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Collagen Hydrolysates from Animal By-Products in Topical Cosmetic Formulations
P. Egner, J. Pavlačková, J. Sedlaříková, L. Matošková, P. Mokrejš, M. Janalíková
Language English Country Switzerland
Document type Journal Article
Grant support
IGA/FT/2025/006
Internal Grant Agency of the Faculty of Technology, Tomas Bata University in Zlín
NLK
Free Medical Journals
from 2000
Freely Accessible Science Journals
from 2000
PubMed Central
from 2007
Europe PubMed Central
from 2007
ProQuest Central
from 2000-03-01
Open Access Digital Library
from 2000-01-01
Open Access Digital Library
from 2007-01-01
Health & Medicine (ProQuest)
from 2000-03-01
ROAD: Directory of Open Access Scholarly Resources
from 2000
PubMed
40141417
DOI
10.3390/ijms26062776
Knihovny.cz E-resources
- MeSH
- Antioxidants chemistry pharmacology MeSH
- Administration, Topical MeSH
- Carps metabolism MeSH
- Collagen * chemistry MeSH
- Cosmetics * chemistry MeSH
- Chickens MeSH
- Skin metabolism drug effects MeSH
- Humans MeSH
- Protein Hydrolysates * chemistry pharmacology MeSH
- Skin Aging drug effects MeSH
- Viscosity MeSH
- Deer MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
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.
References provided by Crossref.org
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