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://dx.doi.org/10.1016/j.lwt.2004.12.005

Keywords

multi-component systems, molecular interactions, calorimetry, conformational stability

Publication Date

2006

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