ETUDE DE L'ACETAMIDASE D'UNE SOUCHE DE BREVIBACTERIUM

Abstract

The acetamidase of Brevibacterium R312, a strain with nitrilase activity, has very different characteristics from those of its acetonitrilase. This acetamidase presents an activity for pH values greater than 3 and has an optimum activity at pH 7. The optimal temperature is between 60° and 70°. The enzyme resists high temperatures and its Michaelis constant is 3.5×10^-3M. The -SH, -OH, -NH₂, -NH-C-NH₂, and tryptophan NH groups seem to be necessary for the acetamidase activity. The enzyme remains in supernatant fluid from the centrifugation at 180, 000×g. It is an adaptative enzyme. This acetamidase looks like aliphatic amidases described by other authors.