Simple item page
 

Comparative proteomic and genetic analysis of the authenticity of collagen preparations

cris.virtual.author-orcid0000-0002-6331-5726
cris.virtual.author-orcid0000-0002-5646-8759
cris.virtual.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtual.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtual.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtual.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtualsource.author-orcid6b8ff0a0-7556-4635-ae2c-064721f8c43a
cris.virtualsource.author-orcid837eac30-6f77-4b6f-bb01-386975edb99a
cris.virtualsource.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtualsource.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtualsource.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtualsource.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
dc.abstract.enCollagen and gelatine have many applications in the food and pharmaceutical industries. The diversity of their sources raises concerns among consumers and regulatory bodies regarding the authenticity of the products on the market, especially from religious, health and economic perspectives. In this study, commercially processed collagen and gelatine powders were examined using both non-targeted liquid chromatography–high resolution quadrupole time-of-flight tandem mass spectrometry (LC-HR-Q-TOF-MS/MS) and real-time polymerase chain reaction (rt-PCR) for the nuclear myostatin and PLAG1 genes using TaqMan probes. Only six samples yielded a sufficient concentration of good-quality DNA for use in real-time PCR with the universal mammalian myostatin marker. Proteomic analysis enabled the identification of processing-stable markers specific to connective tissue proteins of a given species – for collagen subunits (alpha chains of collagen types I, III, VI, IX and XIV) and non-collagenous proteins (decorin, osteoglycin, prolargin, asporin, fibrillin, matrilin, anchorin, chondroadherin, and calsequestrin). Among collagen subunits suitable for authenticity testing were specific to Sus scrofa COL6A1, COL6A3 COL14A1; Gallus gallus COL6A1, COL6A3 and COL9A1; Pangasianodon hypophthalmus COL1A1B; and Gadus morhua COL1A1A and COL1A2. The results highlight better performance and sensitivity of the proteomic method.
dc.affiliationWydział Nauk o Żywności i Żywieniu
dc.affiliation.instituteKatedra Technologii Mięsa
dc.contributor.authorMontowska, Magdalena
dc.contributor.authorMikołajczak, Beata
dc.contributor.authorWielgosz, Alicja
dc.contributor.authorStachniuk, Anna
dc.contributor.authorAdenuga, Bukola M.
dc.contributor.authorFornal, Emilia
dc.date.accessioned2025-07-01T09:03:14Z
dc.date.available2025-07-01T09:03:14Z
dc.date.issued2025
dc.description.bibliographyil., bibliogr.
dc.description.financepublication_nocost
dc.description.financecost0,00
dc.description.if4,6
dc.description.numberSeptember 2025
dc.description.points100
dc.description.volume145
dc.identifier.doi10.1016/j.jfca.2025.107827
dc.identifier.eissn1096-0481
dc.identifier.issn0889-1575
dc.identifier.urihttps://sciencerep.up.poznan.pl/handle/item/3793
dc.languageen
dc.pbn.affiliationfood and nutrition technology
dc.relation.ispartofJournal of Food Composition and Analysis
dc.relation.pagesart. 107827
dc.relation.projectNational Science Centre, Poland, project number 2020/37/B/NZ9/00082.
dc.rightsClosedAccess
dc.sciencecloudsend
dc.subject.enfood authentication
dc.subject.enconnective tissue
dc.subject.encollagen
dc.subject.ennon-collagenous proteins
dc.subject.enpeptide markers
dc.subject.enmyostatin gene
dc.subject.enLC-MS
dc.subject.enRt-PCR
dc.titleComparative proteomic and genetic analysis of the authenticity of collagen preparations
dc.typeJournalArticle
dspace.entity.typePublication
oaire.citation.volume145
project.funder.nameNational Science Centre, Poland, project number 2020/37/B/NZ9/00082.