Collagen hydrolysates from animal by-products in topical cosmetic formulations
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F70883521%3A28110%2F25%3A63594718" target="_blank" >RIV/70883521:28110/25:63594718 - isvavai.cz</a>
Result on the web
<a href="https://www.mdpi.com/1422-0067/26/6/2776" target="_blank" >https://www.mdpi.com/1422-0067/26/6/2776</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms26062776" target="_blank" >10.3390/ijms26062776</a>
Alternative languages
Result language
angličtina
Original language name
Collagen hydrolysates from animal by-products in topical cosmetic formulations
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10404 - Polymer science
Result continuities
Project
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Continuities
S - Specificky vyzkum na vysokych skolach
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal of Molecular Sciences
ISSN
1661-6596
e-ISSN
1422-0067
Volume of the periodical
26
Issue of the periodical within the volume
6
Country of publishing house
CH - SWITZERLAND
Number of pages
26
Pages from-to
nestránkováno
UT code for WoS article
001452543300001
EID of the result in the Scopus database
2-s2.0-105002284098