This review provides a report on properties and recent advances in the application of collagen in cosmetics. Collagen is a structural protein found in animal organisms where it provides for the fundamental structural support. Most commonly it is extracted from mammalian and fish skin. Collagen has attracted significant academic interest as well as the attention of the cosmetic industry due to its interesting properties that include being a natural humectant and moisturizer for the skin. This review paper covers the biosynthesis of collagen, the sources of collagen used in the cosmetic industry, and the role played by this protein in cosmetics. Future aspects regarding applications of collagen-based materials in cosmetics have also been mentioned.
Acid soluble collagen (ASC) was extracted from Silver Carp fish skin. Collagen was dissolved in acetic acid at varying concentrations and its rheological properties were studied. Steady shear flow properties of collagen solutions at concentrations of 5 and 10 mg/mL were characterized using rheometry at 20 °C. Collagen solutions were irradiated with UV light (wavelength 254 nm) for up to 2 h and rheological properties were measured. All the collagen solutions showed a shear-thinning flow behavior. A constant viscosity region was observed after 1 h of UV irradiation, which showed that collagen molecules were fully denatured. A short treatment with collagen solution by UV (ultraviolet) light led to an increase in viscosity; however, the denaturation temperature of UV-irradiated collagen decreased. Depending on the time of UV treatment, collagen extracted from Silver Carp fish skin may undergo physical crosslinking or photodegradation. Physically crosslinked collagen may find applications in functional food, cosmetic, biomedical, and pharmaceutical industries.
Collagen films are widely used as adhesives in medicine and cosmetology. However, its properties require modification. In this work, the influence of salicin on the properties of collagen solution and films was studied. Collagen was extracted from silver carp skin. The rheological properties of collagen solutions with and without salicin were characterized by steady shear tests. Thin collagen films were prepared by solvent evaporation. The structure of films was researched using infrared spectroscopy. The surface properties of films were investigated using Atomic Force Microscopy (AFM). Mechanical properties were measured as well. It was found that the addition of salicin modified the roughness of collagen films and their mechanical and rheological properties. The above-mentioned parameters are very important in potential applications of collagen films containing salicin.
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