Rao Weili, Liu Sijia, Kong Shiquan, Wang Zhenyu, Shi Zidan, Cai Jianming
College of Food Science and Technology, Hebei Agricultural University, Lekai South Avenue, Baoding 071000, China.
Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Integrated Laboratory of Processing Technology for Chinese Meat and Dish Products, Ministry of Agriculture and Rural Affairs, Beijing 100193, China.
Foods. 2024 Mar 19;13(6):930. doi: 10.3390/foods13060930.
To determine whether sarcoplasmic proteins affected water migration in myofibrils during air-drying, with protein denaturation as an indicator of sarcoplasmic protein changes, the extent of sarcoplasmic protein changes in lamb during air-drying was first studied. The results showed that sarcoplasmic protein's thermal stability decreased and secondary structure changed, indicating sarcoplasmic protein denatured in lamb during air-drying (35 °C, 60% RH, 3 m/s wind speed). Subsequently, the effect of sarcoplasmic protein solutions, dried at different times and rates, on myofibril protein-water interaction was studied in vitro. Two sets of sarcoplasmic protein solutions were dried for 0, 3, 6, and 9 h in a drying oven, resulting in different degrees of change. These two sets with higher or lower drying rates were achieved by controlling the contact area between sarcoplasmic protein solution and air. These dried sarcoplasmic protein solutions were then mixed with extracted myofibril and incubated for 2 h. The results showed a significant increase in T relaxation time of the incubation system when sarcoplasmic protein solution was dried at 35 °C for 3 h. This indicated that myofibrillar protein-water interaction was weakened, facilitating water migration from the inside to the outside of myofibrils. The denaturation degree of sarcoplasmic proteins was slowed by a higher drying rate, thereby alleviating the increase in the amount of immobile water within myofibrils when dried for 6 h. In conclusion, the properties of sarcoplasmic proteins were influenced by both drying rate and time, thereby influencing the water migration within myofibrils during air-drying.
为了确定肌浆蛋白在风干过程中是否影响肌原纤维中的水分迁移，以蛋白质变性作为肌浆蛋白变化的指标，首先研究了羊肉在风干过程中肌浆蛋白的变化程度。结果表明，肌浆蛋白的热稳定性降低，二级结构发生变化，表明羊肉在风干过程中（35℃、60%相对湿度、3m/s风速）肌浆蛋白发生了变性。随后，在体外研究了不同干燥时间和速率干燥的肌浆蛋白溶液对肌原纤维蛋白-水相互作用的影响。将两组肌浆蛋白溶液在干燥箱中干燥0、3、6和9小时，导致不同程度的变化。通过控制肌浆蛋白溶液与空气的接触面积，实现了这两组不同干燥速率（较高或较低）的干燥。然后将这些干燥的肌浆蛋白溶液与提取的肌原纤维混合并孵育2小时。结果表明，当肌浆蛋白溶液在35℃下干燥3小时时，孵育体系的横向弛豫时间（T2）显著增加。这表明肌原纤维蛋白-水相互作用减弱，促进了水分从肌原纤维内部向外部迁移。较高的干燥速率减缓了肌浆蛋白的变性程度，从而减轻了在干燥6小时时肌原纤维内不可移动水量的增加。总之，肌浆蛋白的性质受干燥速率和时间的影响，从而影响风干过程中肌原纤维内的水分迁移。
