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• W2507862146 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 0.5 M), urea (0.1, 0.5, 1 and 5 M) and 2-β-mercaptoethanol (0.1 and 2%), was performed. Samples with NaCl and urea (0.1–1 M) had similar temperature profiles and Tgel values to CPI alone whereas no gel was formed with the addition of 5 M 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." @default.
• W2507862146 created "2016-09-16" @default.
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• W2507862146 date "2016-11-01" @default.
• W2507862146 modified "2023-10-14" @default.
• W2507862146 title "Nature of protein-protein interactions during the gelation of canola protein isolate networks" @default.
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• W2507862146 doi "https://doi.org/10.1016/j.foodres.2016.08.018" @default.
• W2507862146 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28460932" @default.
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