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Journal of Dairy Science Vol. 35 No. 12 1036-1045
© 1952 by American Dairy Science Association ®
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Electrophoretic Properties of Milk Proteins. II. Effect of Heating to 300° F. by Means of the Mallory Small-tube Heat Exchanger1 on Skimmilk Proteins

J. Tobias2, R. McL. Whitney and P. H. Tracy

Department of Food Technology, Universtiy of Illinois, Urbana

ABSTRACT

Mellander (12) was the first to obtain an electrophoretic pattern of skimmilk and of casein. Other investigators (4, 5, 6, 7, 8,14, 21) studied various preparations of casein. Slatter and Van Winkle (15) heated skimmilk to 65, 75 and 85° C. for 30 min. and observed changes in the electrophoretic patterns as a result of the heat treatment. The whey proteins of milk and colostrum have received considerable attention in the past few years (1, 2, 3, 7, 9, 11, 16, 17, 18, 19). While whey is considered to contain six or more components, only the immune globulins (16, 17) and ß-lactoglobulin (1, 2, 9, 11, 18, 19) have been studied in detail.

The present research was undertaken to compare the eleetrophoretie properties of raw skimmilk with those of the same skimmilk heated at one well controlled heating temperature and time of exposure.

EXPERIMENTAL PROCEDURE

Milk as received at the University Creamery was separated and, after securing the unheated sample of skimmilk, the temperature of the balance was raised to 300° F. by means of the Mallory tubular heater.

FOOTNOTES

1 Mallorizer. U. S. Patent no. 2,270,540.

2 The data published here are taken from a thesis presented by the senior autor to the Faculty of the Graduate School, University of Illinois, in partial fulfillment of the requirements for the degree of Doctor of Philosophy, Feb., 1952.






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Copyright © 1952 by the American Dairy Science Association ®.