Urease activity was found in the fermented broth of a glutamate produc
ing Brevibacterium sp. Maximum glutamic acid production (49 mu mol/ml)
was obtained after 48 h fermentation with 2% glucose and 0.5% urea, 9
8% of available urea was utilized within 36 h of fermentation. The ini
tial concentration of urea in the medium influenced urease activity, m
aximum specific activity (0.427 mu mol of ammonia liberated per mg pro
tein) of the partially purified enzyme being noted after 12 h of ferme
ntation with 0.25% initial concentration of urea. Urease was most acti
ve at pH 7.0 and the optimum temperature was 35 degrees C in the prese
nce of 0.05 Mphosphate buffer.