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Fish processing and digestion affect parvalbumins detectability in Gilthead Seabream and European seabass

dc.contributor.authorSchrama, Denise
dc.contributor.authorRaposo de Magalhães, Cláudia
dc.contributor.authorCerqueira, Marco
dc.contributor.authorCarrilho, Raquel
dc.contributor.authorRevets, Dominique
dc.contributor.authorKuehn, Annette
dc.contributor.authorEngrola, Sofia
dc.contributor.authorRodrigues, Pedro
dc.date.accessioned2022-11-11T10:40:36Z
dc.date.available2022-11-11T10:40:36Z
dc.date.issued2022-11-03
dc.date.updated2022-11-10T14:27:42Z
dc.description.abstractConsumption of aquatic food, including fish, accounts for 17% of animal protein intake. However, fish consumption might also result in several side-effects such as sneezing, swelling and anaphylaxis in sensitized consumers. Fish allergy is an immune reaction to allergenic proteins in the fish muscle, for instance parvalbumin (PV), considered the major fish allergen. In this study, we characterize PV in two economically important fish species for southern European aquaculture, namely gilthead seabream and European seabass, to understand its stability during in vitro digestion and fish processing. This information is crucial for future studies on the allergenicity of processed fish products. PVs were extracted from fish muscles, identified by mass spectrometry (MS), and detected by sandwich enzyme-linked immunosorbent assay (ELISA) after simulated digestion and various food processing treatments. Secondary structures were determined by circular dichroism (CD) after purification by anion exchange and gel filtration chromatography. In both species, PVs presented as α-helical and β-sheet structures, at room temperature, were shown to unfold at boiling temperatures. In European seabass, PV detectability decreased during the simulated digestion and after 240 min (intestinal phase) no detection was observed, while steaming showed a decrease (<i>p</i> < 0.05) in PVs detectability in comparison to raw muscle samples, for both species. Additionally, freezing (−20 °C) for up to 12 months continued to reduce the detectability of PV in tested processing techniques. We concluded that PVs from both species are susceptible to digestion and processing techniques such as steaming and freezing. Our study obtained preliminary results for further research on the allergenic potential of PV after digestion and processing.
dc.identifier.citationAnimals 12 (21): 3022 (2022)
dc.identifier.doi10.3390/ani12213022
dc.identifier.eissn2076-2615
dc.identifier.urihttp://hdl.handle.net/10400.1/18491
dc.language.isoeng
dc.peerreviewedyes
dc.publisherMDPI
dc.subjectParvalbumin
dc.subjectEuropean seabass
dc.subjectGastrointestinal digestion
dc.subjectFish processing
dc.titleFish processing and digestion affect parvalbumins detectability in Gilthead Seabream and European seabass
dc.typejournal article
dspace.entity.typePublication
oaire.citation.issue21
oaire.citation.startPage3022
oaire.citation.volume12
person.familyNameSchrama
person.familyNameRaposo de Magalhães
person.familyNameCerqueira
person.familyNameCarrilho
person.familyNameEngrola
person.familyNameRodrigues
person.givenNameDenise
person.givenNameCláudia
person.givenNameMarco
person.givenNameRaquel Vaz
person.givenNameSofia
person.givenNamePedro
person.identifier159154
person.identifier237846
person.identifier.ciencia-id501C-AC69-68C0
person.identifier.ciencia-idEB1C-0E40-F003
person.identifier.ciencia-id4F1E-16FC-00D8
person.identifier.ciencia-idF41E-AC88-8BCD
person.identifier.ciencia-idA610-29E7-9B83
person.identifier.orcid0000-0003-0274-5957
person.identifier.orcid0000-0001-7751-2870
person.identifier.orcid0000-0001-7237-5053
person.identifier.orcid0000-0002-5244-5541
person.identifier.orcid0000-0002-9668-1204
person.identifier.ridH-6511-2016
person.identifier.ridA-2485-2012
person.identifier.ridM-3406-2013
person.identifier.scopus-author-id55755583400
person.identifier.scopus-author-id8669620600
person.identifier.scopus-author-id55107531000
rcaap.rightsopenAccess
rcaap.typearticle
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