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I Until recently it has been the custom in this laboratory to name the organism Bacillus granulobacter-pectinovorum; but, in order to minimize confusion, the name suggested by McCoy, Fred, Peterson and Hastings (1926) has been adopted in this paper. The strain of the organism employed throughout all of our investigations is the original strain which was utilized industrially in Toronto during the war. 209

INTRODUCTION. IN a previous paper [Heard and Wynne, 1933] the presence of a phosphatase in active glucose-peptone cultures of Clostridium acetobutylicum Weizmann was reported. It is the purpose of the present communication to describe some of the properties of this enzyme and of a similar enzyme present in Propionibacterium jensenii van Niel. Each of these organisms ferments various carbohydrates and certain related compounds. The first produces, as the chief endproducts of glucose or starch breakdown, carbon dioxide, hydrogen, acetone, ethyl and butyl alcohols; the acetone and alcohols are derived from acetic and butyric acids formed as intermediary compounds. The second organism may be regarded as being representative of a rather large group of bacteria which ferment sugars and some related compounds with the formation of acetic and propionic acids [van Niel, 1928]. Phosphatases exhibit marked differences in their pH-activity relationships. Those of mammalian tissues are, in most cases, much more active under alkaline than acid conditions, irrespective of the nature of the substrate. Usually the speed of hydrolysis reaches a maximum at about PH 9, although, as Kay [1932] points out, this is probably only an apparent optimum since inactivation of the enzyme in more alkaline media may affect the exact identification of the optimum reaction. Roche [1931] observed that the phosphatase of certain mammalian erythrocytes appeared to differ from other mammalian phosphatases since it had a PH optimum of 5*8 to 6-8 varying with the substrate. Among fungi and higher plants the few phosphatase systems which have been investigated are all most active under acid conditions. For example, the enzymes of Aspergillus oryzae and A. niger have PH optima varying from 3-1 to 5-5 according to the method of preparation and the nature of the substrate [Asakawa, 1929].