Non-thermal Approach for Electromagnetic Field Exposure to Unfold Heat-Resistant Sunflower Protein

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dc.authoridYildirim-Elikoglu, Seda/0000-0002-5067-0139
dc.authoridMohammadifar, Mohammad Amin/0000-0001-8804-4873
dc.contributor.authorSubasi, Busra Gultekin
dc.contributor.authorYildirim-Elikoglu, Seda
dc.contributor.authorAltin, Ozan
dc.contributor.authorErdogdu, Ferruh
dc.contributor.authorMohammadifar, Mohammad Amin
dc.contributor.authorCapanoglu, Esra
dc.date.accessioned2024-10-26T18:11:19Z
dc.date.available2024-10-26T18:11:19Z
dc.date.issued2023
dc.departmentSivas Cumhuriyet Üniversitesi
dc.description.abstractThe non-thermal effect of electromagnetic field (NEF) on the structural and thermal properties of heat-resistant globular sunflower protein isolate was investigated by exposing samples to varying power levels (70 W, defrost (DF), and 350 W). Only the lowest consecutive power modes of the electromagnetic unit were conducted to complete at least two exposure cycles (for certainty) without exceeding 45 degrees C (non-thermal processing condition). The total polar amino acid content of the treated samples decreased by 14% with NEF applications since polar amino acids were the main targets of the electromagnetic field due to absorbing that energy as kinetic energy and inducing structural changes. The DF and 350 W treatments dissipated large particles/aggregates over 5000 nm completely. The treatment with the lowest power (70 W) produced the lowest average particle size (14% decrease) while it increased after the DF and 350 W applications (34 and 16%, respectively), which indicated partial unfolding and/or reaggregation. Less ordered structures had increased alpha-helix (max with 350 W by 22%) and decreased beta-sheet contents (max with 70 W by 30%) after the NEF treatments. The tertiary structures of the samples changed significantly following the NEF treatments with a blue shift on emission maxima with different fluorescence intensities. The thermal stability of the samples was analyzed with DSC and TGA; lower peak temperature (decreased by 28%) and denaturation enthalpy (decreased by 82%) besides higher gravimetric loss (by 1.3%) were obtained for DF and 350 W, compared to the control. The NEF could be considered a promising approach for structural alteration of globular sunflower protein.
dc.identifier.doi10.1007/s11947-022-02929-7
dc.identifier.endpage326
dc.identifier.issn1935-5130
dc.identifier.issn1935-5149
dc.identifier.issue2
dc.identifier.scopus2-s2.0-85141504957
dc.identifier.scopusqualityQ1
dc.identifier.startpage313
dc.identifier.urihttps://doi.org/10.1007/s11947-022-02929-7
dc.identifier.urihttps://hdl.handle.net/20.500.12418/30622
dc.identifier.volume16
dc.identifier.wosWOS:000880234500001
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherSpringer
dc.relation.ispartofFood and Bioprocess Technology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectNon-thermal microwave
dc.subjectProtein unfolding
dc.subjectPlant protein
dc.subjectSunflower protein
dc.subjectNon-thermal electromagnetic field
dc.titleNon-thermal Approach for Electromagnetic Field Exposure to Unfold Heat-Resistant Sunflower Protein
dc.typeArticle

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