貯蔵中の筋肉たんばくに対する初期の凍結温度の影響: : ホモジネートの組織学的観察

概要

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1. Homogenates of frozen and thawed cod muscle obtained by Cell Fragility Method varied in their microscopic appearance according to the freezing temperature. 2. After freezing cod muscle in liquid air, thawing and homogenizing, many of the myofibrils were seen to be joined together along their sides, and the cooked material was judged to be tougher than muscle frozen at -30°C. 3. Freezing at -3°C and storing at -16°C caused the homogenates to become pale (“misty”) in appearance. Under the microscope it was seen that some of the fine structure of the myofibrils had disappeared, and they seemed to be considerably depleted of protein. 4. It was concluded that the phenomena at the different temperatures resulted from variations in the amount of ice in the tissue. (a) At very low temperatures, the freezing of tightly-bound water damaged the protein molecules. (b) At -3°C the amount of ice was relatively small, and the resulting lower concentration of tissue salts favoured the dissolution of myofibrillar proteins, i.e. the muscle partially dissolved in its own salt solution, thus accounting for its unusual properties.
公益社団法人日本水産学会の論文