STUDIES ON THE LACTASE OF ESCHERICHIA COLI.
A "lactase solution" was prepared from Escherichia coli. The mechanism of its action has been studied and changes in the rate of hydrolysis under various conditions investigated. The hydrolysis of lactose by the enzyme approximates the course of reaction of the integrated Michaelis-Menten equation. One molecule of enzyme combines with one molecule of substrate. E. coli lactase is readily inactivated at pH 5.0, and its optimal activity at 36 degrees C. is reached between pH 7.0 and pH 7.5. The optimal temperature for its action was found to be 46 degrees C. when determinations were carried out after an incubation period of 30 minutes. Its inactivation by heat follows the course of a first order reaction, and the critical thermal increment between the temperatures of 45 degrees C. and 53 degrees C. was calculated to be 56,400 calories per mol. The enzyme is activated by potassium cyanide, sodium sulfide, and cysteine, and irreversibly inactivated by mercuric chloride, silver nitrate, and iodine. After inactivation with copper sulfate partial reactivation is possible, while the slight inhibition brought about by hydrogen peroxide is completely reversible. The possible structure of the active groups of E. coli lactase as compared with other enzymes has been discussed.
Knopfmacher
H P
HP
Department of Bacteriology, University of California, Berkeley.
Salle
A J
AJ