摘要 : Heat-induced structural changes in bovine beta-lactoglobulin A were investigated by circular dichroism, differential scanning calorimetry, spectrofluorometry, spectrophotometry and electrical conductivity methods. The alpha-helice... 展开 Heat-induced structural changes in bovine beta-lactoglobulin A were investigated by circular dichroism, differential scanning calorimetry, spectrofluorometry, spectrophotometry and electrical conductivity methods. The alpha-helices, beta-turns, beta-sheets and random coils of beta-lactoglobulin A were severely altered by heating. The sulfhydryl group content of beta-lactoglobulin A at pH 6.7 was increased on heating to 80鳦 and then gradually decreased on heating to 100鳦. Fluorescence intensity, electrical conductivity and absorbance of beta-lactoglobulin A at pH 6.7 were gradually increased on heating from 60 to 85鳦. Differential scanning calorimetric study of beta-lactoglobulin A (pH 6.7) showed that the first and second denaturation peaks were at 85.3 and 135.5鳦 respectively. A gel of 5% beta-lactoglobulin A (pH 6.0) was produced by heating at >63鳦 with a maximum storage modulus of 2.7 X 103 dyne/cm2 at 85鳦. 收起