Urease activity was found in the fermented broth of a glutamate producing Brevibacterium sp. Maximum glutamic acid production (49 mu mol/ml) was obtained after 48 h fermentation with 2% glucose and 0.5% urea, 98% of available urea was utilized within 36 h of fermentation. The initial concentration of urea in the medium influenced urease activity, maximum specific activity (0.427 mu mol of ammonia liberated per mg protein) of the partially purified enzyme being noted after 12 h of fermentation with 0.25% initial concentration of urea. Urease was most active at pH 7.0 and the optimum temperature was 35 degrees C in the presence of 0.05 Mphosphate buffer.