LF-NMR to explore water migration and water–protein interaction of lamb meat being air-dried at 35°C

To decrease the drying time and energy consuming, water migration and water–protein interactions of lamb meat being air-dried at 35°C were investigated. Low-field nuclear magnetic resonance T2b indicated the water–protein interactions changed during air-drying. Area of T21 (intramyofibrillar water) decreased, meanwhile the area of T22 (extra-myofibrillar water) increased when the moisture content decreased from 55 to 45%, indicating the water migrated from myofibril to extramyofibril. Drying rate (the rate of water migration from meat to air) could be predicted by the area of T2 populations, and the correlation coefficient was 0.990. Change of water binding and hydration in myofibrils was evident by the increase in hydrophobicity and decrease in solubility of myofibrillar protein. Differential scanning calorimetry showed denaturation of myosin in dried meat which might result in water migration from myofibril to extramyofibril space. In conclusion, water–protein interactions changed, and then influenced the drying rate during drying.