The circular economy of animal by-products rich in collagen focuses on converting collagen into peptides with a defined molecular weight. Collagen hydrolysates prepared by biotechnological methods from chicken gizzards, deer tendons, and Cyprinus carpio skeletons can be an alternative source of collagen for cosmetic products that traditionally use bovine or porcine collagen hydrolysates. Collagen hydrolysates were characterized by antioxidant activity, surface tension, solution contact angle, and other parameters (dry weight, ash content, and solution clarity). Furthermore, the vibrational characterization of functional groups and their molecular weight was performed using the GPC-RID method. Subsequently, emulsion and gel cosmetic matrices were prepared with 0.5% and 1.5% collagen hydrolysates. Microbiological stability, organoleptic properties, and viscosity were investigated. Verification of the biophysical parameters of the topical formulations was performed in vivo on a group of volunteers by measuring skin hydration and pH and determining trans-epidermal water loss. Fish collagen hydrolysate was the most suitable for cosmetic applications in the parameters investigated. Moreover, it also effectively reduces wrinkles in the periorbital region when used in a gel matrix.

• Keywords
• animal by-products, antimicrobial effect, bioengineering methods, collagen hydrolysate, topical formulation, wrinkles,
• MeSH
• Antioxidants chemistry   pharmacology   MeSH
• Administration, Topical MeSH
• Emulsions chemistry   MeSH
• Carps MeSH
• Collagen * chemistry   pharmacology   MeSH
• Cosmetics * chemistry   pharmacology   MeSH
• Chickens MeSH
• Skin drug effects   MeSH
• Humans MeSH
• Swine MeSH
• Protein Hydrolysates * chemistry   pharmacology   MeSH
• Cattle MeSH
• Skin Aging drug effects   MeSH
• Animals MeSH
• Check Tag
• Humans MeSH
• Cattle MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Antioxidants MeSH
• Emulsions MeSH
• Collagen * MeSH
• Cosmetics * MeSH
• Protein Hydrolysates * MeSH

The application of biopolymer-based materials is increasing due to better sustainability and environmental protection properties. Gelatin fibers have a specific surface and high porosity, which is why their use in medicine and the food industry is being researched. This article explores the potential of centrifugal spinning to produce gelatin fibers. Gelatin for fiber preparation was obtained from a non-traditional source of collagen (chicken by-products) using a unique enzymatic process. The fiber quality was compared with those prepared from gelatins produced from traditional collagen tissues (porcine, bovine). The results showed that fibers cross-linked with glutaraldehyde vapor preserved their structure even in contact with water. Using a cross-linker controlled swelling ability and solubility while maintaining the fiber structure. On the contrary, uncross-linked gelatin fibers were water soluble due to a high surface-to-volume ratio, facilitating water penetration and dissolution. Scanning electron microscopy (SEM) provided a clearer picture of the morphology of gelatin fibers obtained by centrifugal spinning. Differences in the amount of bonding depending on the raw material used and the presence of a cross-linker were analyzed using Fourier transform infrared spectroscopy (FTIR). The overall results showed that chicken gelatin is a suitable alternative to gelatins from traditional sources and can be used for preparing food and pharmaceutical packaging and coatings, fibers, or bioprinting of 3D matrices.

• Keywords
• bioprinting, centrifugal spinning, chicken gelatin, enzymatic hydrolysis, fibers, functional groups, morphology, solubility, swelling,
• Publication type
• Journal Article MeSH