Thermal denaturation and aggregation properties of Atlantic salmon myofibrils and myosin from white and red muscles (original) (raw)
Related papers
Foods
The technological properties of raw fish are influenced by the changes in protein structure under heating, which determines the texture and quality of the product. The aim of the study was to examine the protein denaturation temperature and the rheological properties of Baltic herring muscle tissue. The thermal properties were determined by the differential scanning calorimetry (DSC) method and the rheological properties were determined using dynamic oscillatory tests. DSC showed four peaks associated with denaturing transformations of myosin (39.59 °C), sarcoplasm (51.67 °C), connective tissue (63.16 °C), and actin (74.40 °C). Analysis showed that not all transformations occurred according to the same kinetic model. The first two and the last peak are described by 1st order kinetics, while peak 3 is described by 2nd order kinetics. Correlating the changes in fish tissue structure during heating with the rheological characteristics provides more information. The obtained kinetics mo...
Species dependence of fish myosin stability to heat and frozen storage
International Journal of Food Science & Technology, 2007
The thermal stabilities of the proteins of a range of fish muscles of different habitat temperatures were determined by differential scanning calorimetry before and after frozen storage at 20°C.In whole muscle a clear relationship was seen between habitat temperature and the thermal denaturation of myosin, which persisted when isolated myosins were analysed under conditions close to physiological pH and ionic strength. the ionic environment of the myosin molecules in the whole tissue will, however, not be exactly the same as in the myosin solution.No significant correlations were seen between habitat temperature, ultimate pH and other analytical parameters.After frozen storage, the myosin transitions in red snapper, a warm water species, was markedly changed in whole muscle but not in isolated myosin, suggesting the post mortem development of an interaction with other muscle proteins. In contrast, in cod, a cold water species, changes in myosin transitions were very similar, both in...
2016
In our study we aimed the rheological behavior of fish myofibrillar proteins and of the homogenates of which these were obtained. For protein extraction and concentrates purification different methods were used. We tracked the variation of elastic modulus and phase angle according to temperature. Myofibrillar proteins determine the water retention and meat hydration capacity, fat emulsifying and gelling capacity. The source and the method of extraction influence the gelling properties of muscle protein. The protein concentration plays a key role in determining the heat induction properties of gels. Gelling properties of the muscle proteins are also influenced by heating temperature, temperature rise speed and of
Effect of Malonaldehyde on the Gelation Properties of Myofibrillar Proteins of Sea Salmon
Journal of Food Science, 2003
ABSTRACT: Myofibrillar proteins incubated with malonaldehyde (27 °C, t = 0 to 8 h) were used to prepare gels by thermal treatment (80 °C, 45 min). Malonaldehyde did not produce significant modifications (P > 0.05) in the storage modulus (G') and complex viscosity (η*) except for t = 0. Texture analysis showed a significant increase (P < 0.05) in elasticity and cohesiveness with hardness approximately constant. Relaxation test presented a marked increase in the elasticity index. A significant decrease (P < 0.05) in water holding capacity (WHC) was recorded. Ultrastructure showed a different network with the appearance of big filaments. Electrophoretic patterns of protein dispersions remainder after gel formation showed a decrease of 81, 53, 25 to 50, and 20 kDa polypeptides.