Cooking resistant edible crickets-specific peptides for authenticity testing of meat products

cris.lastimport.scopus2025-10-23T07:00:30Z
cris.virtual.author-orcid0000-0002-6331-5726
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cris.virtualsource.author-orcid6b8ff0a0-7556-4635-ae2c-064721f8c43a
cris.virtualsource.author-orcid096e41a9-6ac3-4aa4-9495-6e2699f7f3a3
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dc.abstract.enAs consumer and manufacturer interests in edible insects and processed food with added insects are increasing, new possibilities for detecting edible insect proteins in processed foods have become increasingly important. In the present study, a proteomic strategy was applied to identify insect proteins and thermostable house cricket-specific (Acheta domesticus) peptide markers. To determine the limit of detection (LOD) for house cricket proteins, cooked meatballs containing house cricket protein powder (CP) as a partial pork substitute were investigated. The final concentration of CP ranged from 0.8% to 7.6%. The LODs for tropomyosin 1 and translational elongation factor-2 were 0.8% (w/w), whereas for apolipophorin-III it was 2.5% (w/w). Eight heat-resistant peptides unique to the family Grillidae (true crickets) and four peptides unique to the Acheta domesticus were identified. The results suggest that selected cricket-specific and processing-resistant peptide markers have potential utility in the authentication of the cricket formulations used in meat products. However, this has to be confirmed on different heavily processed meat products.
dc.affiliationWydział Nauk o Żywności i Żywieniu
dc.affiliation.instituteKatedra Technologii Mięsa
dc.contributor.authorMontowska, Magdalena
dc.contributor.authorSzymczak, Aleksandra
dc.contributor.authorSpychaj, Anita
dc.contributor.authorFornal, Emilia
dc.date.accessioned2025-03-27T08:20:28Z
dc.date.available2025-03-27T08:20:28Z
dc.date.issued2025
dc.description.abstract<jats:title>Abstract</jats:title> <jats:p>As consumer and manufacturer interests in edible insects and processed food with added insects are increasing, new possibilities for detecting edible insect proteins in processed foods have become increasingly important. In the present study, a proteomic strategy was applied to identify insect proteins and thermostable house cricket-specific (<jats:italic>Acheta domesticus</jats:italic>) peptide markers. To determine the limit of detection (LOD) for house cricket proteins, cooked meatballs containing house cricket protein powder (CP) as a partial pork substitute were investigated. The final concentration of CP ranged from 0.8% to 7.6%. The LODs for tropomyosin 1 and translational elongation factor-2 were 0.8% (w/w), whereas for apolipophorin-III it was 2.5% (w/w). Eight heat-resistant peptides unique to the family <jats:italic>Grillidae</jats:italic> (true crickets) and four peptides unique to the <jats:italic>Acheta domesticus</jats:italic> were identified. The results suggest that selected cricket-specific and processing-resistant peptide markers have potential utility in the authentication of the cricket formulations used in meat products. However, this has to be confirmed on different heavily processed meat products.</jats:p>
dc.description.bibliographyil., bibliogr.
dc.description.financepublication_nocost
dc.description.financecost0,00
dc.description.if4,7
dc.description.number2
dc.description.points70
dc.description.volume11
dc.identifier.doi10.1163/23524588-00001220
dc.identifier.eissn2352-4588
dc.identifier.issn2352-4588
dc.identifier.urihttps://sciencerep.up.poznan.pl/handle/item/2627
dc.languageen
dc.pbn.affiliationfood and nutrition technology
dc.relation.ispartofJournal of Insects as Food and Feed
dc.relation.pages343–352
dc.rightsClosedAccess
dc.sciencecloudsend
dc.subject.enAcheta domesticus
dc.subject.encricket protein
dc.subject.enpeptide markers
dc.subject.enUHPLC-QTOF-MS/MS
dc.subject.plAcheta domesticus
dc.subject.plbiałko ze świerszczy
dc.subject.plmarkery peptydowe
dc.subject.plUHPLC-QTOF-MS/MS
dc.titleCooking resistant edible crickets-specific peptides for authenticity testing of meat products
dc.typeJournalArticle
dspace.entity.typePublication
oaire.citation.issue2
oaire.citation.volume11