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KMID : 0380619860180030226
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Korean Journal of Food Science and Technology
1986 Volume.18 No. 3 p.226 ~ p.233
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Thermostability of Myofibrillar Proteins from Red Muscle and White Muscle
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Abstract
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Myofibrillar proteins were prepared from red muscle and white muscle, and their thermostabilities were compared. Rate constants of inactivation of myofibrillar proteins were increased as the ionic strength of reaction mixture increased and also dielectric constant of reaction mixture decreased. Thermodynamic data for inactivation of myofibrillar proteins, such as D-value, △H^*, △G^* and △S^*, revealed that thermostabilities of myofibrillar proteins from white muscle were higher than those from red muscle, and that myofibrillar proteins from chicken muscle were more heatlabile than those from bovine muscle.
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KEYWORD
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