Abstract
The effects of heat treatment on the interaction of salt soluble muscle protein and soy protein isolate in model emulsions were studied. Three soy protein isolates (SPI) were used: a commercial one (CSPI) and two pilot plant samples: a native soy protein isolate (NSPI) and an acid treated soy protein isolate (ASPI). Emulsions were prepared with muscle protein (MP), NSPI, ASPI, CSPI and mixtures of MP and the different SPIs, and then treated at 20, 55, 70, 80 and 90°C. Coalescence, soluble protein and electrophoresis of the aqueous phase of the emulsions were evaluated for each temperature. At 20°C the more native soy protein (NSPI) was compatible with MP, producing a stable emulsion that became more stable during heat treatment. CSPI alone could not form a stable interfacial film through the temperature range, however emulsion stabilisation was achieved at 55°C and 70°C when adding MP. Emulsions prepared with MP ASPI were highly unstable at 20°C, while as the emulsion temperature increased, coalescence decreased abruptly and maintained low values at every temperature. MP, NSPI, ASPI and MP NSPI produced stable emulsions both at 20°C and higher temperatures.
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