Some Physicochemical Changes in Quail Egg White During Storage

Abstract The physicochemical changes in the quail egg white stored at 20 and 30 C were examined by several analytical techniques. The final pH's attained in the quail egg albumen were slightly lower than those reported in chicken eggs. Polyacrylamide-gel electrophoretic patterns of albumen proteins became less clear and diffuse in the regions of ovalbumin and ovotransferrin after storage for more than 10 days at 30 C. Conversion of ovalbumin to S-ovalbumin, a more heat-stable form, was observed in the quail egg from the measurement of the changes in solubility and on the thermogram of differential thermal analysis. The ovalbumin, modification progressed slightly slower in the quail egg than in the chicken egg.

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