A bacteriolytic enzyme obtained from the culture filtrate of
Aspergillus melleus was purified by disc electrophoresis and examined for its properties enzymologically and immunologically.
The enzyme was a DFP-sensitive alkaline protease, having residues of either tryptophane, tyrosine, or histidine. Neither metal chelating agents nor thiol poisons inhibited the activity of this proteolytic enzyme.
From experiments concerning the enzymatic inhibition using either bacterial cells or pure casein as the substrates, it was suggested that the bacteriolytic activity of this enzyme was based on its nature to hydrolyze the peptide bonds of the peptidoglycan, a major component of the bacterial cell wall.
In the rabbit sera immunized with this enzyme, there were detected neutralizing and precipitating antibodies which reacted with homologous antigen as well as commercial protease originated from
Aspergillus oryzae. However, the antibodies made no response with purified trypsin, reflecting the immunological difference between trypsin and above mentioned fungal proteases.
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