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-Lactalbumin and ß-Lactoglobulin1Department of Food Science, North Carolina State University, Raleigh 27650
ABSTRACT
Model systems of proteins of milk serum were heated to 143 ± 1 C by steam injection, held for 8 to 10 s and vacuum cooled.
-Lactalbumin was more resistant to heat denaturation when processed alone than when mixed with ß-lactoglobulin according to electrophoretic and densitometric quantification. Variants A and B of ß-lactoglobulin were sensitive to ultra-high-temperature processing. A new component with mobility intermediate between
-lactalbumin and ß-lactoglobulin formed after ultra-high-temperature processing. Analysis of the new component indicated that it was a protein complex of
-lactalbumin and ß-lactoglobulin. ß-Lactoglobulin was the major source of available sulfhydryls. The experimental sulfhydryl value for a mixture of
-lactalbumin and ß-lactoglobulin was 17% lower than calculated from the composition of the mixture. This was possibly because sulfhydryl groups are involved in the heat-induced complex.
1 Paper No. 5143 of the Journal Series of the North Carolina Agricultural Experiment Station, Raleigh. The use of trade names in this publication does not imply endorsement by the North Carolina Agricultural Experiment Station nor criticism of similar ones not mentioned.
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