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090			_aB-11449
245	1	0	_aThermodynamic Parameters of ß-Lactoglobulin-Pectin Complexes Assessed by Isothermal Titration Calorimetry
490	0		_vJournal of Agricultural and Food Chemistry, 51(15), p.4450-4455, 2003
520	3		_aIsothermal titration calorimetry (ITC)was used to determine the binding constant, stoichiometry, enthalpy, and entropy of ß-lactoglobulin/low- and high-methoxyl pectin (ß-lg-LM- and HM-pectin)complexes at 22 °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 ß-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 ß-lg interacted could partially be attributed to conformational changes. The C1 had a binding stoichiometry of 8.3 and 6.1 ß-lg molecules complexed per LM- or HM-pectin molecule, respectively. The C2 had about 16.5 and 15.1 ß-lg molecules complexed per LM- and HM-pectin, respectively.
650	1	4	_aß-LACTOGLOBULIN
650	1	4	_aPECTIN
650	1	4	_aINTERACTIONS
650	1	4	_aISOTHERMAL TITRATION CALORIMETRY
700	1	2	_aGirard, Maude
700	1	2	_aTurgeon, Sylvie L.
700	1	2	_aGauthier, Sylvie F.
856	4	0	_uhttps://drive.google.com/file/d/14ZQwdJyDgH9ZMIomndI1tfGdd-SbmhFu/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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