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Title:

Kinetics of formation and physicochemical charaterization of thermally-induced \textgreekb-lactoglobulin aggregates

Document type:
Zeitschriftenaufsatz
Author(s):
Zúñiga, R. N.; Tolkach, A.; Kulozik, U.; Aguilera, J. M.
Abstract:
The kinetics of heat denaturation and aggregation for β-lactoglobulin dispersions (5% w/v) were studied at 3 pHs (6, 6.4, and 6.8) and at a heating temperature of 80 ◦C. Protein aggregates were characterized for hydrodynamic diameter, microstructure, and molecular weight by means of dynamic light scattering, transmission electron microscopy, and polyacrylamide gel electrophoresis, respectively. Concentration of native β-lactoglobulin decreased with holding time and with a decrease in the pH. App...     »
Keywords:
aggregate size; denaturation kinetics; electrophoresis, heat treatment; rate constants; ß-Lactoglobulin; transmission electron microscopy
Journal title:
Journal of Food Science
Year:
2010
Journal volume:
75
Pages contribution:
E261-E268
Fulltext / DOI:
doi:10.1111/j.1750-3841.2010.01617.x
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