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Tailoring the techno-functional properties of Fava bean protein isolates: A comparative evaluation of ultrasonication and pulsed electric field treatments

Gulzar, Saqib, Martín-Belloso, Olga, Soliva-Fortuny, Robert·2024·Foods
DOI 10.3390/foods13030376PMC PMC10855325
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Abstract

The fava bean protein isolate (FBPI) holds promise as a sustainable plant-based protein ingredient. However, native FBPIs exhibit limited functionality, including unsuitable emulsifying activities and a low solubility at a neutral pH, restricting their applications. This study is focused on the effect of ultrasonication (US) and pulsed electric fields (PEF) on modulating the techno-functional properties of FBPIs. Native FBPIs were treated with US at amplitudes of 60–90% for 30 min in 0.5 s on-and-off cycles and with PEF at an electric field intensity of 1.5 kV/cm with 1000–4000 pulses of 20 μs pulse widths. US caused a reduction in the size and charge of the FBPIs more prominently than the PEF. Protein characterization by means of SDS-PAGE illustrated that US and PEF caused severe-to-moderate changes in the molecular weight of the FBPIs. In addition, a spectroscopic analysis using Fourier-transform infrared (FTIR) and circular dichroism (CD) revealed that US and the PEF induced conformational changes through partial unfolding and secondary structure remodeling from an α-helix to a β-sheet. Crystallographic and calorimetric determinations indicated decreased crystallinity and lowered thermal transition temperatures of the US- and PEF-modified FBPIs. Overall, non-thermal processing provided an effective strategy for upgrading FBPIs’ functionality, with implications for developing competitive plant-based protein alternatives.

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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 Gulzar et al., 2024

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Authors
Gulzar, S., Martín-Belloso, O., & Soliva-Fortuny, R.
Affiliations
Department of Food Technology, Engineering and Science, University of Lleida, Avda. Rovira Roure 191, 25198 Lleida, Spain
ORCID
Venue
Foods
Publisher
MDPI AG
Published
2024-01-24
Volume
13
Issue
3
Pages
376
ISSN
2304-8158
DOI
10.3390/foods13030376
PMC
PMC10855325
Cited by
61
References
1
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
  • European Union’s Horizon 2020 research (101034288)
  • innovation program under the Marie Skłodowska-Curie (101034288)

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