Endocellular enzymes of B. coli communis

Abstract

B. coli communis, grown on nutrient broth and agar, was killed by repeated freezings. The cellular extract, after passing through a Berkefeld candle, was tested for enzymic activity an-aerobically at 37[degree] C. The extract hydrolyzes peptone at [rho]h 7-8 but does not affect glucose. The dehydro-genase activity on succinic and formic acids is associated with the stroma but this activity is destroyed for acetic acid, lactic acid, alcohol and glucose. Toluene also destroys the dehydrogenase activity.