Proteomic analysis of wild boar meat: Effect of storage method and time on muscle protein stability

cris.virtual.author-orcid0000-0001-9062-0665
cris.virtual.author-orcid0000-0002-6331-5726
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cris.virtual.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtualsource.author-orcid1f7921d2-77e8-466f-bd15-132067931ce3
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cris.virtualsource.author-orcid6b8ff0a0-7556-4635-ae2c-064721f8c43a
cris.virtualsource.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
dc.abstract.enOxidation processes affect proteins from various molecular pathways and are crucial for wild boar meat quality, shelf life and human health. This study investigated the effects of different storage methods on the formation and composition of oxygen-induced protein aggregates in the muscles of European wild boar (Sus scrofa scrofa). Vacuum packaging (VAC), modified atmosphere packaging (MAP) and dry-ageing (DA) were compared over a 21-day storage period. The results showed significant differences in protein aggregation depending on the method and storage time. The most intense protein aggregation occurred in the MAP (80 % O2), while air DA (20.9 % O2) resulted in intermediate levels of protein aggregation. Crucial myofibrillar proteins involved in aggregate formation were titin, myosin isoforms (MYH1, MYH2 and MYH7) and nebulin, which were cross-linked with small sarcoplasmic enzymes, such as muscle creatine kinase, isocitrate dehydrogenase and ATPase 1. High‑oxygen storage conditions also promoted the oxidation of ATP synthase, beta-enolase 3, ADP/ATP translocase and myoglobin.
dc.affiliationWydział Nauk o Żywności i Żywieniu
dc.affiliation.instituteKatedra Technologii Mięsa
dc.contributor.authorKasałka-Czarna, Natalia
dc.contributor.authorStachniuk, Anna
dc.contributor.authorFornal, Emilia
dc.contributor.authorMontowska, Magdalena
dc.date.access2024-11-14
dc.date.accessioned2024-11-14T11:30:06Z
dc.date.available2024-11-14T11:30:06Z
dc.date.copyright2024-10-31
dc.date.issued2025
dc.description.accesstimeat_publication
dc.description.bibliographyil., bibliogr.
dc.description.financepublication_nocost
dc.description.financecost0,00
dc.description.if8,5
dc.description.number3
dc.description.points200
dc.description.versionfinal_published
dc.description.volume464
dc.identifier.doi10.1016/j.foodchem.2024.141774
dc.identifier.issn0308-8146
dc.identifier.urihttps://sciencerep.up.poznan.pl/handle/item/2015
dc.languageen
dc.relation.ispartofFood Chemistry
dc.relation.pagesart. 141774
dc.rightsCC-BY
dc.sciencecloudsend
dc.share.typeOPEN_JOURNAL
dc.subject.enwild boar
dc.subject.enmeat storage
dc.subject.enVAC
dc.subject.enMAP
dc.subject.endry-ageing
dc.subject.enproteomics
dc.subject.enprotein aggregation
dc.subject.enLC-MS/MS
dc.titleProteomic analysis of wild boar meat: Effect of storage method and time on muscle protein stability
dc.typeJournalArticle
dspace.entity.typePublication
oaire.citation.volume464