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KMID : 1024620020220020179
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Food Science of Animal Resources
2002 Volume.22 No. 2 p.179 ~ p.182
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Heat-Induced Reaction of Bovine Whey Proteins
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Lee You-Ra
Hong Youn-Ho
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Abstract
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Using differential scanning calorimetry (DSC), changes underwent by a mixture of -lactalbumin (-La) and -lactoglobulin (-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--La was higher than that of apo--La, suggesting hole--La‘s greater stability. The denaturation temperature of a mixture of holo--La and -Lg was also slightly lower than that of holo--La alone. The denaturation temperature of an apo--La and -Lg mixture was higher than that of holo--La and -Lg, suggesting that the heat stability of apo--La was increased by -Lg. Based on these results, it is possible to conclude that a mixture of holo--La and -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.
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KEYWORD
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α-lactalbumin, β-lactoglobulin, differential scanning calorimetry, heat treatment
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