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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10404 - Polymer science

Result continuities

  • Project

  • 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