Abstract
ABSTRACTEffects of the spray‐drying process on egg white proteins were studied by diethylaminoethyl cellulose ion‐exchange chromatography and polyacrylamide gel electrophoresis. Major chromatographic peaks of native egg white were characterized by electrophoresis. Chromatograms and electrophoretographs of native egg white were compared to those of egg white which was adjusted to various pH levels, then spray‐dried. Changes in spray‐dried egg white protein patterns were minor, even at pH levels where conalbumin is heat sensitive. Egg white globulin proteins appear most sensitive to the spray‐drying process. Large scale denaturation of egg white protein does not occur during spray‐drying, but may initiate changes in the protein which affect the functional properties of rehydrated products. Globulin proteins require further characterization in order to properly describe their electrophoretic and chromatographic behavior.
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