A vast sum of fish waste is being annually discarded by marine fishing industries imposing serious environmental pollution concerns. However, these aquatic discarded matters are captivating sources of collagen, a fibrous protein with eminent social and economic relevance. Collagen is conventionally recovered using outdated complex processes requiring many reagents, multiple steps, and extended periods. Hereupon, the current project is the first work on the isolation of Seabass fish scales (FSC) type-I collagen, with preserved secondary and triple helical structures of the native collagen, developing a simple, green, cost-effective, and eco-friendly methodology, utilizing sustainable natural deep eutectic solvents (NADES)-assisted ultrasonication (US) technical route. The operational conditions were optimized based on the one-factor-at-a-time modeling to maximize the yield with no alteration of collagen integrity. Recorded data confirmed type-I collagen with preserved triple helix integrity and thermal stability, improved bio-functionalities, in vitro fibril formation, and functional performances. Finally, the in vitro hemolysis and cytotoxicity tests confirmed the extracted collagens biocompatibility, demonstrating the feasibility of Seabass FSC waste and a NADES-coupled US brief process (20 min) to establish a more sustainable eco-friendly pathway to isolate high-quality type I-collagen, as an attempt to rise industries awareness about wastes valorization within the scheme of circular economy.
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http://dx.doi.org/10.1016/j.ijbiomac.2025.140296 | DOI Listing |
Int J Biol Macromol
January 2025
College of Chemistry and Chemical Engineering, Qingdao University of Science and Technology, Qingdao 266042, China. Electronic address:
A vast sum of fish waste is being annually discarded by marine fishing industries imposing serious environmental pollution concerns. However, these aquatic discarded matters are captivating sources of collagen, a fibrous protein with eminent social and economic relevance. Collagen is conventionally recovered using outdated complex processes requiring many reagents, multiple steps, and extended periods.
View Article and Find Full Text PDFThis study aimed to develop novel hydrogels using polycaprolactone (PCL), nano-silver (Ag), and linalool (Lin) to address the challenge of increasing antimicrobial resistance in healing infected wounds. The hydrogels' morphological properties, in vitro release profiles, antibacterial efficacy, and safety were investigated. Hydrogels were prepared from PCL/Ag, PCL/Lin, and PCL/Ag/Lin formulations and applied to infected wounds.
View Article and Find Full Text PDFPolymers (Basel)
January 2025
Dipartimento di Chimica "G. Ciamician", Alma Mater Studiorum-Università di Bologna, Via F. Selmi 2, 40126 Bologna, Italy.
The development of greener substitutes for plastics is gaining massive importance in today's society. This also involves the medical field, where disposable materials are used to grant sterility. Here, a novel protocol using only a water-based solvent for the preparation of bio-based composite foams of actual β-chitin and collagen type I is presented.
View Article and Find Full Text PDFJ Clin Med
January 2025
Department of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Sklodowska University, 20-614 Lublin, Poland.
Limb lengthening and deformity correction techniques, particularly distraction osteogenesis, have significantly evolved in pediatric orthopedics. This study examines the temporal changes of key biochemical markers-vascular endothelial growth factor (VEGF), fibroblast growth factor 1 (FGF-1), and the propeptide of type I collagen (P1NP)-during the limb lengthening process. Twenty pediatric patients (aged 13-16) underwent distraction osteogenesis using the Circular Hexapod External Fixator.
View Article and Find Full Text PDFInt J Mol Sci
January 2025
Department of Anatomy and Neurobiology, Faculty of Medicine, Kindai University, Osakasayama 589-8511, Japan.
Collagen I is the most abundant type of intramuscular collagen. Lysyl oxidase promotes collagen cross-link formation, which helps stabilize the extracellular matrix. Furthermore, matrix metalloproteinases, responsible for collagen degradation, maintain typical muscle structure and function through remodeling.
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