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Valorization of Fish Waste: Isolation and Characterization of Acid- and Pepsin-Soluble Collagen from the Scales of Mediterranean Fish and Fabrication of Collagen-Based Nanofibrous Scaffolds

In search of alternative and sustainable sources of collagenous materials for biomedical applications, the scales of five Mediterranean fish species—fished in high tonnage in the Mediterranean region since they represent popular choices for the local diet—as well as those of the Atlantic salmon for...

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Autores principales: Tziveleka, Leto-Aikaterini, Kikionis, Stefanos, Karkatzoulis, Labros, Bethanis, Kostas, Roussis, Vassilios, Ioannou, Efstathia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9697972/
https://www.ncbi.nlm.nih.gov/pubmed/36354987
http://dx.doi.org/10.3390/md20110664
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author Tziveleka, Leto-Aikaterini
Kikionis, Stefanos
Karkatzoulis, Labros
Bethanis, Kostas
Roussis, Vassilios
Ioannou, Efstathia
author_facet Tziveleka, Leto-Aikaterini
Kikionis, Stefanos
Karkatzoulis, Labros
Bethanis, Kostas
Roussis, Vassilios
Ioannou, Efstathia
author_sort Tziveleka, Leto-Aikaterini
collection PubMed
description In search of alternative and sustainable sources of collagenous materials for biomedical applications, the scales of five Mediterranean fish species—fished in high tonnage in the Mediterranean region since they represent popular choices for the local diet—as well as those of the Atlantic salmon for comparison purposes, were comparatively studied for their acid- and pepsin-soluble collagen content. Fish scales that currently represent a discarded biomass of no value could be efficiently exploited for the production of a high added-value biomaterial. The isolated collagenous materials, which showed the typical electrophoretic patterns of type I collagen, were morphologically and physicochemically characterized. Using scanning electron microscopy the fibrous morphology of the isolated collagens was confirmed, while the hydroxyproline content, in conjunction with infrared spectroscopy and X-ray diffraction studies verified the characteristic for collagen amino acid profile and its secondary structure. The acid- and pepsin-soluble collagens isolated from the fish scales were blended with the bioactive sulfated marine polysaccharide ulvan and polyethylene oxide and electrospun to afford nanofibrous scaffolds that could find applications in the biomedical sector.
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spelling pubmed-96979722022-11-26 Valorization of Fish Waste: Isolation and Characterization of Acid- and Pepsin-Soluble Collagen from the Scales of Mediterranean Fish and Fabrication of Collagen-Based Nanofibrous Scaffolds Tziveleka, Leto-Aikaterini Kikionis, Stefanos Karkatzoulis, Labros Bethanis, Kostas Roussis, Vassilios Ioannou, Efstathia Mar Drugs Article In search of alternative and sustainable sources of collagenous materials for biomedical applications, the scales of five Mediterranean fish species—fished in high tonnage in the Mediterranean region since they represent popular choices for the local diet—as well as those of the Atlantic salmon for comparison purposes, were comparatively studied for their acid- and pepsin-soluble collagen content. Fish scales that currently represent a discarded biomass of no value could be efficiently exploited for the production of a high added-value biomaterial. The isolated collagenous materials, which showed the typical electrophoretic patterns of type I collagen, were morphologically and physicochemically characterized. Using scanning electron microscopy the fibrous morphology of the isolated collagens was confirmed, while the hydroxyproline content, in conjunction with infrared spectroscopy and X-ray diffraction studies verified the characteristic for collagen amino acid profile and its secondary structure. The acid- and pepsin-soluble collagens isolated from the fish scales were blended with the bioactive sulfated marine polysaccharide ulvan and polyethylene oxide and electrospun to afford nanofibrous scaffolds that could find applications in the biomedical sector. MDPI 2022-10-25 /pmc/articles/PMC9697972/ /pubmed/36354987 http://dx.doi.org/10.3390/md20110664 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Tziveleka, Leto-Aikaterini
Kikionis, Stefanos
Karkatzoulis, Labros
Bethanis, Kostas
Roussis, Vassilios
Ioannou, Efstathia
Valorization of Fish Waste: Isolation and Characterization of Acid- and Pepsin-Soluble Collagen from the Scales of Mediterranean Fish and Fabrication of Collagen-Based Nanofibrous Scaffolds
title Valorization of Fish Waste: Isolation and Characterization of Acid- and Pepsin-Soluble Collagen from the Scales of Mediterranean Fish and Fabrication of Collagen-Based Nanofibrous Scaffolds
title_full Valorization of Fish Waste: Isolation and Characterization of Acid- and Pepsin-Soluble Collagen from the Scales of Mediterranean Fish and Fabrication of Collagen-Based Nanofibrous Scaffolds
title_fullStr Valorization of Fish Waste: Isolation and Characterization of Acid- and Pepsin-Soluble Collagen from the Scales of Mediterranean Fish and Fabrication of Collagen-Based Nanofibrous Scaffolds
title_full_unstemmed Valorization of Fish Waste: Isolation and Characterization of Acid- and Pepsin-Soluble Collagen from the Scales of Mediterranean Fish and Fabrication of Collagen-Based Nanofibrous Scaffolds
title_short Valorization of Fish Waste: Isolation and Characterization of Acid- and Pepsin-Soluble Collagen from the Scales of Mediterranean Fish and Fabrication of Collagen-Based Nanofibrous Scaffolds
title_sort valorization of fish waste: isolation and characterization of acid- and pepsin-soluble collagen from the scales of mediterranean fish and fabrication of collagen-based nanofibrous scaffolds
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9697972/
https://www.ncbi.nlm.nih.gov/pubmed/36354987
http://dx.doi.org/10.3390/md20110664
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