Physical stability and microstructure of rapeseed protein isolate/gum Arabic stabilized emulsions at alkaline pH

Li, Qun; Wang, Zhigao; Dai, Caixia; Wang, Yujiao; Chen, Wenye; Ju, Xingrong; Yuan, Jiugang; He, Rong

doi:10.1016/j.foodhyd.2018.09.020

Cited by 96 publications

(43 citation statements)

References 35 publications

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“…3, in the pH range 4.0-10.0, RPI solubility first decreased and then increased, with a maximum solubility (47.58%) at pH 10.0 and a minimum solubility (12.70%) at pH 7.0; hence, RPI exhibits better solubility in alkaline environments than in acid environments. Interestingly, the poorest solubility of RPI was found at pH 7.0, which is inconsistent with a previous report that the lowest solubility was found at the isoelectric point of RPI (pH 4.5); 5 moreover, in previous studies, it was discovered that RPI has two pIs (4.57 and 7.00), 19 and Radwan and Lu even found that RPI had poor solubility at four points (4.5, 4.8, 7.0, and 7.2). 24 These studies indicated that RPI has two or more isoelectric points, which could be attributed to the difference of rapeseed varieties and methods used to extract proteins.…”

Section: Protein Solubility Of Rpicontrasting

confidence: 86%

“…Characterization of the emulsion stabilized by RPI Droplet size distribution and zeta potential of RPI emulsion The measurement of the average droplet size, polydispersity index, and zeta potential of the emulsion was carried out as described previously using a Zetasizer (NanoZS90; Malvern Instruments Ltd, Worcestershire, UK) with an He-Ne laser (633 nm) at a fixed scattering angle of 90°and temperature of 25 ± 0.1°C. 19 The refractive indexes used were 1.47 for rapeseed oil and 1.33 for water. The emulsion was diluted 100-fold with deionized water before analysis to avoid multiple scattering effects.…”

Section: Preparation Of Oil-in-water Nanoemulsion Stabilized By Rpimentioning

confidence: 99%

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Characterization and analysis of an oil‐in‐water emulsion stabilized by rapeseed protein isolate under pH and ionic stress

et al. 2020

J Sci Food Agric

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BACKGROUND Presently, identifying natural compounds as emulsifiers is a popular topic in the food industry. Rapeseed protein isolate (RPI) is a natural plant protein with excellent emulsifying properties, but it has not been systematically developed and utilized. RESULTS This study investigated the surface hydrophobicity, wettability, and protein solubility of RPI to further explain its emulsifying behavior in emulsion systems. Nanoemulsions stabilized by RPI at varying protein concentration, pH, and ionic strength were prepared. The size distribution, zeta potential, flocculation index, creaming index, microstructure, rheology, and protein secondary structure of emulsions were measured. The emulsion stabilized by 20 g L−1 RPI at pH 10.0, 200 mmol L−1 ionic strength revealed an appropriate droplet size of 555 nm and the most internal gel strength without creaming phenomenon. Circular dichroism spectroscopy showed a positive correlation between emulsion stability and α‐helix ratio, indicating the environment factors affected emulsion stability by acting on its hydrogen bonds. CONCLUSIONS This study demonstrates that RPI is a practical emulsifier for stabilizing nanoemulsions. About 20 g L−1 RPI can stabilize 100 mL L−1 oil in water; stable emulsions can be formed at most pH conditions (except 7.0); ion addition will aggravate the emulsion flocculation, but also increase the internal gel strength. © 2020 Society of Chemical Industry

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Section: Protein Solubility Of Rpicontrasting

confidence: 86%

Section: Preparation Of Oil-in-water Nanoemulsion Stabilized By Rpimentioning

confidence: 99%

Characterization and analysis of an oil‐in‐water emulsion stabilized by rapeseed protein isolate under pH and ionic stress

et al. 2020

J Sci Food Agric

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“…FTIR spectroscopy is a vibrational spectroscopic technique that can be used to optically probe the molecular structure and functional groups in biomaterials. Among nine characteristic absorption bands in the infrared spectra of protein and polypeptide, amide I (1700–1600 cm −1 ), amide II (1550–1500 cm −1 ), and amide III (1300–1200 cm −1 ) bands are the major ones and are sensitive toward their conformation (Li et al, ). The FTIR spectra of RPI, 5% SRPI, 10% SRPI, and 15% SRPI films within the wavenumber range of 1000–4000 cm −1 are shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Effects of Succinylation on the Physicochemical Properties and Structural Characteristics of Edible Rapeseed Protein Isolate Films

Dai

et al. 2019

J Americ Oil Chem Soc

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This study described the manufacture and characterization of different levels of succinic anhydride (0-15%, w/w) on rapeseed protein isolate (RPI) films. Mechanical, barrier, optical, surface, microstructure, and thermal properties were investigated. Results showed that 5% succinylated rapeseed protein isolate (SRPI) film revealed the overall optimal properties. The mechanical and barrier properties of 5% SRPI film were enhanced significantly compared to the RPI film. The water vapor permeability values of RPI and 5% SRPI films were 0.77 and 0.32 g mm/[hour m 2 kPa], respectively. Succinylation improved the color of RPI. The contact angle of 5% SRPI film was 108.68 and was the most hydrophobic combination. Moreover, scanning electron microscopy images revealed that 5% SRPI showed a dense, homogenous, and smooth microstructure. Thermogravimetric analysis results verified a low level of succinylation strengthened the thermal resistance of SRPI films. The content of β-sheet was almost half of all secondary structures after succinylation, which was supported by analyses of Fourier transform infrared spectroscopy. Results demonstrated that succinylation could be employed to improve the properties of rapeseed protein and SRPI films have great potential to be used as edible films.

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“…Typically, the polysaccharide concentration has to be optimized to provide a sufficiently strong steric and electrostatic repulsion between the oil droplets, without promoting bridging or depletion flocculation (Xu, Luo, Liu, & McClements, 2017). If the polysaccharide concentration is too low, then bridging flocculation can occur, whereas if it is too high, then depletion flocculation can occur (Huang et al., 2019; Li et al., 2019). After the droplets flocculate, they may undergo coalescence because they are in contact for extended periods.…”

Section: Mixed Layer Interfaces Prepared By Direct Mixing Methodsmentioning

confidence: 99%

Design principles of oil‐in‐water emulsions with functionalized interfaces: Mixed, multilayer, and covalent complex structures

McClements

Liu

et al. 2020

Comp Rev Food Sci Food Safe

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Proteins and polysaccharides are widely used as ingredients in food emulsions due to their high biocompatibility, good biodegradability, and a broad range of techno-functionalities. In particular, they are used as emulsifiers, texture modifiers, and stabilizers in many emulsion-based foods. Moreover, the functionality of these biopolymers can be extended by forming protein-polysaccharide complexes that can be used to modulate the characteristics of the oil-water interface, thereby altering the stability and performance of food emulsions. This review highlights a number of approaches to modulate the interfacial properties of oil-in-water emulsions based on the utilization of protein-polysaccharide complexes: direct mixing, layer-by-layer assembly, and conjugation. Besides, the impact of altering the interfacial properties on emulsion performance is highlighted, including their formation, stability, and functional attributes. Interfacial engineering approaches can be used to tailor the properties of food emulsions to particular applications. For instance, they can be used to create emulsionbased delivery systems for bioactive agents, such as vitamins, nutraceuticals, antimicrobials, colors, flavors, and antioxidants. Moreover, they can be used to create emulsion-based foods with lower calorie contents and enhanced satiety responses. Nevertheless, it is important to account for various factors when developing successful interfacial engineering technologies, including safety concerns, production costs, environmental impact, sustainability, government regulations, and labeling issues.

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Physical stability and microstructure of rapeseed protein isolate/gum Arabic stabilized emulsions at alkaline pH

Cited by 96 publications

References 35 publications

Characterization and analysis of an oil‐in‐water emulsion stabilized by rapeseed protein isolate under pH and ionic stress

Characterization and analysis of an oil‐in‐water emulsion stabilized by rapeseed protein isolate under pH and ionic stress

Effects of Succinylation on the Physicochemical Properties and Structural Characteristics of Edible Rapeseed Protein Isolate Films

Design principles of oil‐in‐water emulsions with functionalized interfaces: Mixed, multilayer, and covalent complex structures

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