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Characterization of Collagen from Sakhalin Taimen Skin as Useful Biomass

Takeshi Nagai1,2,3*orcid tiny, Masataka Saito4, Yasuhiro Tanoue5, Norihisa Kai6 and Nobutaka Suzuki7

1Graduate School of Agricultural Sciences, Yamagata University, 9978555 Yamagata, Japan

2The United Graduate School of Agricultural Sciences, Iwate University, 0208550 Iwate, Japan

3Graduate School, Prince of Songkla University, 90112 Songkhla, Thailand

4Kagawa Nutrition University, 3500288 Saitama, Japan

5Department of Food Science and Technology, National Fisheries University, 7596595 Yamaguchi, Japan

6Department of Integrated Science and Technology, Oita University, 8701192 Oita, Japan

7Nagoya Research Institute, 4701131 Aichi, Japan

Article history:

Received: 7 April 2020

Accepted: 17 December 2020

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Key words:

Sakhalin taimen skin, useful biomass, collagen, succinylation, improvement of functional property


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.

*Corresponding author:

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