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    <subfield code="2">doi</subfield>
    <subfield code="a">10.1016/j.ifset.2025.104313</subfield>
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    <subfield code="2">sideral</subfield>
    <subfield code="a">146176</subfield>
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    <subfield code="a">ART-2025-146176</subfield>
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    <subfield code="a">eng</subfield>
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  <datafield tag="100" ind1=" " ind2=" ">
    <subfield code="a">Galvis-Nieto, Juan David</subfield>
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  <datafield tag="245" ind1=" " ind2=" ">
    <subfield code="a">Boosting catalytic performance of two immobilized enzymes via pulsed electric fields (PEF)</subfield>
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    <subfield code="c">2025</subfield>
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    <subfield code="a">This study investigates the impact of Pulsed Electric Fields (PEF) treatment on the activity and stability of immobilized enzyme systems (IES), specifically Candida rugosa lipase (CRL) and Trichoderma reesei mannanase (TRM). Results demonstrate that PEF significantly enhances enzymatic activity under adjusted conditions, with lipase IES achieving a 53.11 ± 3.08 % increase at 3 kV/cm (28 pulses) and mannanase IES reaching 63.26 ± 16.12 % activation rise under similar conditions. However, higher field strengths (4 kV/cm) led to variable effects, including activity reductions of up to 45 % for lipase and 28 % for mannanase IES. Operational stability tests revealed that untreated IES lost ∼20 % of their initial activity after 10 reuse cycles. However, applying PEF treatment after the 10th cycle successfully reactivated the enzymes, temporarily restoring activity to over 100 % of the initial value before a subsequent decline occurred. Storage stability studies showed a remarkable but transient surge in lipase IES activity (reaching 507 % after one week), whereas mannanase IES activity increased to 207 % after one week but returned to baseline levels thereafter. Pulse width influenced activation, with optimal activation at 10 μs for lipase and both 10 μs and 60 μs for mannanase. Frequency also influenced enzyme performance, with 1 Hz proving more effective than 10 Hz.
These findings highlight PEF as a powerful tool for short-term enzyme activation, though long-term stability remains a challenge. The study provides critical insights into optimizing PEF parameters for industrial biocatalytic applications.</subfield>
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    <subfield code="a">Access copy available to the general public</subfield>
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    <subfield code="9">info:eu-repo/grantAgreement/ES/DGA/A03-23R</subfield>
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  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Abad, Vanesa</subfield>
    <subfield code="u">Universidad de Zaragoza</subfield>
    <subfield code="0">(orcid)0009-0000-8889-1263</subfield>
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  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Salgado, Natalia</subfield>
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    <subfield code="a">Narvaez-Perez, Jorge M.</subfield>
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  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Cardona, Carlos A.</subfield>
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  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Álvarez-Lanzarote, Ignacio</subfield>
    <subfield code="u">Universidad de Zaragoza</subfield>
    <subfield code="0">(orcid)0000-0003-2430-858X</subfield>
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  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Orrego A., Carlos E.</subfield>
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  <datafield tag="710" ind1="2" ind2=" ">
    <subfield code="1">2008</subfield>
    <subfield code="2">780</subfield>
    <subfield code="a">Universidad de Zaragoza</subfield>
    <subfield code="b">Dpto. Produc.Animal Cienc.Ali.</subfield>
    <subfield code="c">Área Tecnología de Alimentos</subfield>
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  <datafield tag="773" ind1=" " ind2=" ">
    <subfield code="g">107 (2025), 104313 [14 pp.]</subfield>
    <subfield code="p">Innov. food sci. emerg. technol.</subfield>
    <subfield code="t">INNOVATIVE FOOD SCIENCE &amp; EMERGING TECHNOLOGIES</subfield>
    <subfield code="x">1466-8564</subfield>
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    <subfield code="z">info:eu-repo/date/embargoEnd/2026-10-31</subfield>
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    <subfield code="a">2025-11-21-14:25:29</subfield>
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