The effect of temperature upon the denaturation process of ostrich egg‐white protein was studied, and it compared with that of commercial hen eggs. Turbidity and color properties evolution were used to determine this effect. In addition, egg‐white gels (from both ostrich and hen egg whites) were obtained by heat treatment at 80C, and these were characterized by means of color, textural properties and water‐holding capacity (WHC). Results showed that although 55C was the temperature for the start of coagulation in both types of egg white, only in hen egg white was the process completed at 65C. The gels obtained at 80C (both ostrich and hen egg‐white gels) presented a strong structure that would allow ostrich egg white to be used as a gelling agent in the food industry as it happens with hen egg white.
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Fernández‐López et al. (2006) studied this question.
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