Abstract
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 s. Native PAGE was used to determine the effect of ultrapasteurization in combination with homogenization on LWE protein. The α-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/β-livetin and ovotransferrin/γ-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.
Published Version
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