Characterization of Collagen from Sakhalin Taimen Skin as Useful Biomass

Research background. Animal collagen has been widely utilized in foods, cosmetics and biomedical fields. The non-edible parts, such as fish skin and bones, are generated during cooking processes. Most of them are currently discarded as waste, although the nutritional values of the skins and bones ar...

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Bibliographic Details
Published inFood Technology and Biotechnology Vol. 58; no. 4; pp. 445 - 454
Main Authors Nagai, Takeshi, Saito, Masataka, Tanoue, Yasuhiro, Kai, Norihisa, Suzuki, Nobutaka
Format Journal Article
LanguageEnglish
Published Croatia Faculty of Food Technology and Biotechnology - University of Zagreb 01.12.2020
Sveuciliste U Zagrebu
Sveuciliste u Zagrebu, Prehramheno-Biotehnoloski Fakultet
University of Zagreb Faculty of Food Technology and Biotechnology
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Summary:Research background. Animal collagen has been widely utilized in foods, cosmetics and biomedical fields. The non-edible parts, such as fish skin and bones, are generated during cooking processes. Most of them are currently discarded as waste, although the nutritional values of the skins and bones are high. It needs to utilize the non-edible parts for the reduction of environmental impact, as it may be one of source of environmental pollution. Experimental approach. Collagen was prepared from Sakhalin taimen skins as wastes generated during cooking processes. Next, the colour, SDS-polyacrylamide gel electrophoresis, ultraviolet absorption, subunit composition, amino acid composition, denaturation temperature, and attenuated total reflectance-Fourier transform infrared spectroscopy analysis were conducted to explore the properties of the collagen. Lastly, it tried to improve the functional properties of the collagen using chemical modification technique for future applications. Results and conclusions. Cold acetone treatment made it possible to easily remove the fats and pigments from skins. The odorless and pure-white collagen was obtained with high-yield. The α3 chain did not exist in the collagen. Sakhalin taimen skin collagen had rich α-helix and low β-sheet structures. Succinylation caused the secondary structural changes of the collagen molecule. Moreover, succinylation made it possible not only to increase the viscosity of collagen solution and but also to improve the solubility of collagen in the physiological conditions around pH=6. Novelty and scientific contribution. This finding was the first report on the absence of the α3 chain in Salmonid fish skin collagens. The succinylated collagen from Sakhalin taimen skin as useful biomass has potential to utilize in foods, cosmetics, and its related industries.
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AUTHORS’ CONTRIBUTION
This work was carried out in collaboration among all authors. T. Nagai took part in designing and performing experiments, data collection, data analysis and interpretation, drafting the manuscript, critical revision and final approval of the version to be published. M. Saito, Y. Tanoue, N. Kai and N. Suzuki contributed to data interpretation.
ISSN:1330-9862
1334-2606
DOI:10.17113/ftb.58.04.20.6734