Synergistic modification of pea protein structure using high-intensity ultrasound and pH-shifting technology to improve solubility and emulsification

Zhang, Jingnan; Liu, Qian; Chen, Qian; Sun, Fangda; Liu, Haotian; Kong, Bing

doi:10.1016/j.ultsonch.2022.106099

Cited by 75 publications

(25 citation statements)

References 43 publications

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“…However, the HIPEs which were stabilized by MPPI showed a gel-like appearance with good self-supporting properties and no phase separation, indicating that it had the ability to stabilize HIPE. The possible explanation for this phenomenon was that the structure of natural PPI was highly ordered, had a certain rigidity, and presented an agglomeration state, which meant it could not be adsorbed at the interface [ 4 ]. As depicted in Figure 1 A, the natural PPI aggregates were scattered in the continuous phase and could not play the role of stabilizing the oil droplets.…”

Section: Resultsmentioning

confidence: 99%

“…Under the action of external force, the system would undergo severe coalescence and demulsification. However, the hydrophobic groups and polar sites of the MPPI were exposed and the α-helical content was reduced, thus improving the solubility and emulsification [ 4 ]. MPPI with flexible structure could effectively expand and rearrange at the oil–water interface during the shearing process to tightly coat oil droplets and form a compact elastic interface film [ 4 ].…”

Section: Resultsmentioning

confidence: 99%

“…Similar to our previous work [ 4 ], the hydrated overnight PPI (5 wt%) was adjusted to pH 12 using 2 M NaOH, and then treated at 20 kHz with 500 W ultrasonic power for 10 min. The solution was stirred at room temperature for 1 h, after which the pH was adjusted to 7 with 1 M HCl and then the solution diluted to various concentrations (1–5 wt%).…”

Section: Methodsmentioning

confidence: 99%

“…Pea protein isolate (PPI), with its high nutritional value and hypoallergenicity, has aroused considerable interest as a sustainable alternative to animal-based protein [ 3 ]. However, the highly ordered spherical structure and poor solubility of native PPI inhibit its ability to emulsify at the oil–water interface [ 4 ]. Although some studies have demonstrated that treatment of PPI by glycosylation [ 5 ], potassium metabisulfite induction [ 6 ] and microgel [ 7 ] formation enabled it to stabilize HIPEs, these strategies are complex and require precise control of the reaction process.…”

Section: Introductionmentioning

confidence: 99%

“…Bubbles generated by acoustic cavitation collapse upon reaching a critical size, thereby increasing the local pressure in the cavitation zone and creating high shear forces and turbulence around the bulk liquid, enabling physical modification of the material [ 12 ]. Our group earlier found that HIU treatment can make the conformation of the molten spherical state PPI undergoing pH-shifting more flexible, endowing better solubility and emulsification [ 4 ]. A fascinating hypothesis is that the molten state induced by pH-shifting promotes the adsorption of proteins at the interface, whereas the flexible conformation caused by HIU treatment increases the possibility of intertwined interfacial proteins, providing better stability and support for HIPEs.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

High Internal Phase Emulsions Stabilized by Pea Protein Isolate Modified by Ultrasound Combined with pH-Shifting: Micromorphology, Rheology, and Physical Stability

Zhang

Zhao

et al. 2023

Foods

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In this study, the interfacial behavior of high internal phase emulsions (HIPEs), stabilized by ultrasound combined with pH-shifting modified pea protein isolate (MPPI), was investigated, and its emulsification process and stabilization mechanism were discussed. The effects of MPPI concentration on the micromorphology, droplet size, rheology, and stability of HIPEs were investigated. As the MPPI concentration increased, the appearance of HIPEs gradually changed from a relatively fluid state to a plastic solid-like state with detailed texture. There occurred a gradual decrease in droplet size, the cohering of an orderly and tight arrangement, in addition to the formation of a bilayer elastic interface layer. The macro- and microrheological assessments confirmed that the apparent viscosity, storage modulus, elasticity index, and macroscopic viscosity index increased gradually. Furthermore, it was demonstrated that 5 wt% MPPI-stabilized HIPEs had the potential to be used as 3D printing inks. Stability evaluation showed that the TURBISCAN stability index decreased and centrifugal stability increased. The appearance and microstructure remained highly stable after heating at 80 °C for 30 min and storage at 4 ℃ for 90 days. These findings confirm that MPPI improves the rheological behavior and stability of HIPEs by modulating the interfacial adsorption and network structure.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

High Internal Phase Emulsions Stabilized by Pea Protein Isolate Modified by Ultrasound Combined with pH-Shifting: Micromorphology, Rheology, and Physical Stability

Zhang

Zhao

et al. 2023

Foods

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Toward Diverse Plant Proteins for Food Innovation

Kim,

Yiu,

Wang

et al. 2024

Advanced Science

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This review highlights the development of plant proteins from a wide variety of sources, as most of the research and development efforts to date have been limited to a few sources including soy, chickpea, wheat, and pea. The native structure of plant proteins during production and their impact on food colloids including emulsions, foams, and gels are considered in relation to their fundamental properties, while highlighting the recent developments in the production and processing technologies with regard to their impacts on the molecular properties and aggregation of the proteins. The ability to quantify structural, morphological, and rheological properties can provide a better understanding of the roles of plant proteins in food systems. The applications of plant proteins as dairy and meat alternatives are discussed from the perspective of food structure formation. Future directions on the processing of plant proteins and potential applications are outlined to encourage the generation of more diverse plant‐based products.

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On treatment options to improve the functionality of pea protein

Mathew,

Kim,

Wang

et al. 2023

J Americ Oil Chem Soc

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Pea proteins have garnered attention as a viable alternative to animal proteins, offering health, and sustainability benefits. However, their functional limitations, such as poor solubility, hinder their application in plant‐based food products. This review details the specific physical, chemical, and biological methods employed to enhance pea protein functionality. Chemical methods have been the most effective, particularly in improving solubility, emulsification, and foaming properties, which are essential for food applications like dairy alternatives and meat analogues. Biological methods significantly enhance water and oil retention, contributing to better food texture. Physical methods, including ultrasound and heat treatment, also show promise but require careful application to avoid protein denaturation. While chemical methods are efficacious, they raise concerns about cost‐effectiveness and environmental impact. The review identifies combined treatment approaches as a fertile area for future research, suggesting that a multi‐faceted strategy may provide comprehensive improvements to pea protein functionality.

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Synergistic modification of pea protein structure using high-intensity ultrasound and pH-shifting technology to improve solubility and emulsification

Cited by 75 publications

References 43 publications

High Internal Phase Emulsions Stabilized by Pea Protein Isolate Modified by Ultrasound Combined with pH-Shifting: Micromorphology, Rheology, and Physical Stability

High Internal Phase Emulsions Stabilized by Pea Protein Isolate Modified by Ultrasound Combined with pH-Shifting: Micromorphology, Rheology, and Physical Stability

Toward Diverse Plant Proteins for Food Innovation

On treatment options to improve the functionality of pea protein

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