Effects Of High Pressure Treatment On α-actinin Of Bovine Skeletal Muscle

Myofibrillar extracted from bovine skeletal muscle was treated under different pressures (100, 200, 300 and 400 MPa ) and then the changes of myofibrillar protein and their Mg2 +-ATPase activities were investigated. Theα-actinin was also extracted from mature bovine skeletal muscle .The changes of fluorescence spectroscopy , center of emission spectral mass, shrinkage rate and hydrosulfide groups ofα-actinin were detected and analyzed to study structural changes ofα-actinin. The results were as follows:(1) The bands of myofibril gradually fade and their Mg2 +-ATPase activities gradually decreased with increasing pressure.(2) With the increasing pressure, fluorescence intensity ofα-actinin gradually declined, and its peak moved from maximum wavelength to short wavelength.The center of emission spectral mass ofα-actinin also gradually declined.(3) With the increasing pressure, shrinkage rate ofα-actinin decreased gradually and the shrinkage rate was 41% at 400MPa after decompression.(4) Aromatic hydrophobic groups content ofα-actinin increased with the increasing pressure and achieved highest at 300MPa. Aromatic hydrophobic groups content slightly decreased at 400MPa.(5) With the increasing pressure, surface sulfhydryl content ofα-actinin increased. In comparation with the control group, surface sulfhydryl content increased by 33% with 400MPa treatment.It could be concluded that changes in tertiary structure ofα-actinin induced by high pressure was irreversible.