Milk Clotting Enzyme from Microorganisms

Part III. The Purification of the Enzyme and Its Properties

Abstract

The purification of the milk clotting enzyme from Mucor pusillus Lindt could be achieved by column chromatography on Amberlite IRC-50 by raising pH from 3.5 to 4.5 and about 70% of activity was recovered after this treatment. After the treatment through the column of DEAE-Sephadex A-25, the trace cellulase activity could be eliminated.
The homogeneity of the purified preparation was proved by ultracentrifugal analysis and electrophoretic patterns at various pH values.
Isoelectric point of this enzyme is considered to lie between pH 3.5 and 3.8.
The enzyme activity was inhibited by Hg⁺⁺ or Fe⁺⁺⁺.
Trypsinogenkinase activity was not contained in this enzyme.