Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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Isolation and characterization of acid-soluble bluefin tuna (Thunnus orientalis) skin collagen

  • Tanaka, Teruyoshi (Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University) ;
  • Takahashi, Kenji (Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University) ;
  • Tsubaki, Kazufumi (ADEKA Corporation) ;
  • Hirata, Maika (Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University) ;
  • Yamamoto, Keiko (Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University) ;
  • Biswas, Amal (Aquaculture Research Institute, Uragami Station, Kindai University) ;
  • Moriyama, Tatsuya (Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University) ;
  • Kawamura, Yukio (Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University)
  • Received : 2017.11.07
  • Accepted : 2018.01.17
  • Published : 2018.04.30
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Abstract

In this study, we isolated and characterized the acid-soluble skin collagen of Pacific bluefin tuna (PBT, Thunnus orientalis). The PBT skin collagen was composed of two ${\alpha}$ chains (${\alpha}1$ and ${\alpha}2$) and one ${\beta}$ chain. The denaturation temperature of PBT collagen was low although it was rich in proline and hydroxyproline. The primary structure of PBT skin collagen was almost identical to that of calf and salmon skin collagen; however, it differed with respect to the epitope recognition of the antibody against salmon type I collagen. These results suggest that the primary structure of skin collagen was highly conserved among animal species, although partial sequences that included the epitope structure differed among collagens.

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