Interfacial dilatational and emulsifying properties of ultrasound-treated pea protein

Lei Sha; Aeneas O. Koosis; Qingling Wang; Alma D. True; Youling L. Xiong

doi:10.1016/j.foodchem.2021.129271

Interfacial dilatational and emulsifying properties of ultrasound-treated pea protein

Lei Sha
, Aeneas O. Koosis
, Qingling Wang
, Alma D. True
, Youling L. Xiong

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

197 Scopus citations

Abstract

In this study, the structural, interfacial, and emulsifying properties of high-intensity ultrasound (HUS)-treated pea protein isolate (PPI_US) were investigated. HUS at 50% amplitude and 57–60 W·cm⁻² for 5 min markedly improved protein solubility (by 132%), surface hydrophobicity (by 173%), and reduced particle size (by 52%). These physicochemical changes in PPI_US led to more rapid protein adsorption at the oil–water interface, improved emulsifying activity (by 18–27%) and capacity (by 11%), and enhanced emulsion physical stability. The multilayer nature, albeit less elastic, of the interfacial membrane formed by PPI_US when compared to control protein (PPI_C), based on dilatational testing, contributed to the above results. Moreover, PPI_US-stabilized emulsions exhibited a tendency of being less susceptible to lipid oxidation during storage. Thus, structure-modifying HUS may be a valuable processing technology for the manufacture of pea protein-based emulsion foods.

Original language	English
Article number	129271
Journal	Food Chemistry
Volume	350
DOIs	https://doi.org/10.1016/j.foodchem.2021.129271
State	Published - Jul 15 2021

Bibliographical note

Publisher Copyright:
© 2021 Elsevier Ltd

Funding

This study is supported by the USDA National Institute of Food and Agriculture, Hatch (Project 1020736) and by Roquette America Inc. Author Lei Sha acknowledges the sabbatical opportunity to study at the University of Kentucky which is supported through the First-class Discipline Project of Liaoning Province, China.

Funders	Funder number
First-class Discipline Project of Liaoning Province
Roquette America, Inc.
US Department of Agriculture National Institute of Food and Agriculture, Agriculture and Food Research Initiative	1020736

Keywords

1-Anilino-8-naphthalenesulfonate magnesium salt (PubChem CID: 87458)
2-Thiobarbituric acid (PubChem CID: 2723628)
Dilatational rheology
Fluorescein isothiocyanate (PubChem CID: 18730)
Lipid oxidation
Nile red (PubChem CID: 65182)
O/W emulsions
Pea protein
Sodium azide (PubChem CID: 33557)
Sodium dodecyl sulfate (PubChem CID: 3423265)
Ultrasonication

ASJC Scopus subject areas

Analytical Chemistry
Food Science

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10.1016/j.foodchem.2021.129271

Cite this

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title = "Interfacial dilatational and emulsifying properties of ultrasound-treated pea protein",

abstract = "In this study, the structural, interfacial, and emulsifying properties of high-intensity ultrasound (HUS)-treated pea protein isolate (PPIUS) were investigated. HUS at 50\% amplitude and 57–60 W·cm−2 for 5 min markedly improved protein solubility (by 132\%), surface hydrophobicity (by 173\%), and reduced particle size (by 52\%). These physicochemical changes in PPIUS led to more rapid protein adsorption at the oil–water interface, improved emulsifying activity (by 18–27\%) and capacity (by 11\%), and enhanced emulsion physical stability. The multilayer nature, albeit less elastic, of the interfacial membrane formed by PPIUS when compared to control protein (PPIC), based on dilatational testing, contributed to the above results. Moreover, PPIUS-stabilized emulsions exhibited a tendency of being less susceptible to lipid oxidation during storage. Thus, structure-modifying HUS may be a valuable processing technology for the manufacture of pea protein-based emulsion foods.",

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author = "Lei Sha and Koosis, \{Aeneas O.\} and Qingling Wang and True, \{Alma D.\} and Xiong, \{Youling L.\}",

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doi = "10.1016/j.foodchem.2021.129271",

language = "English",

volume = "350",

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AU - Sha, Lei

AU - Koosis, Aeneas O.

AU - Wang, Qingling

AU - True, Alma D.

AU - Xiong, Youling L.

PY - 2021/7/15

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AB - In this study, the structural, interfacial, and emulsifying properties of high-intensity ultrasound (HUS)-treated pea protein isolate (PPIUS) were investigated. HUS at 50% amplitude and 57–60 W·cm−2 for 5 min markedly improved protein solubility (by 132%), surface hydrophobicity (by 173%), and reduced particle size (by 52%). These physicochemical changes in PPIUS led to more rapid protein adsorption at the oil–water interface, improved emulsifying activity (by 18–27%) and capacity (by 11%), and enhanced emulsion physical stability. The multilayer nature, albeit less elastic, of the interfacial membrane formed by PPIUS when compared to control protein (PPIC), based on dilatational testing, contributed to the above results. Moreover, PPIUS-stabilized emulsions exhibited a tendency of being less susceptible to lipid oxidation during storage. Thus, structure-modifying HUS may be a valuable processing technology for the manufacture of pea protein-based emulsion foods.

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Interfacial dilatational and emulsifying properties of ultrasound-treated pea protein

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

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