Rabbit skeletal (M. psoas) myosin subunits, heavy meromyosin (HMM) and light meromyosin (LMM), were purified and treated by high pressure processing (HPP). The HPP (100, 200 and 300 MPa)-modified myosin subunits were subjected to thermal treatment (25–70 °C), during which their conformational and rheological properties were explored. The turbidity of all HMM and LMM samples slightly improved from 25 to 55 °C, and then sharply increased from 55 °C to 70 °C (from). Pressure ≥200 MPa changed the structural properties of HMM, exhibited as more exposed hydrophobic and sulfhydryl patches, whereas the increase of hydrophobicity induced by heating decelerated afterwards. The LMM portion exhibited inferior heating stability. Upon heating, both pressurized and nontreated HMM showed similar trends of changes of secondary structure, which included the reduction of α-helices and the increase of β-structures. Only a slight change of secondary structure occurred on LMM after HPP, indicating a higher resistance of LMM on HPP than HMM. These findings suggested that a moderate denaturation generated by HPP would not affect the thermal behavior of myosin subfragments, while pressures of ≥200 MPa might lead to disadvantageous rheological properties by mediating the thermophysical properties of HMM.

兔骨骼肌（M. psoas）纯化肌球蛋白亚基，重肌球蛋白（HMM）和轻肌球蛋白（LMM），并通过高压处理（HPP）处理。HPP（100、200和300 MPa）修饰的肌球蛋白亚基经过热处理（25–70°C），在此期间对其构象和流变性质进行了研究。所有HMM和LMM样品的浊度从25到55°C略有改善，然后从55°C急剧增加到70°C（从）。≥200 MPa的压力改变了HMM的结构特性，表现出更多的疏水性和巯基斑块暴露，而加热引起的疏水性增加随后减速。LMM部分表现出较差的加热稳定性。加热后，加压和未经处理的HMM都显示出相似的二级结构变化趋势，其中包括α-螺旋的减少和β-结构的增加。HPP后LMM仅发生轻微的二级结构变化，这表明LMM对HPP的抵抗力要高于HMM。这些发现表明，HPP产生的适度变性不会影响肌球蛋白亚片段的热行为，而≥200MPa的压力可能通过介导HMM的热物理性质而导致不利的流变性质。