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Quakenbrück, Germany

Tintchev F.,German Institute of Food Technology | Tintchev F.,TU Berlin | Tintchev F.,McAirlaids GmbH and Co. KG | Bindrich U.,German Institute of Food Technology | And 4 more authors.
Meat Science | Year: 2013

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. © 2013 Elsevier Ltd. Source

Tintchev F.,German Institute of Food Technology | Wackerbarth H.,German Institute of Food Technology | Kuhlmann U.,TU Berlin | Toepfl S.,German Institute of Food Technology | And 3 more authors.
Annals of the New York Academy of Sciences | Year: 2010

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. © 2010 New York Academy of Sciences. Source

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