| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2450067 | Meat Science | 2013 | 12 Pages |
•The pressurizing gradient PG had a significant effect on protein properties.•Protein solubilization was found to be higher at low PG.•Increase of myosin head sub fragments, MLC and actin in the aqueous phase.•Batter secondary-structure was found to be ionic-strength dependant.•Solubilization after HP-T was found to be similar for batters with 2% and 1% NaCl.
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.
