[Substrate specificity of enzymes from Bacillus mesentericus].

Area of Science:

• Enzymology
• Microbiology
• Biochemistry

Background:

• Bacillus mesentericus strains are known producers of proteolytic enzymes.
• Understanding the specific activities of these enzymes is crucial for potential biotechnological applications.

Purpose of the Study:

• To isolate and characterize proteolytic enzymes from Bacillus mesentericus strains 64 and 8.
• To compare the substrate specificity and activity of these enzymes with a commercial preparation, terrilytin.

Main Methods:

• Proteolytic enzymes were isolated using affinity chromatography on bacillichine-silochrome.
• Enzyme activity was assessed using various protein substrates (casein, hemoglobin, elastin, albumin) and synthetic peptides.
• Esterase activity was measured via indophenyl acetate cleavage.

Main Results:

• The proteinase from strain 64 showed activity against casein, hemoglobin, and elastin, with specificity similar to terrilytin.
• The proteinase from strain 8 exhibited higher thrombolytic and fibrinolytic activity, along with significant esterase activity.

Conclusions:

• Bacillus mesentericus strains 64 and 8 produce distinct proteolytic enzymes with unique substrate specificities and activities.
• The enzyme from strain 8 demonstrates potential for applications requiring thrombolytic, fibrinolytic, and esterase functions.