Bioconversion of Eel Skin Waste into Valuable Collagen: Isolation, Spectral Characterization, and Biocompatibility Assessment

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Abstract The current investigation was carried out to evaluate the structural and cell proliferation capability of pike conger eel collagen derived by acid and enzymatic extraction methods. The recovery yield of pepsin-soluble collagen (PSC) (40.65%) was significantly higher (p<0.05) than acid-soluble collagen (ASC) (29.9%) on a dry weight basis. In terms of molecular weight pattern, α1 and α2 bands of extracted collagen occurred to be 130KDa and 112KDa, respectively, and were confirmed to have a Type 1 structure. The presence of characteristic peaks of amide bands in Fourier transform infrared spectra (FTIR) and the d value of 12.28 Å and 11.37 Å in X-ray diffraction (XRD) revealed no significant changes in the highly ordered, intact triple helical structure of collagen through pepsin digestion. The higher thermal stability with a denaturation temperature of 33.3°C for ASC and 35.1°C for PSC was well documented in the differential scanning calorimetry (DSC) curve, which showed a substantial correlation with the findings of the imino acid content of both ASC and PSC collagen (203.5 ± 1.06 and 216.81 ± 0.32 residues/1000g respectively). In addition, the nontoxic behavior of isolated collagen samples to L929 fibroblast cell lines emphasized the possible utilization of pike conger eel skin as a safe source of thermally stable collagen.
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Bioconversion of Eel Skin Waste into Valuable Collagen: Isolation, Spectral Characterization, and Biocompatibility Assessment | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Research Article Bioconversion of Eel Skin Waste into Valuable Collagen: Isolation, Spectral Characterization, and Biocompatibility Assessment Fathima Asharaf, Radhika Rajasree S.R, Roopa Rajan This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-3704353/v1 This work is licensed under a CC BY 4.0 License Status: Published Journal Publication published 04 Apr, 2024 Read the published version in Waste and Biomass Valorization → Version 1 posted 5 You are reading this latest preprint version Abstract The current investigation was carried out to evaluate the structural and cell proliferation capability of pike conger eel collagen derived by acid and enzymatic extraction methods. The recovery yield of pepsin-soluble collagen (PSC) (40.65%) was significantly higher (p<0.05) than acid-soluble collagen (ASC) (29.9%) on a dry weight basis. In terms of molecular weight pattern, α1 and α2 bands of extracted collagen occurred to be 130KDa and 112KDa, respectively, and were confirmed to have a Type 1 structure. The presence of characteristic peaks of amide bands in Fourier transform infrared spectra (FTIR) and the d value of 12.28 Å and 11.37 Å in X-ray diffraction (XRD) revealed no significant changes in the highly ordered, intact triple helical structure of collagen through pepsin digestion. The higher thermal stability with a denaturation temperature of 33.3°C for ASC and 35.1°C for PSC was well documented in the differential scanning calorimetry (DSC) curve, which showed a substantial correlation with the findings of the imino acid content of both ASC and PSC collagen (203.5 ± 1.06 and 216.81 ± 0.32 residues/1000g respectively). In addition, the nontoxic behavior of isolated collagen samples to L929 fibroblast cell lines emphasized the possible utilization of pike conger eel skin as a safe source of thermally stable collagen. Muraenesox bagio ASC PSC Thermal stability Solubility Biocompatibility Full Text Cite Share Download PDF Status: Published Journal Publication published 04 Apr, 2024 Read the published version in Waste and Biomass Valorization → Version 1 posted Reviewers agreed at journal 27 Jan, 2024 Reviewers invited by journal 10 Jan, 2024 Editor invited by journal 06 Jan, 2024 Editor assigned by journal 04 Dec, 2023 First submitted to journal 03 Dec, 2023 You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. 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