Effects of heat treatment on the emulsifying properties of pea proteins

Peng, Wenqin; Kong, Xiangzhen; Chen, Yeming; Zhang, Caimeng; Yang, Yumin; Hua, Yufei

doi:10.1016/j.foodhyd.2015.06.025

Cited by 273 publications

(143 citation statements)

References 35 publications

Supporting

Mentioning

121

Contrasting

Unclassified

Order By: Relevance

“…Ye () reported that the stability of emulsions was dependent mainly on the interfacial protein concentration and droplet size. The above results have demonstrated that the emulsion prepared at 20% power for 20 min has good interfacial protein concentration, zeta potential, and droplet size, and these findings were in agreement with previous researches (Peng et al, ; Sui et al, ).…”

Section: Resultssupporting

confidence: 93%

“…This might be because high-power ultrasound resulted in partial protein denaturation, which was adverse for emulsifying capacity of protein. The clusters of oil droplets would produce large flocculated particles (Peng et al, 2016), and these observations were well in agreement with the abovementioned results.…”

Section: Particle Size Distributionsupporting

confidence: 90%

“…This phenomenon was in accordance with above discussions of particle size distribution. The study of Peng et al () also observed that smaller oil droplets could also be obtained as increasing interfacial protein concentration of the pea protein‐stabilized emulsion.…”

Section: Resultsmentioning

confidence: 88%

See 2 more Smart Citations

Preparation and characterization of rice bran protein‐stabilized emulsion by using ultrasound homogenization

Sun

Chen

et al. 2019

Cereal Chem

View full text Add to dashboard Cite

Background and objectives The ultrasound homogenization, an emerging technology with cost‐effectiveness, is widely used in food industry. Rice bran protein is a high‐quality protein with hypoallergenic and attracts a growing interesting in exploring its application. In this study, ultrasound homogenization was used to produce rice bran protein‐stabilized emulsions and the effects of ultrasound power and ultrasound time on characterizations of emulsion were then investigated. Findings Results indicated that the emulsions prepared by ultrasound homogenization at 20% power for 20 min had a higher interfacial protein concentration and a smaller droplet size, leading to an increase in stability against creaming. Subsequently, the effects of environmental conditions on emulsion stability were explored, and results demonstrated that emulsion exhibited excellent tolerance for high concentration of NaCl (500 mM) and high temperature (90°C). However, emulsion stability was destroyed under acid conditions. Conclusions The ultrasound homogenization technique was an effective method to prepare rice bran protein‐stabilized emulsion, and the emulsions prepared by ultrasound homogenization at 20% power for 20 min possessed good stability against creaming. Significance and novelty Rice bran protein isolate showed good emulsifying properties. Ultrasound homogenization could produce an emulsion with good stability and tolerance for high concentration of NaCl and high temperature.

show abstract

Section: Resultssupporting

confidence: 93%

Section: Particle Size Distributionsupporting

confidence: 90%

See 1 more Smart Citation

Preparation and characterization of rice bran protein‐stabilized emulsion by using ultrasound homogenization

Sun

Chen

et al. 2019

Cereal Chem

View full text Add to dashboard Cite

show abstract

“…The improvement of emulsifying property and emulsifying stability may be due to the expansion of the folded polypeptide chains and the change of secondary structure during the phosphorylation of PPI. These changes result in the enhancement of hydrophobicity on the surface of PPI and improve the ability of protein to diffuse to oil–water interface (Peng et al , ). The increase in OAC may also due to the significant increase in hydrophobic groups on the surface of protein, which enhances the binding force between protein and oil.…”

Section: Resultsmentioning

confidence: 99%

Functional properties and structural characteristics of phosphorylated pea protein isolate

Liu

Wang

et al. 2019

Int J of Food Sci Tech

View full text Add to dashboard Cite

In order to expand the application of pea proteins in the food industry, pea protein isolate (PPI) was chemically phosphorylated to improve its functional properties. Based on the comprehensive membership value (CMV) degree, the optimal condition for PPI phosphorylation modification was as follows: pH 12, modification temperature at 70°C and an addition of 7.0% (w/v) sodium tripolyphosphate (STP). Under this condition, the solubility, emulsifying property, emulsifying stability, foaming property and oil absorption capacity of the modified PPI were improved substantially. In addition, the structure of modified PPI was characterised by scanning electron microscope (SEM) and Fourier transform infrared (FTIR) spectroscopy. The results showed that the modified PPI had a smooth and uniform lamellar structure, where the content of a-helix and b-sheet structure increased, but the content of b-corner and random coil structure decreased. The thermodynamic properties were analysed by differential scanning calorimetry (DSC) and the results showed that ΔH of the modified PPI increased significantly. Finally, the optimum phosphorylated PPI was mixed with 0.4% (w/v) xanthan gum to form PPI fat mimics (PPI-FM). PPI-FM was added into mango mousse cake to reduce the amount of light cream, and the result showed up to 20% of light cream could be substituted.

show abstract

“…Barac et al () found that the emulsifying ability of the pea proteins increased as the pH moved away from the isoelectric point. Peng et al () used heat treatment (95 °C, 30 min) to improve the emulsifying properties of pea proteins. Donsì, Senatore, Huang, and Ferrari () showed that high‐pressure homogenization (300 MPa, five passes) enhanced the emulsifying ability of pea proteins by disrupting the disulfide bonds, unraveling the hydrophobic moieties, and forming NE with an average droplet size of less than 200 nm.…”

Section: Introductionmentioning

confidence: 99%

Stability and Bioavailability of Curcumin in Mixed Sodium Caseinate and Pea Protein Isolate Nanoemulsions

Yerramilli

Longmore

Ghosh

2018

J Americ Oil Chem Soc

View full text Add to dashboard Cite

The goals of this research were to develop oil-inwater nanoemulsions (NE) encapsulating curcumin by partially replacing sodium caseinate (SC) with pea protein isolate (1:1) and to investigate the lipid digestibility and bioaccessibility of curcumin using in vitro digestion. Structural changes in oil droplets during digestion were also examined using particle-size measurement and confocal laser-scanning microscopy. Both SC and mixed protein (MP)-stabilized NE were stable for the experimental time frame of eight weeks without significant changes in the droplet size. About 50% active curcumin encapsulated in the NE remained stable over eight weeks where the stability was higher for SC compared to the MP-stabilized NE (MPE). An increase in the droplet sizes and changes in their distribution during in vitro digestion were found to be a combined effect of the presence of digestive enzymes and also the rapid changes in the ionic strength and pH of the system. The lipid digestibility of the MPE was significantly lower than the SCstabilized NE, which was attributed to a stronger viscoelastic oil-droplet interface in the presence of pea proteins. However, the former was found to be as efficient as the latter in successfully releasing about 50% curcumin in the simulated intestine phase. Therefore, pea proteins can be used to partially replace SC as an emulsion stabilizer for the protection and delivery of oil-soluble bioactive compounds.Keywords Curcumin Á Nanoemulsion Á Sodium caseinate Á Pea protein isolate Á In vitro digestion Á Bioaccessibility J Am Oil Chem Soc (2018) 95: 1013-1026.

show abstract

Effects of heat treatment on the emulsifying properties of pea proteins

Cited by 273 publications

References 35 publications

Preparation and characterization of rice bran protein‐stabilized emulsion by using ultrasound homogenization

Preparation and characterization of rice bran protein‐stabilized emulsion by using ultrasound homogenization

Functional properties and structural characteristics of phosphorylated pea protein isolate

Stability and Bioavailability of Curcumin in Mixed Sodium Caseinate and Pea Protein Isolate Nanoemulsions

Contact Info

Product

Resources

About