魚類筋形質タンパク質の凝固特性

概要

論文の詳細を見る
Using 0.1M NaCl extract (pH 6.8) of fish muscle homogenate the solubilizing-coagulating properties of the sarcoplasmic proteins (Sp-p) were examined on different pH, ionic-strength and heating conditions. (1) The isoelectric precipitation occurred at pHs ranging from pH 4.5-6.5, varying in magnitude with species of fish. The amount of precipitation at pH 5.2, being considered to be I. P., was 25%, 13% and 7% for common mackerel, horse mackerel and croaker, respectively. (2) Increasing the ionic-strength of the extracts caused not only an enlargement of the isoelectric zone toward the more acidic side but also a rise in the amount of precipitation. (3) When the extract was at first acidified to pH‹4 or alkalified to pH›11 and thereafter neutralized to the neutral zone ranging from pH 6 to 8, almost all the proteins except myoalbumin became insoluble. The insolubility rate was 95%, 87% and 80% for common mackerel, horse mackerel and nemipterid, respectively. (4) The heat coagulation of Sp-p took place at the definite pH range of pH 5.0-9.5 re-gardless of fish species, but the coagulability varied with the species because of a variable content of myoalbumin. The coagulability was 95%, 87% and 75% at pH 6.8 for common mackerel, horse mackerel and croaker, respectively.