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

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Abstract
The primary and secondary phases of rennin action on whole casein and K- casein were investigated by high resolution starch gel electrophoresis. K-Casein was the only component of whole casein attacked during 50 rain of enzyme action, resulting in one major and two minor components with faster mobilities than whole a~-casein and two minor com- ponents with slower mobilities than K-casein. Thirty and six-tenths per cent and 48.4% of the K-casein were solubilized at pH 4.60 after 60 and 120 rain of rennin action at pH 6.80 and 36 C. The balance of the ~- casein aggregated. The para-K-caseins re- sulting from 60 and 130 rain of rennin ac- tion showed an electrophoretic composition similar to that reported by others (3, 10). The 12% trichloroacetic acid insoluble pro- duct recovered from ~-casein after 30 rain of rennin action showed a complex electro- phoretie p~ttern composed of at least 14 components. No specific electrophoretic changes ac- companied the eoagulum characterizing the secondary phase of rennin action on whole casein.