy proteins in acid dispersed systems stable to environmental stresses.

Impact of environmental stresses on the stability of acidic oil-in-water emulsions prepared with tofu whey concentrates.

The emulsifying properties of tofu-whey concentrates (TWCs) at pH 3.0, 4.0, and 5.0, and the stability of the resultant oil-in-water emulsions against freeze-thawing (24 h, -20 °C) and controlled or mechanical stress (orbital stirring at 275 rpm, 40 min) were addressed. TWCs were prepared from tofu-whey by heating at 50 °C (8.0 kPa) or 80 °C (24.0 kPa), dialysis (4 °C, 48 h), and freeze-drying, giving the samples TWC50 and TWC80, respectively. The particle size and interfacial properties at the oil/water interface were measured. Emulsions were prepared by mixing the TWC aqueous dispersions (1.0% protein w/w) and refined sunflower oil (25.0% w/w) by high-speed and ultrasound homogenization. The preparation of TWCs at higher temperatures (80 °C) promoted the formation of species of larger particle size, a slight decrease of interfacial activity, and the adsorption of more rigid biopolymer structures associated with an increase of film viscoelasticity in interfacial rheology measurements. The emulsifying properties of both concentrates were enhanced with decreasing pH (5.0-3.0), through a significant decrease of particle size (D4,3) and flocculation degree (FD), but only those prepared with TWC80 exhibited higher stability to freeze-thawing and mechanical stress at pH 3.0. This could be ascribed to a combination of low initial D4,3 and FD values, high protein load, and the presence of rigid species that impart high viscoelasticity to the oil/water interface. These results would be of great importance for the utilization of TWCs as food emulsifiers in acidic systems to impart high stability to environmental stresses.

Influence of chemical composition and structural properties on the surface behavior and foam properties of tofu-whey concentrates in acid medium.

This article focuses on the impact of chemical composition and structural properties of tofu-whey concentrates on their surface behavior at the air/water interface and foaming properties in acid medium. Liquid tofu-whey (pH 5.6 ±â€¯0.1) was concentrated at three combinations of temperature and pressure (50 °C-8.0 kPa, 65 °C-16.0 kPa and 80 °C-24.0 kPa), with further dialysis (4 °C, 48 h) and freeze-drying, giving the samples TWC50, TWC65 and TWC80, respectively. The increase of temperature during the concentration step promoted the enrichment of the concentrates in crude protein and calcium, without appreciable changes in the yield, the carbohydrate content and the polypeptide composition. For TWC80, the increase the degree of glycosylation and the intensity of the hydrophobic effect promoted the decrease of molecular flexibility and the formation of compact aggregates mediated by disulfide bridges as was evidenced by tricine-SDS-PAGE, TGA and FTIR assays. These structural differences have a pronounced impact of the pH-dependence of turbidity and solubility of protein and polysaccharides. At pH 4.0 all concentrates evidenced a ζ-potential close to zero, which enhanced their foam ability (overrun >1500%). Nevertheless, at this pH, TWC80 showed both the highest carbohydrate-to-protein mass ratio in the soluble fraction (>1.8) and foam stability (FS). Thus, the improvement of FS at pH 4.0 would be associated to the effective adsorption of compact rich-in-protein aggregates at the air/water interface and the higher content of soluble polysaccharides in the bulk phase. These findings are relevant for the application of tofu-whey concentrates in acidic dispersed systems, such as foams and aerated food emulsions.

Emulsifying properties of defatted rice bran concentrates enriched in fiber and proteins.

BACKGROUND: Rice bran (RB), a by-product of the rice milling industry, constitutes around 10% of the total weight of rough rice. The interest in the use of RB is centered on its nutritional quality, its low cost, and its extensive worldwide production. As RB is commonly used for oil extraction, the defatted rice bran (DRB) is obtained as a second by-product. The aim of this work was to obtain a defatted rice bran concentrate (DRBC), enriched in protein and fiber, from defatted rice bran flour (DRBF) and to determine its physicochemical and emulsifying properties. RESULTS: To obtain the DRBC, the starch was efficiently hydrolyzed (> 98%) with α-amylase and amyloglucosidase, with a concomitant increase in the proportions of crude protein (from 154.7 to 274.3 g kg-1 ) and total dietary fiber (from 276.1 to 492.3 g kg-1 ). Defatted rice bran concentrate exhibited a loss of protein solubility and increased surface hydrophobicity compared with DRBF. Defatted rice-bran concentrate dispersions with and without previous ultrasound treatment were prepared. The sonication led to an increase in the apparent viscosity. Emulsions were prepared with dispersions with and without previous ultrasound treatment and showed high stability in quiescent conditions over 28 days. However, the emulsions prepared with dispersions treated with ultrasound resulted in lower D4,3 values and higher elastic and viscous moduli. CONCLUSION: The rice bran concentrate can be used to obtain stable oil-in-water (O/W) emulsions, including both soluble and insoluble fractions, in acidic and neutral conditions. These innovative findings thus contribute to increasing the added value of this important by-product of the rice-milling industry. © 2019 Society of Chemical Industry.

Effect of water content on thermal behavior of freeze-dried soy whey and their isolated proteins.

Thermal behavior of lyophilized soy whey (LSW) and whey soy proteins (WSP) at different water contents (WC) was studied by DSC. In anhydrous condition, Kunitz trypsin inhibitor (KTI) and lectin (L) were more heat stable for WSP with respect to LSW sample. The increase of WC destabilized both proteins but differently depending on the sample analyzed. Thermal stability inversion of KTI and L was observed for WSP and LSW at 50.0% and 17.0% WC, respectively, which correspond to the same water-protein content mass ratio (W/P ≈ 1.9). At W/P < 1.9, KTI was more heat stable than L. Before the inversion point, WC strongly modified the peak temperatures (T(p)) of KTI and L for WSP, whereas this behavior was not observed for LSW. The high sugar content was responsible for the thermal behavior of KTI and L in LSW under anhydrous condition and low WC. These results have important implications for the soy whey processing and inactivation of antinutritional factors.

Thermal behavior of soy protein fractions depending on their preparation methods, individual interactions, and storage conditions.

Different soy protein isolates (SPI) and whey soy protein (WSP) samples were obtained from fresh and stored soybean flour. Some samples were subjected to a long, cold storage. DSC thermograms of SPI showed the two characteristic endotherms, corresponding to denaturation of ß-conglycinin and glycinin. Low value of denaturation enthalpy and high glycinin denaturation temperature were related to a reduction of protein solubility of SPI. DSC thermograms of WSP also showed two characteristic endotherms, corresponding to Kunitz trypsin inhibitor and lectin. The methods and conditions of preparation and storage of WSP samples were factors that modified their thermal behavior. Some SPI-WSP mixtures (1:1) exhibited more complex thermograms and higher denaturation temperatures. Thermograms of SPI-denatured WSP mixtures showed that the thermal stabilization of soybean storage proteins was attributed to protein-protein interactions. The differences in the thermal behavior of single or mixed SPI and WSP could not be explained on the basis of mineral content.