ABSTRACT
The impact of high pressure/temperature treatment on structure modification and functional sensory properties of frankfurter batter was investigated. The degree of solubilization of meat proteins, particularly of myosin, was identified as a key process with significant effect on the batter's structural properties. The maximal solubilization level was at 200 MPa/40 °C IT for all formulations which was found to be treatment time dependent. The impact of the pressurizing gradient - PG=40 MPa/s and PG=2.5 MPa/s was investigated and estimated to have a significant effect on the protein network and functional properties, respectively. These were improved at low PG (2.5 MPa/s) as a phenomenon of secondary network formation parallel to the main matrix. Batter secondary-structure characteristics were found to be ionic-strength dependent. According to SDS-PAGE analysis, the major role in the solubilization, aggregation and gelation processes occurring in the aqueous phase was due to the myosin S-1 and S-2, N-terminal, C-terminals, the MLC and actin during the high pressure/temperature treatment.
Subject(s)
Meat Products/analysis , Temperature , Animals , Chromatography, High Pressure Liquid , Electrophoresis, Polyacrylamide Gel , Food Handling , Hydrostatic Pressure , Models, Chemical , Myosin Subfragments/analysis , Myosin Subfragments/metabolism , Osmolar Concentration , Protein Structure, Secondary , Salts/analysis , Salts/metabolism , SwineABSTRACT
Pressurization may cause unwanted side effects including color or texture changes of fish and meat. The color changes of poultry, pork, and smoked salmon were studied by CIE L*, a*, b* system, and resonance Raman (RR). High-pressure processing (HPP) of pork and chicken meat resulted in significant color modification at pressures higher than 270 and 280 MPa, respectively. RR spectra were taken after a high-pressure treatment of pork meat. According to the RR-data, deoxymyoglobin is the dominating myoglobin species in pork meat. High-pressure treatment causes conformational changes resulting in a stabile nonnative ferrous myoglobin species while the ferrous myoglobin state is maintained. High-pressure treatment causes a decrease of the relative RR intensities of astaxanthin by salmon as probed with 514 nm. RR spectra excited at 413 nm revealed a heterogeneous broadening of astaxanthin bands accompanied by the formation of deoxymyoglobin or deoxyhemoglobin. The broadening is interpreted as the degradation products of astaxanthin. Obviously, the high-pressure treatment of smoked salmon triggers redox processes of astaxanthin and the heme protein.
