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Kinetics of the Irreversible Thermal Denaturation and Disulfide Aggregation of α‐Lactalbumin in Milk Samples of Various Concentrations
Author(s) -
Anema S.G.
Publication year - 2001
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2001.tb15573.x
Subject(s) - lactalbumin , chemistry , denaturation (fissile materials) , kinetics , casein , chromatography , protein aggregation , micelle , whey protein , disulfide bond , alpha lactalbumin , biochemistry , nuclear chemistry , aqueous solution , physics , quantum mechanics
ABSTRACT: α‐lactalbumin denaturation was first order and was virtually unaffected by milk solids concentration, with a similar denaturation rate at all the concentrations for each temperature investigated. Similarly, disulfide aggregation of α‐lactalbumin was first order and unaffected by milk solids concentration. Only about 70% of the denatured α‐lactalbumin was involved in disulfide‐aggregated complexes with other denatured whey proteins or with the casein micelles. Calculated thermodynamic parameters (activation energies, enthalpies of activation, entropies of activation and free energies of activation) for irreversible denaturation and for disulfide aggregation were similar for all milk concentrations.