Departamento de Tecnología y Calidad de los Alimentos, Facultad de Ciencias Veterinarias, Universidad Nacional del Centro de la Provincia be Buenos Aires, Campus Universitario, Pje. Arroyo Seco, B7001BBO Tandil, Argentina.
Meat Sci. 2018 Oct;144:127-134. doi: 10.1016/j.meatsci.2018.03.026. Epub 2018 Mar 31.
Variations in the quantity and thermal stability of collagen in intramuscular connective tissue (IMCT) play a role in variations in cooked meat tenderness. This review is focussed on sources of variability, especially in the perimysial IMCT, and challenges some of the accepted ideas about its denaturation behaviour, its contribution to cooking shrinkage at high temperatures and the concept of IMCT as an immutable "background toughness". IMCT dominates the shear strength of raw and lightly cooked muscle, but at cooking temperatures of 70-80° its contribution is smaller than the myofibrillar component. The thermal denaturation temperature of IMCT collagen given by differential scanning calorimetry at fast heating rates is usually in the range of 62-67 °C, but collagen denaturation is a multistep, non-equilibrium process that is highly heating-rate dependent and can occur at 55-60 °C in slow heating regimes, such as slow roasting or sous-vide cooking. Although it is commonly assumed that collagen shrinkage drives shrinkage of meat and greater cooking losses above 65 °C, an examination of currently available information suggested that there is no evidence to support this idea. The amount and thermal stability of IMCT collagen can be varied by factors manipulating growth rate, and a recent model of these effects is discussed. The characteristics of the thermally-stable fraction of IMCT collagen as the most important component influencing the connective tissue contribution to cooked meat toughness and the need for future work investigating mechanisms to degrade or turnover this specific fraction is suggested.
肌肉内结缔组织（IMCT）中胶原蛋白的数量和热稳定性的变化在熟肉嫩度的变化中起着作用。本综述重点介绍了变异性的来源，特别是在肌束膜 IMCT 中的变异性，并且对其变性行为、在高温下对烹饪收缩的贡献以及将 IMCT 视为不可改变的“背景韧性”的概念提出了一些质疑。IMCT 支配着生肉和轻度烹饪肌肉的剪切强度，但在 70-80°C 的烹饪温度下，其贡献小于肌原纤维成分。在快速加热速率下通过差示扫描量热法给出的 IMCT 胶原蛋白的热变性温度通常在 62-67°C 范围内，但胶原蛋白变性是一个多步骤、非平衡过程，高度依赖于加热速率，并且在缓慢加热条件下（如缓慢烘烤或低温慢煮）可以在 55-60°C 下发生。尽管通常认为胶原蛋白收缩驱动肉的收缩和超过 65°C 时更大的烹饪损失，但对现有信息的检查表明，没有证据支持这一观点。IMCT 胶原蛋白的数量和热稳定性可以通过操纵生长速度的因素来改变，并且讨论了这些影响的最新模型。建议探讨热稳定的 IMCT 胶原蛋白部分作为影响熟肉韧性的结缔组织最重要成分的特征，以及需要进一步研究降解或转化这种特定部分的机制。
