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.
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。
