ENZYMATIC ACTIVITY OF STAPHYLOCOAGULASE I

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Abstract
A purified preparation of staphylocoagulase, when incubated with egg yolk, was observed to produce turbidity similar to that produced by the toxin (lecithinase) of Clostridium perfringens. A study of the reaction on a group of synthetic methyl and glyceryl esters as substrates revealed a marked specificity for tributyrin. The enzymatic activity has, therefore, been designated a tributyrinase. The coagulase-tributyrin reaction has a pH optimum of 8.0, and a temperature optimum at 38[degree]C. The reaction is zero order in the presence of excess substrate. The pH maximal stability is 7.0, and heat-inactivation of the enzyme is first order.