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Processing and Physicochemical Properties of Collagen from Yellowfin Tuna (Thunnus albacares) Abdominal Skin

황다랑어 복부 껍질을 이용한 콜라겐의 제조 및 물리화학적 특성 해석

  • Yoo, Sung-Jae (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Cho, Sueng-Mock (Research Division for Food Industry Promotion, Korea Food Research Institute) ;
  • Woo, Jin-Wook (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kim, Sang-Ho (Song-Ho Food Development Co.) ;
  • Han, Yoo-Na (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Ahn, Ju-Ryun (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kim, Su-Yeon (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kim, Tae-Wan (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kim, Seon-Bong (Department of Food Science and Technology/Institute of Food Science, Pukyong National University)
  • 유승재 (부경대학교 식품공학과/식품연구소) ;
  • 조승목 (한국식품연구원) ;
  • 우진욱 (부경대학교 식품공학과/식품연구소) ;
  • 김상호 (송호식품개발(주)) ;
  • 한유나 (부경대학교 식품공학과/식품연구소) ;
  • 안주련 (부경대학교 식품공학과/식품연구소) ;
  • 김수연 (부경대학교 식품공학과/식품연구소) ;
  • 김태완 (부경대학교 식품공학과/식품연구소) ;
  • 김선봉 (부경대학교 식품공학과/식품연구소)
  • Published : 2008.12.31

Abstract

Processing of collagen from yellowfin tuna (Thunnus albacares) abdominal skins was optimized by response surface methodology and central composite design. The values of independent variables at optimal conditions were NaOH concentration: 0.5 N, NaOH treatment time: 36.2 hr, pepsin concentration: 1:4.9 ratio (0.245%, w/v), and digestion time: 48.1 hr, respectively. The collagen content estimated under optimal conditions was 33.1%, and the actual experimental collagen content was 32.3%. Physicochemical properties of collagen from yellowfin tuna abdominal skin were investigated by amino acids analysis, SDS-PAGE, FT-IR, viscosity and denaturation temperature. Amino acids content of the collagen was 21.0%. SDS-PAGE pattern of the collagen showed two different $\alpha$-chain (${\alpha}_1$- and ${\alpha}_2$- chain), $\beta$-component and $\gamma$-component. The spectrum of FT-IR of the collagen showed wavenumber at 3,434, 1,650, 1,542 and $1,235\;cm^{-1}$ representing the regions of amide A, I, II and III, respectively. Relative viscosity of the collagen decreased continuously on heating up to $32^{\circ}C$, and the rate of decrease was retarded in the temperature range of $35-50^{\circ}C$. Denaturation temperature (Td) of the collagen solution (0.06%, w/v) was $31^{\circ}C$ and was lower than calf skin collagen ($35^{\circ}C$).

Keywords

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