Effects Of High-pressure Treatment On The Myosin Of Bovine Skeletal Muscle

In this paper, Myosin was extracted from Bovine skeletal muscle and then treated with different pressures(100,200,300,400 MPa). Detected through SDS-PAGE to be the purity of myosin, as well as the degree of compression.The properties of the extracted myosin, such as solubility,ATPase activity, aromatic hydrophobic surface, spectral center of mass , and sulfhydryl (SH), were studied .SDS-PAGE showed that band of myosin, whose light chain with 13.8 KDa nearly disappeared under pressure 400 MPa, gradually disappearred under increasing pressure. This may be treated with ultra-high pressure into small molecular weight protein degradation of the protein or peptide, amino acids and so on.Myosin protein Solubility gradually decreased with increasing pressure, with a respective slight and obvious decline under 100~200 MPa . There was a drastic decreasing solubility after 200 MPa. ATPase activity decreased under increasing pressure and KCL concentration . The amount of hydrophobic residues of aromatic surface escalated with increased pressure. However, declined slightly after 300 MPa. Tyrosine and tryptophan fluorescence intensity generally declined with increasing pressure. There was a decrease in light scattering intensity of myosin. This value at 400MPa was 57% of it at no extra pressure. Center of spectral mass gradually dropped with increasing pressure, and it plunged after 300MPa, reaching a minimum 276/105cm-1 under 400MPa. Absorbance of SH,obtained from different increased pressures, gradually reduced, with an obvious deduction between 300~400 MPa so that it reached a minimum 0.178A under 400MPa. In conclusion, effects of different pressures treatment on myosin and changing regularity were studied. Not only did we provide theoretical foundation in practical application of high-pressure technology to production by our study, but it is also predicted potential economic and social benefits .