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Starch Gel Electrophoresis of Products of Action of Crystalline Rennin on Casein and Its Components¹

Department of Animal and Range Sciences, Montana State University, Bozeman

ABSTRACT

The primary and secondary phases of rennin action on whole casein and -casein were investigated by high resolution starch gel electrophoresis. -Casein was the only component of whole casein attacked during 50 min of enzyme action, resulting in one major and two minor components with faster mobilities than whole _s-casein and two minor components with slower mobilities than -casein. Thirty and six-tenths per cent and 48.4% of the -casein were solubilized at pH 4.60 after 60 and 120 min of rennin action at pH 6.80 and 36 C. The balance of the -casein aggregated. The para--caseins resulting from 60 and 130 min of rennin action showed an electrophoretic composition similar to that reported by others (3, 10). The 12% trichloroacetic acid insoluble product recovered from -casein after 30 min of rennin action showed a complex electrophoretic pattern composed of at least 14 components.

No specific electrophoretic changes accompanied the coagulum characterizing the secondary phase of rennin action on whole casein.

¹ A contribution from Montana State University, Agricultural Experiment Station. Paper no. 850, Project no. 150.