Universidade de São Paulo, Escola Superior de Agricultura Luiz de Queiroz, Departamento de Agroindústria, Alimentos e Nutrição, Piracicaba, SP 13418-900, Brazil.
Universidade de São Paulo, Escola Superior de Agricultura Luiz de Queiroz, Departamento de Agroindústria, Alimentos e Nutrição, Piracicaba, SP 13418-900, Brazil.
Meat Sci. 2017 Sep;131:25-27. doi: 10.1016/j.meatsci.2017.04.017. Epub 2017 Apr 20.
The thermal denaturation of proteins was evaluated in the natural state of bovine muscle using differential scanning calorimetry (DSC). The Longissimus lumborum muscle was selected according to ultimate pH (pH) values classified into two groups: low pH with values between 5.4 and 5.8, and intermediate pH with values between 5.81 and 6.19. The muscles were cut and aged at 2°C up to 21d post mortem. The three maximum temperatures of denaturation (T, T, T) found in muscle were evaluated, showing higher thermal stability in the intermediate pH group, which could be an indicator of protection of proteins against aggregation or enzymatic activity. The thermal behavior of muscle proteins could be defined by biochemical factors that are affected by pH of the muscle, however, further studies are necessary to explain this process, which could have a great impact on the understanding of the final tenderness achieved in meat.
采用差示扫描量热法（DSC）评估了牛肌肉自然状态下蛋白质的热变性。根据最终 pH 值（pH）将腰最长肌分为两组：pH 值在 5.4 到 5.8 之间的低 pH 值组和 pH 值在 5.81 到 6.19 之间的中 pH 值组。肌肉切割后在 2°C 下成熟，直到死后 21 天。评估了在肌肉中发现的三个变性温度（T1、T2 和 T3），中间 pH 值组的热稳定性更高，这可能表明蛋白质对聚集或酶活性的保护。肌肉蛋白质的热行为可以通过受肌肉 pH 值影响的生化因素来定义，但是，需要进一步的研究来解释这一过程，这可能对理解肉的最终嫩度有很大影响。
