Title
Structural thermostability of commercial canola protein-hydrocolloid mixtures
Abstract
Proteins in a mixed system with polysaccharides may behave differently than when used alone. The thermal transition properties (denaturation temperature, Td; enthalpy of denaturation, ΔH) of canola protein isolate (CPI)–hydrocolloid (κ-carrageenan, guar gum) mixtures were assessed using differential scanning calorimetry. Factorial and response surface models were used to examine the effects of pH, salt, protein, guar gum and κ-carrageenan concentrations on the conformational stability of CPI (Td=86 °C, ΔH=16.2 J/g). CPI–κ-carrageenan mixtures treated with sodium acetate (NaC2H3O2, 68 g/l) had the highest Td values (103.2 °C), whereas mixtures treated with sodium thiocyanate (NaSCN, 40.5 g/l) had the lowest Td (92.3 °C) values. Salts decreased ΔH values of CPI–κ-carrageenan mixtures in the order: acetate
Department(s)
Biomedical Sciences
Document Type
Article
DOI
https://doi.org/10.1016/j.lwt.2004.12.005
Keywords
multi-component systems, molecular interactions, calorimetry, conformational stability
Publication Date
2006
Recommended Citation
Uruakpa, Florence O., and S. D. Arntfield. "Structural thermostability of commercial canola protein–hydrocolloid mixtures." LWT-Food Science and Technology 39, no. 2 (2006): 124-134.
