鱼类肌球蛋白和猪肉肌球蛋白稳定性的比较研究。
Comparative study on the stability of fish actomyosin and pork actomyosin.
机构信息
College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei Province 430070, PR China.
出版信息
Meat Sci. 2011 Jun;88(2):234-40. doi: 10.1016/j.meatsci.2010.12.026. Epub 2010 Dec 24.
Effects of temperature, pH and ionic strength on the stability of actomyosin (AM) from fish and pork were studied using UV spectra, solubility, turbidity, and sulfhydryl group content measurement for comparison. Pork AM exhibited higher stability to cold storage and heating than fish AM. The unfolding rate of AM increased with increasing temperature. Intense aggregation occurred over 30 °C for fish AM and 40 °C for pork AM. New disulfide bonds mainly formed over 40 °C for fish AM and 60 °C for pork AM. Pork AM exhibited the higher turbidity than fish AM in the range of 50-90 °C, suggesting the higher extent of aggregation of pork AM. Ionic strength mainly influenced solubility of AM, but there was no effect on cleavage and formation of disulfide bond. The lowest solubility of both AM was at pH 5.42. Additionally, fish AM was more sensitive to pH changes than pork AM.
采用紫外光谱、溶解度、浊度和巯基含量测定法，比较了温度、pH 值和离子强度对鱼和猪肉肌球蛋白（AM）稳定性的影响。与鱼 AM 相比，猪肉 AM 在冷藏和加热时表现出更高的稳定性。AM 的展开速率随温度的升高而增加。鱼 AM 在 30°C 以上、猪肉 AM 在 40°C 以上会强烈聚集。新的二硫键主要在鱼 AM 40°C 以上和猪肉 AM 60°C 以上形成。在 50-90°C 的范围内，猪肉 AM 的浊度高于鱼 AM，表明猪肉 AM 的聚集程度更高。离子强度主要影响 AM 的溶解度，但对二硫键的断裂和形成没有影响。两种 AM 的最低溶解度均在 pH 5.42 时。此外，鱼 AM 对 pH 值变化比猪肉 AM 更敏感。
Zotero 插件