The effects of thawing methods (refrigeration thawing (RT, 4 °C), water immersion thawing (WT, 18 °C), vacuum thawing (VT, 25 °C), ultrasonic thawing (UT, 20 °C) and microwave thawing (MT)) on the conformation and gel qualities of myofibrillar protein (MP) obtained from porcine longissimus muscle were investigated. The results showed that MP conformation and gel qualities of porcine longissimus muscles by VT and UT were insignificantly changed compared to fresh meat (FM). A significant decrease in free amino groups of MP from MT illustrated that MT induced protein aggregation and oxidation (P < 0.05). The results of circular dichroism (CD) spectra analysis and fluorescence spectroscopy indirectly proved that thawing can cause protein cross-linking and degradation, secondary structure destruction, non-hydrophilic domain exposed and conformational change of samples. The largest changes in solubility, surface hydrophobicity and particle size were obtained with MT. The effects on the conformation and gel quality of MP were verified during thawing process.

解冻方法的影响（冷冻解冻（RT，4°C），水浸解冻（WT，18°C），真空解冻（VT，25°C），超声解冻（UT，20°C）和微波解冻（ MT））研究了从猪背最长肌获得的肌原纤维蛋白（MP）的构象和凝胶质量。结果表明，与新鲜肉（FM）相比，VT和UT对猪背最长肌的MP构象和凝胶质量的影响不显着。MT中MP的游离氨基显着减少表明MT诱导蛋白质的聚集和氧化（P < 0.05）。圆二色性（CD）光谱分析和荧光光谱的结果间接证明，解冻可导致蛋白质交联和降解，二级结构破坏，非亲水性结构域暴露以及样品的构象变化。用MT获得了最大的溶解度，表面疏水性和粒度变化。在解冻过程中验证了对MP的构象和凝胶质量的影响。