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KMID : 1007520020110020161
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Food Science and Biotechnology
2002 Volume.11 No. 2 p.161 ~ p.164
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Heat-induced aggregation behavior of bovine β-lactoglobulin B
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Hong Youn-Ho
Lawrence K. Creamer
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Abstract
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In order to elucidate the reaction path of the heat-induced aggregation of bovine β-lactoglobulin B (β-Lg) at constant temperature, samples of a β-Lg solution were heated in a phosphate buffer at 77℃ for 0 to 10 min and then frozen. The mobility and intensity of the protein species in the β-Lg products were analysed using alkaline (native)-polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulfate (SDS)-PAGE, and near-UV circular dichroism (CD). Heating the β-Lg at 77℃ resulted in the disappearance of the native β-Lg band, as well as the formation of protein species with lower electrophoretic mobilities. Aggregates of various sizes were formed, and the amounts of native-like and SDS monomeric β-Lg decreased as heating time increased. The increase and subsequent decrease in the concentration of the nonnative β-Lg monomer indicates that this intermediate was probably an essential member of the denaturation and aggregation pathways. The changes in CD at 270 nm, an index of significant alteration to disulfide bond dihedral angles, occurred after more extensive heating. The intensity of deep troughs decreased as heating time increased. These latter results indicate that the initial irreversible stage in the heat-induced aggregation of β-Lg modified the tertiary structure of the protein.
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