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J Bacteriol. 1968 April; 95(4): 1407-1414
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Purification and Properties of Mucor pusillus Acid Protease1

G. A. Somkuti and F. J. Babel

a Department of Animal Sciences, Purdue University, Lafayette, Indiana 47907

ABSTRACT

The protease produced by Mucor pusillus was recovered from a wheat bran medium by treatment with ammonium sulfate, ethyl alcohol, gel filtration and ion-exchange chromatography. The yield of the enzyme was 55%. The overall increase in the specific activity of the protease was 34-fold. The purified protease was most active at pH 3.8 and 5.6 against hemoglobin and casein, respectively. Optimal hydrolysis of casein was observed at 55 C. The enzyme was stable from pH 3.0 to 6.0. Enzyme inactivated by metal ions was reactivated by ethylenediaminetetraacetate and o-phenanthroline. Reducing agents and thiol poisons had no effect on the protease, suggesting that free sulfhydryl groups were not required for enzyme activity. Diisopropyl fluorophosphate did not inhibit the protease, indicating the probable absence of serine in the active center. The Michaelis-Menten constant for casein was 0.357%. Electrophoretic analysis of active protein recovered by ion-exchange chromatography showed that the protease preparation was homogeneous.

FOOTNOTES

1 Presented in part at Annual Meeting of the American Society for Microbiology, New York, New York, 30 April-4 May 1967. Published with the approval of the Director of the Purdue University Agricultural Experiment Station as Journal Series Paper No. 3283.

J Bacteriol. 1968 April; 95(4): 1407-1414
Copyright © 1968 American Society for Microbiology. All Rights Reserved.



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