Authors: Galani, D Apenten, RKO

Citation: D. Galani et Rko. Apenten, Revised equilibrium thermodynamic parameters for thermal denaturation of beta-lactoglobulin at pH 2.6, THERMOC ACT, 363(1-2), 2000, pp. 137-142

Authors: Apenten, RKO Galani, D

Citation: Rko. Apenten et D. Galani, Thermodynamic parameters for beta-lactoglobulin dissociation over a broad temperature range at pH 2.6 and 7.0, THERMOC ACT, 359(2), 2000, pp. 181-188

Authors: Apenten, RKO Galani, D

Citation: Rko. Apenten et D. Galani, Protein stability function relations: native beta-lactoglobulin sulphhydryl-disulphide exchange with PDS, J SCI FOOD, 80(4), 2000, pp. 447-452

Authors: Galani, D Apenten, RKO

Citation: D. Galani et Rko. Apenten, Beta-lactoglobulin denaturation by dissociation-coupled unfolding, FOOD RES IN, 32(2), 1999, pp. 93-100

Authors: Galani, D Apenten, RKO

Citation: D. Galani et Rko. Apenten, Heat-induced denaturation and aggregation of beta-Lactoglobulin: kinetics of formation of hydrophobic and disulphide-linked aggregates, INT J FOOD, 34(5-6), 1999, pp. 467-476

Authors: Apenten, RKO Galani, D

Citation: Rko. Apenten et D. Galani, Is the rate of sulfur-disulfide exchange between the native beta-Lactoglobulin and PDS related to protein conformational stability?, INT J FOOD, 34(5-6), 1999, pp. 483-486