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

Chicken collagen is a promising raw material source for the production gelatins and hydrolysates. These can be prepared biotechnologically using proteolytic enzymes. By choosing the appropriate process conditions, such changes can be achieved at the molecular level of collagen, making it possible to prepare gelatins with targeted properties for advanced cosmetic, pharmaceutical, medical, or food applications. The present research aims to investigate model samples of chicken gelatins, focusing on: (i) antioxidant activity using 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2-azinobis-3-etylbenzotiazolin-6-sulfonic acid (ABTS); (ii) the distribution of molecular weights via gel permeation chromatography with refractometric detection (GPC-RID); (iii) functional groups and the configuration of polypeptide chains related to molecular-level properties using Fourier transform infrared spectroscopy (FTIR); (iv) the microbiological populations on sabouraud dextrose agar (SDA), plate count agar (PCA), tryptic soy agar (TSA), and violet red bile lactose (VRBL) using the matrix-assisted laser desorption ionization (MALDI) method. Antioxidant activity towards ABTS radicals was more than 80%; activity towards DPPH radicals was more than 69%. The molecular weights of all gelatin samples showed typical α-, β-, and γ-chains. FTIR analysis confirmed that chicken gelatins all contain typical vibrational regions for collagen cleavage products, Amides A and B, and Amides I, II, and III, at characteristic wavenumbers. A microbiological analysis of the prepared samples showed no undesirable bacteria that would limit advanced applications of the prepared products. Chicken gelatins represent a promising alternative to products made from standard collagen tissues of terrestrial animals.

• Keywords
• antioxidant activity, biotechnology, functional groups, gelatin, microbial population, molecular weight,
• MeSH
• Agar MeSH
• Amides MeSH
• Antioxidants MeSH
• Benzothiazoles * MeSH
• Biphenyl Compounds * MeSH
• Poultry * MeSH
• Collagen MeSH
• Chickens MeSH
• Sulfonic Acids * MeSH
• Gelatin * MeSH
• Animals MeSH
• Check Tag
• Animals MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid MeSH Browser
• Agar MeSH
• Amides MeSH
• Antioxidants MeSH
• Benzothiazoles * MeSH
• Biphenyl Compounds * MeSH
• biphenyl MeSH Browser
• Collagen MeSH
• Sulfonic Acids * MeSH
• Gelatin * MeSH