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Heat-Induced Reaction of Bovine Whey Proteins  

이유라 (전남대학교 식품영양학과)
홍윤호 (전남대학교 식품영양학과)
Publication Information
Food Science of Animal Resources / v.22, no.2, 2002 , pp. 179-182 More about this Journal
Abstract
Using differential scanning calorimetry (DSC), changes underwent by a mixture of $\alpha$-lactalbumin ($\alpha$-La) and $\beta$-lactoglobulin ($\beta$-Lg) during heat treatment were studied, yielding useful information for the dairy industry. Results of the DSC showed that the heat denaturation temperature of the hobo-$\alpha$-La was higher than that of apo-$\alpha$-La, suggesting hole-$\alpha$-La‘s greater stability. The denaturation temperature of a mixture of holo-$\alpha$-La and $\beta$-Lg was also slightly lower than that of holo-$\alpha$-La alone. The denaturation temperature of an apo-$\alpha$-La and $\beta$-Lg mixture was higher than that of holo-$\alpha$-La and $\beta$-Lg, suggesting that the heat stability of apo-$\alpha$-La was increased by $\beta$-Lg. Based on these results, it is possible to conclude that a mixture of holo-$\alpha$-La and $\beta$-Lg is more intensively affected by an increase in temperature than other samples, and that free sulphydryl groups seem to take part in this heat-induced denaturation.
Keywords
${\alpha}$-lactalbumin; ${\beta}$-lactoglobulin; differential scanning calorimetry; heat treatment;
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