Ultrasound-induced structural modification and thermal properties of oat protein

Runnan Li, Youling L. Xiong

Research output: Contribution to journalArticlepeer-review

56 Scopus citations


The objective of this study was to characterize the solubility, structural, thermal, and aggregation properties of oat protein under high-intensity ultrasound (HIU) treatment. Suspensions of oat protein isolate (OPI) at pH 2.0–8.0 were subjected to HIU for 5 min at 70% amplitude; solubility, particle size, surface attributes, UV–Vis absorption, intrinsic fluorescence, polypeptide profiles, calorimetric properties, and thermal aggregation were determined. The HIU treatment significantly reduced particle size (up to 37%) and increased surface charge of OPI leading to solubility increases (up to 48%, P < 0.05) at pH 2.0–3.0 and pH 5.5–8.0. However, HIU did not alter the protein profile nor disrupt disulfide linkages between α and β subunits. Reduced enthalpy of denaturation with no shift in thermal transition temperature were observed in HIU samples unless disulfide bonds were pre-cleaved. While control OPI displayed variable changes in particle size upon heating from 20 to 95 °C, the HIU sample maintained a relatively uniform and smaller particle size. The findings indicate that protein particle disruption and weakening of intermolecular forces by HIU improved physicochemical and thermal properties of OPI, which are of value to processing oat protein-based beverages and other food products.

Original languageEnglish
Article number111861
StatePublished - Sep 2021

Bibliographical note

Publisher Copyright:
© 2021 Elsevier Ltd


  • High-intensity ultrasound (HIU)
  • Oat protein isolate (OPI)
  • Solubility
  • Thermal property

ASJC Scopus subject areas

  • Food Science


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