Freeze Denaturation of Squid Actomyosin

  • Lee Kang-Ho (Department of Food Science and Technology, Pukyong National University) ;
  • Ryu Hong-Soo (Department of Food and Life Science, Pukyong National University) ;
  • Cho Young-Je (Department of Food Science and Technology, Pukyong National University) ;
  • Jung Byung-Chun (Department of Food Science and Technology, Pukyong National University) ;
  • Hong Byung-Il (Department of Food Science and Technology, Pukyong National University) ;
  • Je Yoi-Kwon (Department of Food Technology, Dong Myung Junior College) ;
  • Lee Goon-Ja (Department of Food Technology, Dong Myung Junior College)
  • Published : 1999.06.01

Abstract

Denaturation of actomyosin from the obliquely striated mantle muscle of squids (Todarodes pacificus) was studied by measuring the changes in $Ca^{2+}$-ATPase activity, relative viscosity, and solubility during frozen storage at three different temperature zones of maximum ice crystal formation $(-3^{\circ}C,\;-\;-5^{\circ}C)$, the eutectic point $(-11^{\circ}C)$, and $-20^{\circ}C$. The logarithms of $Ca^{2+}$-ATPase activity, relative viscosity and solubility of the actomyosin solutions (0.6 M KCl) and suspensions (0.05 M KCl) tended to decrease during frozen storage. The denaturation of squid actomyosin at the zone of maximum ice crystal formation significantly differed by only two degree of temperature difference between $-3^{\circ}C$ and $-5^{\circ}C$, and it (0.05 M KCl) at $-3^{\circ}C$ was less than those of other temperature. The denaturation at $-11^{\circ}C$ was more rapid than at $-5^{\circ}C$. The logarithms of $Ca^{2+}$ -ATPase activity, relative viscosity, and solubility were changed slower in the suspensions (0.05 M KCl) than the solutions (0.6 M KCl) at all experimental temperatures.

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