EFFECT OF ULTRAPASTEURIZATION WITH AND WITHOUT HOMOGENIZATION ON THE ELECTROPHORETIC PATTERNS OF ASEPTICALLY PROCESSED LIQUID WHOLE EGG

Polyacrylamide gel electrophoresis was performed on ultrapasteurized liquid whole egg (LWE), which was either homogenized or unhomogenized and heated at 64, 68, or 72 C each for 30, 60, or 95 a Native PAGE was used to determine the effect of ultrapasteurization in combination with homogenization on LWE protein. The alpha-livetin band was absent at 72 C for 60 and 95 s processing times but remained present at the 30-s treatment time at 72 C and for all processing times at 64 and 68 C. Protein bands of the globulin/beta-livetin and ovotransferrin/gamma-livetin fractions appear to have faded in all heat-treated samples in comparison with the unheated samples, reflecting their heat instability. Homogenization had no effect on the presence of protein bands identified by PAGE.