The Role of B-Lactoglobulin in the Development of the Core-and-Lining Structure of Casein Particles in Acid-Heat-Induced Milk Gels

Authors

V. R. Harwalkar
Miloslav Kalab

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This work is licensed under a Creative Commons Attribution 4.0 License.

Abstract

Acid-heat-induced gels were obtained by coagulating casein micelle dispersions at 90 C using glucono-and-lactone. The casein micelles used were isolated from raw skim milk by centrifugation, washed free of whey proteins and soluble salts, and dispersed in water or a milk dialyzate. The pH values of the gels varied from 4.7 to 6.3. A core-and-lining ultrastructure developed in casein particles coagulated at pH 5.2 to 5.5 from casein micelle dispersions in the milk dialyzate provided that B-lactoglobulin or whey proteins (10 mg/ml) were added to them prior to coagulation. Addition of B-lactoglobulin to aqueous casein micelle dispersions led to the development of a considerably less distinct core-and-lining ultrastructure of the resulting gels. Coagulated casein particles obtained from casein micelle dispersions in water or in the milk dialyzate to which neither B-lacto-globulin nor whey proteins were added, did not show the core-and-lining ultrastructure but constained void spaces inside and were covered with loosely aggregated protein on the surface.

It was concluded that both B-lactoglobulin or whey proteins and the milk salt system are essential for the formation of the core-and-lining ultrastructure in the casein micelle dispersions gelled by heating at 90 C at pH 5.2 to 5.5.

Recommended Citation

Harwalkar, V. R. and Kalab, Miloslav (1988) "The Role of B-Lactoglobulin in the Development of the Core-and-Lining Structure of Casein Particles in Acid-Heat-Induced Milk Gels," Food Structure: Vol. 7: No. 2, Article 7.
Available at: https://digitalcommons.usu.edu/foodmicrostructure/vol7/iss2/7