Ultrasound‐assisted extraction and modification of plant‐based proteins: Impact on physicochemical, functional, and nutritional properties
Abstract
Ultrasonication is a green technology that has recently received an enormous research attention for extraction of plant‐based proteins and tailoring the functionalities of these ingredients. Ultrasonication is generally used as a pretreatment method in the conventional protein solubilization protocols because it can break the cell matrix to improve the extractability. The rate of protein extraction and increase in the extraction yields depend on operating conditions such as sonic energy density, time of sonication, the substrate to slurry ratio, agitation, and so on. Ultrasonication is also applied to modify the physical, structural, and functional properties of protein‐based ingredients, besides simultaneous extraction and modifications. Significant changes that occur in protein physical properties due to sonication include size reduction, rheology, electrical conductivity, and zeta (ζ) potential. These changes are due to cavitation‐induced shear leading to changes in secondary and tertiary structures, including protein aggregation and cross‐linking due to oxidation. Physical and structural changes affect the resulting ingredient functionality and nutritional quality of protein. Changes in the functional properties, especially hydrophobicity, solubility, emulsion, and foaming, depend on the extent of ultrasound energy applied to the protein. This study aims to review major ultrasound process parameters and conditions for extraction and modification of plant proteins and their impact on protein structural changes and resulting physicochemical, functional, and nutritional properties.
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The decreases in Tc, To, and Tp for MB-70-US are likely due to greater disruption of ordered structures and enhanced protein unfolding.
“likely due to greater disruption of ordered structures and enhanced protein unfolding (Rahman et al., 2021; Sidiq et al., 2024)”
From Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states (2027) · cites this paper as Rahman et al., 2021
The slight increase in transition temperatures for FB-70-US may reflect ultrasound-induced rearrangement of intermolecular interactions.
“The slight increase in these transition temperatures for FB-70-US may reflect ultrasound-induced rearrangement of intermo lecular interactions (Adal, 2024; Rahman & Lamsal, 2021).”
From Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states (2027) · cites this paper as Rahman & Lamsal, 2021
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Zhu, M., Kasapis, S., & Dhital, S. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113251
- Authors
- Rahman, M. M., & Lamsal, B. P.
- Affiliations
- Department of Food Science and Human Nutrition Iowa State University Ames Iowa
- Venue
- Comprehensive Reviews in Food Science and Food Safety
- Publisher
- Wiley
- Published
- 2021-02-02
- Volume
- 20
- Issue
- 2
- Pages
- 1457-1480
- ISSN
- 1541-4337
- Cited by
- 407
- References
- 0
- Language
- en
- Licence
- Funders
- National Institute of Food and Agriculture (2018‐67017‐27560)
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