Studies on Aspergillus fumigatus; properties of intracellular proteinase.

Mycelial filtrates from Aspergillus fumigatus (AF) hydrolyzed protein substrate buffered at various pH values. Using casein as substrate there were distinct activity optima at pH 2.9, pH 6.2, and pH 10, with maximum activity at pH 6.2. Using haemoglobin as substrate there were activity optima at pH 3.6, pH. 4.6, and pH 10, with the biggest activity peak at pH 4.6. The pH stability at 4°G of the caseinase activity at pH 6.2 and pH 10 was strongest at pH 4, common to both, whereas the caseinase activity at pH 2.9 showed maximum pH stability at pH 6—7. The casein hydrolyzing activity at pH 2.9, pH 6.2, and pH 10 showed different optimum incubation temperatures and irregular heat inactivation. Normal rabbit serum inhibited the caseinase activity at pH 2.9 and pH 6.2 to some extent. The caseinase activity at pH 10 was almost completely inhibited. Antiserum against mycelial filtrate showed no definite inhibition beyond that exerted by normal serum. Following electrophoresis of antiserum, the presence of specific neutralizing antibodies against the casein precipitating enzyme of mycelial filtrate from AF could be established. Investigations of 14 AF strains showed immunological uniformity with respect to the casein precipitating enzyme.