L-组氨酸在低离子强度溶液中抑制肌球蛋白的热诱导凝胶化。
L-histidine inhibits the heat-induced gelation of actomyosin in a low ionic strength solution.
机构信息
Laboratory of Applied Food Science, Graduate School of Agriculture, Hokkaido University, Sapporo, Hokkaido, Japan.
Department of Food and Life Science, Toyo University, Ora, Gunma, Japan.
出版信息
Anim Sci J. 2023 Jan-Dec;94(1):e13825. doi: 10.1111/asj.13825.
The heat-induced gelation of actomyosin plays a key role in meat processing. Our previous study showed that L-histidine could affect the characteristics of a heat-induced gel of myosin on a low ionic strength. To apply the specific effect of L-histidine to meat processing, the heat-induced gel properties of actomyosin in the presence of L-histidine were investigated. Actomyosin in a low ionic strength solution containing L-histidine did not form a gel upon heating. The dynamic rheological properties of actomyosin in low ionic strength solutions were distinct depending on the presence or absence of L-histidine. Electron microscopy showed that, heated at 50°C, actomyosin in a low ionic strength solution containing L-histidine remained a filamentous structure. The surface hydrophobicity of actomyosin was stable up to 50°C in a low ionic strength solution containing L-histidine. In conclusion, L-histidine might suppress the aggregation of actomyosin and inhibit heat-induced gelation in a low ionic strength solution.
肌球蛋白的热诱导凝胶在肉品加工中起着关键作用。我们之前的研究表明，L-组氨酸可以影响低离子强度下肌球蛋白热诱导凝胶的特性。为了将 L-组氨酸的特殊作用应用于肉类加工，研究了存在 L-组氨酸时肌球蛋白的肌球蛋白的热诱导凝胶特性。在低离子强度溶液中含有 L-组氨酸的肌球蛋白在加热时不会形成凝胶。低离子强度溶液中肌球蛋白的动态流变特性取决于 L-组氨酸的存在与否。电子显微镜显示，在 50°C 加热时，含有 L-组氨酸的低离子强度溶液中的肌球蛋白仍然保持丝状结构。在含有 L-组氨酸的低离子强度溶液中，肌球蛋白的表面疏水性在 50°C 时保持稳定。总之，L-组氨酸可能抑制肌球蛋白的聚集，并抑制低离子强度溶液中的热诱导凝胶形成。
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