Gelation mechanism of fish proteins.

点击翻译按钮获取中文摘要

Participation of the alpha-helix in setting was investigated using circular dichroism, DSC and Rheometer.1)Thermal stability of myosin from several species of fish adapted to different environmental temperatures has been studied by using differential scanning calorimetery, fluorescence intensity and circular dichroism.2)The temperature range of the sharp decrease in the alpha-helical content agreed very closely with that of the endothermic peaks.3)The structure of fish myosin was much more unstable than that of rabbit.4)The alpha-helicity of the actomyosin from several species of fish decrease during incubation at 30ﾟC or at 40ﾟC.5)The extent and pattern of decrease different among species.6)When rate of decrease was plotted vs rate of increase in strength of gel preincubated at 30ﾟC or 40ﾟC, the two factors correlated closely.From 1)-6), we propose that the unfolding of alpha-helix of fish myosin initiated setting.