000164049 001__ 164049
000164049 005__ 20251121161351.0
000164049 0247_ $$2doi$$a10.1016/j.ifset.2025.104313
000164049 0248_ $$2sideral$$a146176
000164049 037__ $$aART-2025-146176
000164049 041__ $$aeng
000164049 100__ $$aGalvis-Nieto, Juan David
000164049 245__ $$aBoosting catalytic performance of two immobilized enzymes via pulsed electric fields (PEF)
000164049 260__ $$c2025
000164049 5060_ $$aAccess copy available to the general public$$fUnrestricted
000164049 5203_ $$aThis 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.
000164049 536__ $$9info:eu-repo/grantAgreement/ES/DGA/A03-23R
000164049 540__ $$9info:eu-repo/semantics/embargoedAccess$$aby-nc-nd$$uhttps://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
000164049 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/submittedVersion
000164049 700__ $$0(orcid)0009-0000-8889-1263$$aAbad, Vanesa$$uUniversidad de Zaragoza
000164049 700__ $$aSalgado, Natalia
000164049 700__ $$aNarvaez-Perez, Jorge M.
000164049 700__ $$aCardona, Carlos A.
000164049 700__ $$0(orcid)0000-0003-2430-858X$$aÁlvarez-Lanzarote, Ignacio$$uUniversidad de Zaragoza
000164049 700__ $$aOrrego A., Carlos E.
000164049 7102_ $$12008$$2780$$aUniversidad de Zaragoza$$bDpto. Produc.Animal Cienc.Ali.$$cÁrea Tecnología de Alimentos
000164049 773__ $$g107 (2025), 104313 [14 pp.]$$pInnov. food sci. emerg. technol.$$tINNOVATIVE FOOD SCIENCE & EMERGING TECHNOLOGIES$$x1466-8564
000164049 8564_ $$s472323$$uhttps://zaguan.unizar.es/record/164049/files/texto_completo.pdf$$yPreprint$$zinfo:eu-repo/date/embargoEnd/2026-10-31
000164049 8564_ $$s1085721$$uhttps://zaguan.unizar.es/record/164049/files/texto_completo.jpg?subformat=icon$$xicon$$yPreprint$$zinfo:eu-repo/date/embargoEnd/2026-10-31
000164049 909CO $$ooai:zaguan.unizar.es:164049$$particulos$$pdriver
000164049 951__ $$a2025-11-21-14:25:29
000164049 980__ $$aARTICLE