Cc. Chen et Hm. Chang, EFFECT OF THERMAL PROTECTANTS ON THE STABILITY OF BOVINE-MILK IMMUNOGLOBULIN-G, Journal of agricultural and food chemistry, 46(9), 1998, pp. 3570-3576
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 fou
nd to be unstable and susceptible to denaturation when incubated at pH
<4 or >10 or thermally treated at temperature >75 degrees C. IgG in t
he 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 IgG content reduced more sharply wi
th increasing heating times, and almost no IgG content was detected wh
en 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 cont
ents in whey and colostrum were found to be 42 and 59%, respectively.
For IgG in PBS heated at 95 OC for 15 s, addition of 5% fructose or ma
ltose displayed most remarkable protection effects by raising the resi
dual IgG content to 31%, followed by sucrose, lactose, glucose, and ga
lactose. However, extravagant addition (>30%) to IgG in PBS led to a d
ecline in residual Ige 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. Gly
cerol and sugar alcohol, such as sorbitol, stabilized IgG during the t
hermal treatment.