Nature of protein-protein interactions during the gelation of canola protein isolate networks

Abstract

The nature of interactions involved during the gelation of a canola protein isolate was investigated using rheology and fractal imaging at neutral pH as a function of protein concentration (5.0–9.0% w/w). The onset of denaturation and the denaturation temperature by differential scanning calorimetry for canola protein isolate (CPI; 98.2% protein) was 78.6°C and 87.1°C, respectively. Rheological testing determined the gelation temperature (Tgel) to be ~87–90°C for all concentrations. The log % strain at break increased from 1.70 to 1.80 as CPI concentration increased from 5.0 to 7.0% (w/w). Rheological testing of CPI in the presence of destabilizing agents, NaCl (0.1 and 0.5M), urea (0.1, 0.5, 1 and 5M) and 2-β-mercaptoethanol (0.1 and 2%), was performed. Samples with NaCl and urea (0.1–1M) had similar temperature profiles and Tgel values to CPI alone whereas no gel was formed with the addition of 5M urea and 2-β-mercaptoethanol reduced the strength of the gel network. Fractal dimension and lacunarity was analyzed using CLSM imaging. The fractal dimension value for all CPI concentrations was ~1.5. The lacunarity of the gel decreased from 0.62 to 0.41 as the concentration of CPI increased from 5 to 7% (w/w). Mechanistic understanding of CPI aggregation and network formation will enable the food industry to better tailor food structure when CPI is present as ingredient.