Changes in the $Ca^{2+}-,\;Mg^{2+}-dependent$ Adenosine Triphosphatase Activity and Ultrastructure of Marine Fishes by Partial Freezing -I. Denaturation of Yellowtail Myofibrillar ATPase During Cold Storage-

해산어의 부분동결에 의한 $Ca^{2+}-,\;Mg^{2+}-dependent$ Adenosine Triphosphatase 활성 및 근섬유의 미세구조의 변화 -I. 저온저장에 의한 방어 근원섬유 단백질의 변성-

  • Choi, Kyoung-Ho (Dept. of Food Science and Nutrition, Hyosung Women's University) ;
  • Park, Chan-Sung (Dept. Food Science, Taegu Oriental Medical College)
  • 최경호 (효성여자대학교 식품영양학과) ;
  • 박찬성 (대구한의과대학 식품과학과)
  • Published : 1989.03.01

Abstract

Myofibrillar protein(myofibil) was prepared from Yellowtail fish (Seriola quinqueradiata), and then, it was stored at $0^{\circ}C$(ice-cooling), $-3.5^{\circ}C$(partial freezing) and $-20^{\circ}C$(freezing). Another myofibrils were prepared from the fish stored with ice-cooling, partial freezing and freezing for a week as the maximum. Denaturation of muscle protein during the storage was investigated by the measurement of $Ca^{2+}-$ and $Mg^{2+}-ATPase$ activity. Specific activity of $Ca^{2+}-\;and\;Mg^{2+}-ATPase$ associated with Yellowtail myofibrils was 0.155 and $0.149\;{\mu}\;mole$ Pi/min/mg of protein, respectively, before storgae. ATPase activity of myofibils did not show any significant difference between $0^{\circ}C$ and $-3.5^{\circ}C$ whereas it was decreased faster at $-20^{\circ}C$ than at $0^{\circ}C$ or $-3.5^{\circ}C$. ATPase activity of myofibirls extracted from the fish stored for a week was 1.2-1.8 times higher than myofibils stored with ice-cooling or partial freezing while it was 2.5-3 times higher than that with freezing. Apparent denaturation constant of $Ca^{2+}-ATPase$ of myofibrils was between 0.48-0.65, and it was 2-3 times higher than that of $Mg^{2+}-ATPase$. The constant of myofibrils extracted from the fish did not show significant difference between $Ca^{2+}-\;and\;Mg^{2+}-ATPase$.

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