Changes in the $Ca^{2+}$-, $Mg^{2+}$- dependent Adenosine Triphosphatase Activity and Ultrastructure of Marine Fishes by Partial Freezing II. Changes in ATPase Activity of Yellowtail Actomyosin during Cold Storage

해산어의 부분동결에 의한 $Ca^{2+}$-, $Mg^{2+}$- dependent Adenosine Triphosphatase 활성 및 근섬유의 미세구조 변화 II. 저온저장에 의한 방어 Actomyosin ATPase의 활성변화

  • 박찬성 (대구한의과학대학 식품과학과) ;
  • 최경호 (효성대학교 식품영양학과)
  • Published : 1990.08.01


Actomyosine prepared from Yellowtail fish(seriola quinqueradiata) were stored at $0^{\circ}C$(ice-cooling) -3.5$^{\circ}C$(partial freeaing) and -2$0^{\circ}C$(freezing) Another actomyosin samples were prepared from the fish previously stored at the temperatures for a week as the maximum .Remaining activity of {{{{ {Ca }^{2+ } }}}}-and {{{{ {Mg }^{2+ } }}}}- dependent adenosine triphosphatase(ATPase) activity was measured fronm the actomyosin preparations. Specific activity of {{{{ {Mg }^{2+ } }}}}-ATPase of actomy-osin before storagew was 0.253$\mu$ mole pi/min/mg of protein and it was 1.5 times higher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. The enzyme activities were markedly decreased during early period of storage. However no significant differences in the enzyme activity were revealed among the samples stored at different temperature. The enzyme of actomyosin prepared from the fish previously stored at the temperatures for a week revealed an acitivity of 2-3 times higher than that of freezing. Apparent denaturation constant of {{{{ {Mg }^{2+ } }}}} -ATPase of actomyosin was between 0.810-1.139 per day and it was about 1.5 times hgiher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. But the constant of {{{{ {Mg }^{2+ } }}}} ATPase of actomyosin extracted from the fist stored for a week at each temperature was between 0.176-0.356 per day. This constant was 4 times higher than that of {{{{ {Ca }^{2+ } }}}}- ATPase in frozen stored fish. It was presumed from these results that denaturation of ATPase is largely accorded to the structural changes of actomyosin.