Structural and molecular characterization of collagen-type I extracted from lamb feet

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dc.authoridKumcuoglu, Seher/0000-0002-3663-2881
dc.authoridKaplan Turkoz, Burcu/0000-0003-3040-3321
dc.authorscopusid57483443500
dc.authorscopusid57924592100
dc.authorscopusid57923958500
dc.authorscopusid15765552500
dc.authorscopusid55968275900
dc.authorscopusid57298408800
dc.authorscopusid57207929690
dc.authorwosidKumcuoglu, Seher/JVO-0252-2024
dc.contributor.authorAta, Özge
dc.contributor.authorBakar, Bahar
dc.contributor.authorKaplan Turkoz, Burcu
dc.contributor.authorKumcuoğlu, Seher
dc.contributor.authorAydoğdu, Yıldırım
dc.contributor.authorGümüştaş, Barış
dc.contributor.authorDinler Doğanay, Gizem
dc.date.accessioned2024-08-25T18:31:50Z
dc.date.available2024-08-25T18:31:50Z
dc.date.issued2023
dc.departmentEge Üniversitesien_US
dc.description.abstractThis study aimed to extract collagen-I from lamb feet (LF) and examine the effects of ultrasound treatment on the structural and molecular characteristics of the collagen. Compared to ultrasonic bath treatment and conventional extraction methods, ultrasonic probe (USP) treatment significantly increased the collagen content of the extract (p < 0.05). The electrophoretic profiles confirmed the presence of alpha- and beta-chains, indicating it as type I. Furthermore, X-ray diffraction, Fourier-transform infrared spectroscopy, and circular dichroism spectra analyses revealed that the extraction method did not adversely affect the triple helix structure of the collagen. Moreover, the fibrillar structure of the collagen samples was verified through scanning electron microscopy analyses. Notably, the LF collagen exhibited a high thermal denaturation temperature owing to its elevated imino acid content. The collagen samples exhibited high solubility in acidic pH but low solubility in high salt concentrations. The present findings signified that sonication with USP can effectively enhance the yield of collagen from LF without compromising its quality.en_US
dc.description.sponsorshipTrkiye Bilimsel ve Teknolojik Arascedil;timath;rma Kurumu [119O491]; Scientific and Technological Research Council of Turkey (TUBITAK); Ege University Planning and Monitoring Coordination of Organizational Development and Directorate of Library and Documentationen_US
dc.description.sponsorshipThis research was supported by the Scientific and Technological Research Council of Turkey (TUBITAK) Project No. 119O491. We are grateful to Ege University Planning and Monitoring Coordination of Organizational Development and Directorate of Library and Documentation for their support in editing and proofreading service of this study.en_US
dc.identifier.doi10.1111/1750-3841.16870
dc.identifier.issn0022-1147
dc.identifier.issn1750-3841
dc.identifier.pmid38051022en_US
dc.identifier.scopus2-s2.0-85178422070en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.urihttps://doi.org/10.1111/1750-3841.16870
dc.identifier.urihttps://hdl.handle.net/11454/100033
dc.identifier.wosWOS:001113813800001en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.relation.ispartofJournal of Food Scienceen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.snmz20240825_Gen_US
dc.subjectcharacterizationen_US
dc.subjectlamb feeten_US
dc.subjecttriple helixen_US
dc.subjecttype I collagenen_US
dc.subjectultrasound treatmenten_US
dc.subjectAcid-Soluble Collagenen_US
dc.subjectSkinen_US
dc.subjectBoneen_US
dc.subjectFooden_US
dc.titleStructural and molecular characterization of collagen-type I extracted from lamb feeten_US
dc.typeArticleen_US

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