<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-04-18T00:06:25Z</responseDate><request verb="GetRecord" identifier="oai:www.recercat.cat:10459.1/465167" metadataPrefix="marc">https://recercat.cat/oai/request</request><GetRecord><record><header><identifier>oai:recercat.cat:10459.1/465167</identifier><datestamp>2025-09-15T18:56:38Z</datestamp><setSpec>com_2072_3622</setSpec><setSpec>col_2072_479130</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
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      <subfield code="a">Gulzar, Saqib</subfield>
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      <subfield code="a">Martín Belloso, Olga</subfield>
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      <subfield code="a">Soliva-Fortuny, Robert</subfield>
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      <subfield code="c">2024</subfield>
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      <subfield code="a">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.</subfield>
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      <subfield code="a">This project has received funding from the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement No 101034288.</subfield>
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      <subfield code="a">Ultrasonication</subfield>
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      <subfield code="a">Pulsed electric fields</subfield>
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      <subfield code="a">Fava bean protein isolate</subfield>
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      <subfield code="a">Protein functionality</subfield>
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      <subfield code="a">Plant-based proteins</subfield>
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      <subfield code="a">Tailoring the techno-functional properties of fava bean protein isolate: A comparative evaluation of ultrasonication and pulsed electric field treatments</subfield>
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