Thermosonication-induced structural changes and solution properties of mung bean protein

Zhifeng Zhong, Youling L. Xiong

Research output: Contribution to journalArticlepeer-review

92 Scopus citations


Mung bean protein is considered a highly nutritive food ingredient, but its solution properties are not well defined. In this study, suspensions of mung bean protein isolate (MPI, 10%, w/v) were subjected to high intensity ultrasound (20 kHz, 30% amplitude) at varied durations (5, 10, 20, and 30 min) with controlled temperatures (30, 50, and 70 °C) to determine the effects of thermosonication treatment on physical properties of the protein solution. Results showed that thermosonication treatment significantly reduced the particle size and free sulfhydryl content of MPI in a time-dependent manner. Ultrasound increased surface hydrophobicity, and the exposure of nonpolar groups led to the formation of soluble aggregates. Changes in secondary structure of MPI were minimal at 30 and 50 °C but were significant at 70 °C. The dissociation of native components followed by reaggregation into soluble particles following ultrasound treatment at 70 °C resulted in remarkable improvements of protein solubility (>2 fold), clarity, and stability of the MPI suspensions. The findings indicated that thermosonication could be a promising technology for the processing of mung bean protein beverage.

Original languageEnglish
Article number104908
JournalUltrasonics Sonochemistry
StatePublished - Apr 2020

Bibliographical note

Publisher Copyright:
© 2019 Elsevier B.V.


  • Conformational structure
  • Mung bean protein
  • Protein aggregation
  • Solution properties
  • Thermosonication

ASJC Scopus subject areas

  • Chemical Engineering (miscellaneous)
  • Environmental Chemistry
  • Radiology Nuclear Medicine and imaging
  • Acoustics and Ultrasonics
  • Organic Chemistry
  • Inorganic Chemistry


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