Impact of plasma reactive species on the structure and functionality of pea protein isolate

Research output: Contribution to journalArticlepeer-review

47 Scopus citations

Abstract

The impact of plasma-produced reactive oxygen and nitrogen species, in particular O3, NxOy, H2O2 and OH, on the structure and functionality of pea protein isolate (PPI) was evaluated. Reactive species were produced through a combination of controlled measurements and plasma treatments. Pronounced structural and functional effects were observed upon treatment with reactive species at pH 2. All reactive species induced protein denaturation and the formation of disulfide-linked soluble aggregates. A significant increase in surface hydrophobicity and β-sheet content was only induced by treatment with O3 and OH. These specific changes resulted in significant enhancement in gelation and emulsification. While H2O2 enhanced PPI color by increasing whiteness, it had the least impact on protein structure and functionality. Results of this work can be used to optimize cold atmospheric plasma treatment of PPI to induce specific structural changes and a directed enhancement in functionality.

Original languageEnglish (US)
Article number131135
JournalFood Chemistry
Volume371
DOIs
StatePublished - Mar 1 2022

Bibliographical note

Funding Information:
This project was generously funded by the Plant Protein Innovation Center (PPIC). FTIR-ATR data collection of this work was carried out in the Characterization Facility, University of Minnesota, which receives partial support from the NSF through the MRSEC (Award Number DMR-2011401) and the NNCI (Award Number ECCS-2025124) programs.

Publisher Copyright:
© 2021 Elsevier Ltd

Keywords

  • Cold atmospheric plasma
  • Pea protein isolate
  • Pea protein structure and functionality
  • Reactive oxygen and nitrogen species

MRSEC Support

  • Shared

PubMed: MeSH publication types

  • Journal Article

Fingerprint

Dive into the research topics of 'Impact of plasma reactive species on the structure and functionality of pea protein isolate'. Together they form a unique fingerprint.

Cite this