Rigidity and Viscosity Changes of Croaker Actomyosin During Thermal Gelation
Rigidity and Viscosity Changes of Croaker Actomyosin During Thermal Gelation
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黄鱼肌动球蛋白热凝胶过程中硬度和粘度的变化
DOI：
10.1111/j.1365-2621.1985.tb13267.x
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发表时间：
2006
影响因子：
3.9
通讯作者：
D. D. Hamann
中科院分区：
文献类型：
--
作者：
M. C. Wu;T. Lanier;D. D. Hamann
开发了两种类型的热扫描刚性监测器（TSRM），其是非破坏性的，并且能够在宽范围的浓度下监测蛋白质加热期间的刚性或粘度变化。通过这些TSRM装置和Brookfield粘度计在恒定速率加热（1°C/min）期间研究了在黄鱼肌动球蛋白的凝胶化期间发生的热转变。在这些条件下，肌动球蛋白的甘精酶仅在蛋白质浓度高于5.5%时发生。在硬度与温度的关系图中，在凝胶化过程中观察到三个转变，分别发生在38°C、46°C和60°C附近。在较低浓度下，仅观察到一个峰，发生在36°C附近。假设了鱼蛋白的流变学性质在36-38°C的转变与高温“凝固”现象之间的关系。
Two types of thermal scanning rigidity monitors (TSRM) were developed which are nondestructive and capable of monitoring rigidity or viscosity changes during heating of proteins over a wide range of concentrations. Thermal transitions which occur during gelation of croaker actomyosin were studied by these TSRM devices and the Brookfield viscometer during constant rate heating (1°C/min). Gelation of actomyosin occurred only at protein concentrations above 5.5% under these conditions. In plots of rigidity versus temperature, three transitions were observed during gelation, occurring near 38°C 46°C and 60°C. At lower concentrations, only one peak was observed, occurring near 36°C. A relationship between the 36–38°C transition in rheological properties and the high temperature “setting” phenomenon of fish proteins is postulated.