Abstract
This paper relates the protein solubility and rheological changes occurring in washed sardine mince gels produced by different treatments: heat-induced, pressure-induced, and pressure-assisted gelation. In batter and set gel, there was considerable involvement of low molecular mass proteins (<67 kDa), such as actin, linked chiefly by weak bonds. High molecular mass proteins (200−67 kDa) were implicated in the other samples, but only myosin heavy chain (MHC) appeared in the cases heated at 90 °C. The highest values for work of penetration in the heat-induced gel and the pressure-induced gel were associated with the highest amounts of insoluble proteins. All the gel networks were stable enough to hold water. The highest lightness value was obtained in the pressure-assisted gel as a result of the application of both treatments: pressure and heat. The ultrastructure of the gels induced by heating, with or without pressure treatment, was more spongy than in the case of the gel induced only by pressure, which was more compact. Keywords: Heat; pressure; gel; solubility; ultrastructure; rheology
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