Thermal and Functional Properties of Bovine Blood Plasma and Egg White Proteins

Abstract

ABSTRACT All blood plasma proteins denatured at lower temperatures than the major protein of egg white (ovalbumin). γ‐Globulin was the most heat‐stable, and fibrinogen was the most heat‐sensitive protein of blood plasma. The plasma had similar foaming capacity as egg white, but foam stability of plasma was less. Among plasma fractions, serum albumin, fibrinogen, and α‐globulin had good foaming capacities and stabilities. Globulins were the only protein fraction of egg white with good foaming properties. Blood plasma and its component proteins were better emulsifiers than egg white and its component proteins.