Elastolytic activity of the halotolerant strain Bacillus pumilus CMM 5
21, isolated from an unidentified sponge obtained from a depth of 120
m near Iturup Island (the Kurile Islands), was investigated. The strai
n was grown in a peptone-yeast extract medium supplemented with elasti
n and seawater. Elastase was shown to be a secretory enzyme. Specific
elastolytic activity of the culture was maximal after 48 h of growth.
The enzyme was partially purified from the culture liquid by fractiona
tion with ammonium sulfate. The elastase purified in this manner exhib
ited a specific activity of 119 units/mg protein. Elastase was found t
o be a thermolabile metal-dependent enzyme with a pH-optimum from 8.0
to 9.0. In the presence of 0.5% NaCl, the enzyme retained 85% of its a
ctivity.