Thermodynamic parameters of beta-lactoglobulin-pectin complexes assessed by isothermal titration calorimetry.
Isothermal titration calorimetry (ITC) was used to determine the binding constant, stoichiometry, enthalpy, and entropy of beta-lactoglobulin/low- and high-methoxyl pectin (beta-lg-LM- and HM-pectin) complexes at 22 degrees C and at pH 4. The binding isotherms revealed the formation of soluble intrapolymer complexes (C1) further followed by their aggregation in interpolymer complexes (C2). The interaction between beta-lg and LM- or HM-pectin in C1 and C2 occurred spontaneously with a Gibbs free energy around -10 kcal/mol. The C1 were enthalpically driven, whereas enthalpic and entropic factors were involved in the C2 formation. Because ITC did not allow the dissociation of different enthalpic contributions, the values measured as pectin and beta-lg interacted could partially be attributed to conformational changes. The C1 had a binding stoichiometry of 8.3 and 6.1 beta-lg molecules complexed per LM- or HM-pectin molecule, respectively. The C2 had about 16.5 and 15.1 beta-lg molecules complexed per LM- and HM-pectin, respectively.
Girard
Maude
M
STELA Dairy Research Centre, Faculté des sciences de l'agriculture et de l'alimentation, Pavillon Paul-Comtois, Université Laval, Québec, Canada, G1K 7P4.
Turgeon
Sylvie L
SL
Gauthier
Sylvie F
SF
D002151:Calorimetry / Q000379:methods*; D007782:Lactoglobulins / Q000737:chemistry*; D010368:Pectins / Q000737:chemistry*; D013816:Thermodynamics
D007782:Lactoglobulins; D010368:Pectins