Differential scanning calorimetric study of different genetic variants of beta-lactoglobulin
1991
Imafidon, G.I. | Ng-Kwai-Hang, K.F. | Harwalkar, V.R. | Ma, C.Y.
The onset temperatures, denaturation temperatures, and temperatures at width of half-peak height of beta-lactoglobulins AA, BB, and AB were compared using differential scanning calorimetry. Heat stability of the different phenorms of beta-lactoglobulin was variable, depending on the pH and composition of buffer. At pH 6.80, denaturation temperatures of beta-lactoglobulin BB were 3.0, 3.3, and 5.5 degrees C higher than those of the AA variant in Jenness-Koops, sodium phosphate, and sodium or potassium phosphate buffers, respectively. Although beta-lactoglobulin AB had denaturation temperatures similar to those of AA type in the first two buffers, its denaturation temperature was lowest at 73.4 degrees C in the last buffer system. beta-Lactoglobulin AB was the most stable in water and piperazine-N,N'-bis-(ethanesulfonic acid), and similar denaturation temperatures were obtained for beta-lactoglobulins AA and BB in these solvents. The cooperativity of the transition process was also associated with the genetic types of beta-lactoglobulin. In a 1:1 mixture of beta-lactoglobulin and k-casein; K-casein BB and AB lowered both the onset and denaturation temperatures of beta-lactoglobulin. In contrast, k-casein AA slightly raised the transition temperatures of beta-lactoglobulin.
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