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Electrophoretic Behaviors of α-Lactalbumin and β-Lactoglobulin Mixtures Caused by Heat Treatment
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Electrophoretic Behaviors of α-Lactalbumin and β-Lactoglobulin Mixtures Caused by Heat Treatment
Lee, You-Ra; Hong, Youn-Ho;
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In order to study the reaction behaviors of bovine -lactalbumin (-La), -lactoglobulin (-Lg), and their mixtures during heat treatment, samples were analyzed using native-polyacrylamide gel electrophoresis (Native-PAGE), sodium dodecylsulfate (SDS)-PAGE, and two-dimensional (2-D)-PAGE. The electrophoresis demonstrated that the loss of native--La increased as temperature increased, and that the loss of apo--La was slightly higher than that of holo--La. The tests also showed that during heat treatment, a mixture of -La and -Lg was less stable than -La alone. As such, it was assumed that -Lg induced holo--La to be less stable than apo--La during heat treatment. The reaction behavior of -La (holo-, apo-form) during heat treatment showed similar patterns in the 2-D-PAGE electropherogram, but the mixture of -La and -Lg created new bands. In particular, the results showed a greater loss of native -La in the holo--La and -Lg mixture than in the apo--La and -Lg mixture. Thus, it can be concluded that the holo--La and -Lg mixture was more intensively affected by heat treatment than other samples, and that free sulphydryl groups took part in the heat-induced denaturation.
-lactalbumin;-lactoglobulin;Heat Treatment;Electrophoresis;2-D PAGE;SH Group;
 Cited by
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