Effect of thermal protectants on the stability of bovine milk immunoglobulin G
1998
Chen, C.C. | Chang, H.M.
pH stability, thermal stability, and the effect of homogenization and ultrasonic treatment on the stability of bovine milk immunoglobulin G (IgG) in model systems was studied. Separated IgG (0.02 mg/mL) was found to be unstable and susceptible to denaturation when incubated at pH < 4 or > 10 or thermally treated at temperature > 75 degrees C. IgG in the colostrum, on the other hand, was found to be much more stable than in whey or in PBS when thermally treated at temperatures in the range of 75-100 degrees C. The residual IgC content reduced more sharply with increasing heating times, and almost no IgG content was detected when IgG in PBS (0.15 M NaCl/0.01 M phosphate buffer, pH 7.0) was heated at 95 degrees C for 15 s, whereas the corresponding residual IgG contents in whey and colostrum were found to be 42 and 59%, respectively. For IgG in PBS heated at 95 degrees C for 15 s, addition of 5% fructose or maltose displayed most remarkable protection effects by raising the residual IgG content to 31%, followed by sucrose, lactose, glucose, and galactose. However, extravagant addition (> 30%) to IgG in PBS led to a decline in residual IgG content. Addition of 0.4% glutamic acid and 2% glycine to IgG in PBS heated at 95 degrees C for 15 s also remarkably improved the residual IgG content by 13.5 and 26.7%, respectively. Glycerol and sugar alcohol, such as sorbitol, stabilized IgG during the thermal treatment.
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