Comparative structural and emulsifying properties of ultrasound-treated pea (Pisum sativum L.) protein isolate and the legumin and vicilin fractions

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4 Scopus citations

Abstract

The structural properties, interfacial behavior, and emulsifying ability of ultrasound-treated pea protein isolate (PPI) and the legumin (11S) and vicilin (7S) globulin fractions prepared with a salt-solubilization procedure were investigated. Of the three protein groups, PPI was strongly responsive to ultrasound perturbation (20 kHz, 57–60 W·cm−2) showing the greatest solubility increase, particle size reduction, structure destabilization, and conformational change. Similar but less remarkable effects were observed on 11S globulins; 7S proteins, already highly soluble (>99%), were generally less sensitive to ultrasound. The ultrasound treatment significantly improved emulsifying activity, which resulted in greater emulsifying capacity and stronger interfacial adsorption for all protein samples. PPI exhibited the higher activity increase (70.8%) compared to approximately 30% for 11S and 7S. For both control and ultrasound treated proteins, the emulsifying capacity was in the order of 7S > 11S > PPI, inversely related to the trend of protein loading at the interface, indicating efficiency differences. The latter was attributed to emulsion clusters formed through protein–protein interaction in PPI and 11S emulsions which were visibly absent in 7S emulsions.

Original languageEnglish
Article number111179
JournalFood Research International
Volume156
DOIs
StatePublished - Jun 2022

Bibliographical note

Funding Information:
This study is supported by the USDA National Institute of Food and Agriculture (Hatch Project 1020736) and Roquette America Inc.

Publisher Copyright:
© 2022 Elsevier Ltd

Keywords

  • Emulsion
  • Interfacial loading
  • Legumin
  • Pea protein isolate
  • Ultrasound
  • Vicilin

ASJC Scopus subject areas

  • Food Science

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