Abstract

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.

Highlights

  • Collagen is a widely used material in the cosmetics, biomedicine, and food industries

  • The results showed that the solution of collagen extracted from the Silver Carp fish skin used in this study is a rheologically stable fluid in which the rheological properties do not change over time

  • UV-treatment of collagen solution leads to the increase of the viscosity in the beginning, but after prolonged UV-treatment a large reduction of the apparent viscosity value was observed showing that collagen molecules are fully denatured after one hour of UV treatment

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Summary

Introduction

Collagen is a widely used material in the cosmetics, biomedicine, and food industries. Native collagen is sensitive to high temperatures and UV treatment. UV irradiation of collagen molecules leads to several photochemical reactions [1,2,3,4,5,6,7,8,9,10,11]. The UV treatment of the collagen materials may influence the mechanical properties of the final collagen products [8,9,10]. There are some interesting studies regarding collagen alterations by UV irradiation, the molecular mechanisms behind the influence of UV light on collagen are still unknown. It has been shown that aromatic amino acids play the main role in the absorption of UV light by collagen molecules [11]

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