坐りに対する蛍光分光学的検討〔英文〕

概要

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On the assumption that hydrophobic interactions are involved in the setting (low-temperature gelation of fish flesh sol), the thermal behaviors of muscle proteins were compared fluorometrically for some species which set easily: sardine, jack mackerel, flatfish, yellowtail, and mackerel, and for some which set with some difficulty: striped mullet, dophinfish, beef, pork and chicken. An actomyosin or myosin solution (10 ml) was heated at 40°C for 10min. The emission intensity was recorede from 350 to 500 nm at the excitation wavelength of 365nm, after the addition of 0.04% (w/v) Na-8-anilino-1-naphthalene sulfonate (1 ml). The emission intensity at 470 nm per 1 mg/ml protein decreased with the increase in the protein concentration, and increased if the protein solution was previously heated. For actomyosin, the increasw in the emission intensity was larger in the easily setting species than in the other ones. For myosin, large increases were found, in the order of striped mullet, dolphinfish, pork and chicken; this order corresponds to that of the ease to set. But in the easily setting species, the increase was not always alrge. The scattering of the excitation light increased upon heating, especially in the sardine actomyosin and the myosins from the easily setting species. Sucrose suppressed the increase in the emission intensity and also the increase in the scattering of the excitation linght upon heating.
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