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Cited by 3Proteins in Food SystemsProtein Structure and DynamicsProtein Hydrolysis and Bioactive Peptides

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Improving fava bean protein functionality via mild ultrasonication: A comparative study with other plant proteins

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Mukhtar, Kinza, Wang, Yong, Selomulya, Cordelia·2026·Food Research International
DOI 10.1016/j.foodres.2026.119231
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Abstract

Fava bean protein isolate (FBPI) is a promising alternative protein source in food formulation due to its high nutritional value and environmental sustainability. However, its limited solubility and functional properties restrict its use in food applications. This study investigated the effect of mild ultrasonication (72-102 W; 1-15 min) on the structural and functional properties of FBPI and compared it with those of pea, soy, and rice protein isolates. Mild ultrasonication increased FBPI solubility from 40% (untreated) to 92%, particularly after 3-5 min of treatment, which was attributed to the disruption of protein aggregates. In comparison, solubility also increased for pea from 10 to 12% (untreated) to 60-86% for different commercial isolates, soy from control 19% to 36% and rice control 5% to 6% at ultrasonication US 72 W with 5 min treatment. Structural analysis (FTIR and MMS) revealed a high β-sheet content in native FBPI and an increase in β-sheet proportion following mild ultrasonication in all protein isolates, suggesting conformational rearrangements and partial protein unfolding. These molecular changes were accompanied by a marked increase in surface hydrophobicity (H o ), likely due to the exposure of buried hydrophobic residues. The enhanced interfacial properties resulted in a twofold improvement in emulsion stability index, although the emulsifying activity index (EAI) remained relatively unchanged (p > 0.05). Overall, mild ultrasonication induced structural…

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  • Ultrasonication effects can reduce particle size, promote partial unfolding, and modify non-covalent interactions, thereby altering solubility, aggregation behaviour, and gelation performance.

    “These effects can reduce particle size, promote partial unfolding, and modify non-covalent interactions, thereby altering solubility, aggregation behaviour, and gelation performance”

    From Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states (2027) · cites this paper as Mukhtar et al., 2026

  • Existing studies have primarily focused on the effects of ultrasound parameters on native or untreated protein isolates, with emphasis on extraction efficiency, solubility and interfacial properties, particularly for legume proteins such as faba bean and mung bean proteins.

    “existing studies have primarily focused on the effects of ultrasound parameters on native or untreated protein isolates, with emphasis on extraction efficiency, solubility and interfacial properties, particularly for legume proteins such as faba bean and mung bean proteins”

    From Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states (2027) · cites this paper as Mukhtar et al., 2026

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Cited by

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Metadata

Authors
Mukhtar, K., Wang, Y., & Selomulya, C.
Affiliations
UNSW Sydney (AU)
Corresponding author
Wang, Yong
ORCID
Venue
Food Research International
Publisher
Elsevier BV
Published
2026-07
Volume
236
Pages
119231
ISSN
0963-9969 (ISSN-L)
DOI
10.1016/j.foodres.2026.119231
OpenAlex
W7154716692
Cited by
3
References
0
Citations by year
2026: 3
FWCI
7.11
Type
journal article
Language
en
Open access
Licence
Locations
  • Food Research International (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
Australian Research Council (DP250101468)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
Keywords
protein solubility, protein functional properties, protein structure modification, β-sheet content, protein unfolding, surface hydrophobicity, emulsifying properties, emulsion stability, pea protein isolate, soy protein isolate, rice protein isolate, plant proteins, alternative protein sources
MeSH terms
Food Handling, Plant Proteins, Oryza, Solubility, Sonication, Glycine max, Spectroscopy, Fourier Transform Infrared, Pisum sativum, Soybean Proteins, Hydrophobic and Hydrophilic Interactions

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