Heat‐induced denaturation of water‐leached fish muscle proteins, as affected by addition of sucrose and/or salt, were investigated by differential scanning calorimetry (DSC). Net enthalpic changes for these muscle proteins were always endothermic in nature, and of a greater magnitude at faster heating rates. This was interpreted to infer that aggregation at lower heating rates led to formation of a gel structure in which potential bondings were more completely accomplished; that is, a more energetically favorable structure was attained with slow heating. The stabilization of proteins by sucrose, and destablization of proteins by salt, were revealed by shifts in transition peaks and activation energies, the latter determined by two methods of kinetic analysis.
|Number of pages||10|
|Journal||Journal of Food Biochemistry|
|Publication status||Published - 1990 Oct|
ASJC Scopus subject areas
- Food Science
- Cell Biology