Effects of sonication on the physicochemical and functional properties of walnut protein isolate
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The objective of this study was to investigate the impact of high-intensity ultrasound treatment (sonication) on the molecular, physicochemical, and functional properties of walnut protein isolate. Aqueous walnut protein suspensions were sonicated at varying power levels (200, 400 or 600 W) and times (15 or 30 min), and then any alternations in protein structure and properties were determined. SDS-PAGE demonstrated that there were no changes in protein electrophoretic patterns, indicating that sonication did not break covalent bonds. Circular dichroism spectroscopy indicated a small change in protein secondary structure after sonication, with a decrease in α-helix and increase in β-sheet, β-turn, and random coil content. There was an increase in surface free sulfhydryl (SH) groups and a decrease in fluorescence intensity after sonication, indicating that appreciable changes in tertiary structure occurred. Ultrasound reduced the size of the particles in aqueous walnut protein dispersions as confirmed by static light scattering and scanning electron microscopy, suggesting that sonication dissociated protein aggregates. Moreover, the water-solubility (+22%), emulsifying activity index (+26%), and emulsifying stability index (+41%) all increased after sonication. These results suggest that sonication is a valuable tool for improving the functional attributes of walnut proteins.
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Ultrasonic conditions can affect the structure of proteins after UAE.
“Another study has proposed that ultrasonic conditions can affect the structure of proteins after UAE [50].”
From A comprehensive review of ultrasonic assisted extraction (UAE) for bioactive components: Principles, advantages, equipment, and combined technologies (2023) · cites this paper as [50]
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“Another study has proposed that ultrasonic conditions can affect the structure of proteins after UAE [50].”
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- Authors
- Zhu, Z., Zhu, W., Yi, J., Liu, N., Cao, Y., Lu, J., Decker, E. A., & McClements, D. J.
- Affiliations
- University of Massachusetts Amherst (US)
- Shaanxi University of Science and Technology (CN)
- Corresponding author
- McClements, David Julian
- Venue
- Food Research International
- Publisher
- Elsevier BV
- Published
- 2018-04
- Volume
- 106
- Pages
- 853-861
- ISSN
- 0963-9969 (ISSN-L)
- OpenAlex
- W2789293326
- Cited by
- 382
- References
- 59
- Citations by year
- 2026: 54 · 2025: 59 · 2024: 53 · 2023: 63 · 2022: 71 · 2021: 44 · 2020: 22 · 2019: 13 · 2018: 2
- FWCI
- 19.00
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (am, 313 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Food Research International (acceptedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (31671888, 31501443)
- Doctoral Research Foundation of Shaanxi University of Science and Technology (2017BJ-21)
- National Institute of Food and Agriculture, USDA, Massachusetts Agricultural Experiment Station (MAS00491)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Physical Sciences › Materials Science › Materials Chemistry › Ultrasound and Cavitation Phenomena
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Keywords
- walnut protein isolate, sonication, high-intensity ultrasound, protein functional properties, protein secondary structure, protein tertiary structure, protein aggregation, emulsifying properties, water solubility, protein particle size, sulfhydryl groups
- MeSH terms
- Ultrasonic Waves, Circular Dichroism, Electrophoresis, Polyacrylamide Gel, Emulsions, Molecular Weight, Nuts, Particle Size, Plant Proteins, Solubility, Sonication, Sulfhydryl Compounds, Plant Proteins, Dietary, Water, Protein Structure, Secondary, Juglans, Hydrophobic and Hydrophilic Interactions
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