Abstract
We investigated the functional properties of egg white, bovine blood plasma, and their component proteins to explain differences in their cake-baking potential. All blood plasma proteins denatured at lower temperatures than the major protein of egg white (ovalbumin). y-Globulin was the most heat stable and fibrinogen was the most heat-sensitive protein of blood plasma. Blood plasma had similar foaming capacity as egg white, but the foam stability of blood plasma protein was significantly less than for egg white. Among blood plasma fractions, serum albumin, fibrinogen, and Cohn fraction IV-1 (predominantly a-globulin) had good foaming capacities and stabilities. Globulins were the only protein fractions in egg white with good foaming properties. Blood plasma and its component proteins were better emulsifiers than egg white and its component proteins. The authors are affiliated with the Dept. of Food Science & Human Nutrition and the Center for Crops Utilization Research, Iowa State Univ., Ames, lA 50011. Address inquiries to L. A. Johnson.
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