OXIDASE AND CATALASE.
Many enzymes are found in bacteria in a condition which defies extraction except by means of the Buchner press, and it is difficult to obtain luminous bacteria in sufficient quantity for this method. The oxidases seem to be contained in these bacteria in this endoenzyme condition. All my efforts to obtain an oxidase in solution which will oxidize the common oxidase reagents—guaiac, a-napthol, para-pheny len diamine, phenolphthalin, and pyrogallol—have failed, even though hydrogen peroxide is added.
Similar results have been obtained by other workers. Gessard (29) showed that a melanogenic variety of Bacterium pyocyaneum would turn tyrosin brown, but he was unable to separate a solution of tyrosinase from the bacteria. Lehmann and Sano (so) found also that Aciinomyces chromogenes, Bacterium putidum, and B. phosphor esce= would oxidize tyrosin in the culture medium, but Vibrio indices, which phosphoresces strongly, Sarcina lutea, B. typhi, B. coli, and many
others would not. They found in addition that a substance oxidizing aloin and giving a very weak guaiac reaction could be extracted from Actinomyces chromogenes, B. putidum, and B. phosphoreseens by a mix ture of two parts glycerine to one of water, but no tyrosinase reaction could be obtained with this extract. Here also the tyrosinase is appar ently in an endoenzyme condition.
As we shall see (p. 225) the vegetable oxidases are capable of oxidiz ing pyrogallol with light-production, but many attempts to produce light with pyrogallol and extracts of luminous bacteria failed.
Catalase also occurs in the luminous bacteria with which I worked, but in small amount.