• Korean Journal of Food Science and Technology
• /
• v.20 no.6
• /
• pp.862-867
• /
• 1988

Myofibrillar proteins were prepared from cold(pollack, salmon) and warm current fish(shark), and their thermostabilities were compared. Thermodynamic data for inactivation of myofibrillar proteins, such as D-value, Kd-value, revealed that thermostability of myofibrillar proteins from warm current fish was higher than that from cold current fish.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.30 no.4
• /
• pp.574-578
• /
• 2001

Myofibrillar proteins were prepared from red muscle and white muscle of fresh water fish and sea water fish, and their thermostabilities and effect of temperature on the myofibrillar ATPase activities were compared. Differences in temperature dependency of myofibrillar ATPase activities were found between two species. Thermodynamic data for inactivation of myofibrillar proteins, such as D value, Z value, $\Delta$ $H^{{\neq}}$, $\Delta$ $G^{{\neq}}$ and $\Delta$ $S^{\neq}$ revealed that thermostabilities of myofibrillar proteins from fresh water fish were higher than those from sea water fish, and that myofibrillar proteins from red muscle were more heat labile than those from white muscle.