Changes of protein profiles in pork and beef meat caused by high hydrostatic pressure treatment

Abstract

In the experiments pork loin and beef sirloin were treated by pressures of 100 to 600 MPa by 100 MPa steps for 5 min. Colour changes of samples and the changes of proteins were investigated. The latter were examined with isoelectric focusing and SDS polyacrylamide gel electrophoresis. We found that myoglobin behaved completely differently in case of the two different species. Myoglobin has mostly lost its native state at 300 MPa pressure in case of pork, but the beef myoglobin could remain native even up to 500 MPa. The treatment at 300 MPa or higher pressure values caused almost complete aggregation and denaturation in case of pork and beef proteins. The results of SDS-PAGE and the colour measurement confirmed this finding.