[Serine proteinase with lytic properties]

Area of Science:

• Microbiology
• Enzymology
• Biochemistry

Background:

• Bacillus licheniformis is known to produce extracellular enzymes.
• Serine proteinases are a significant class of enzymes with diverse applications.
• Subtilisin of the Carlsberg type is a well-characterized serine proteinase.

Purpose of the Study:

• To characterize a serine proteinase synthesized by a thermophilic Bacillus licheniformis strain.
• To compare this enzyme with subtilisin of the Carlsberg type.
• To investigate novel properties such as thermostability and lytic activity.

Main Methods:

• Isolation and cultivation of thermophilic Bacillus licheniformis.
• Enzyme purification and characterization (amino acid composition, inhibition patterns, immunochemical properties).
• Assays for thermostability, lytic activity against bacteria and yeast.

Main Results:

• The serine proteinase produced by Bacillus licheniformis shares similarities with subtilisin Carlsberg in composition, specificity, inhibition, and immunochemistry.
• The enzyme exhibits significantly greater thermostability compared to subtilisin Carlsberg.
• The proteinase demonstrates the ability to lyse living cells of Gram-negative bacteria and yeast.

Conclusions:

• The thermophilic Bacillus licheniformis strain synthesizes a unique extracellular serine proteinase.
• This enzyme possesses enhanced thermostability and potent lytic activity against microbial cells.
• The findings suggest potential applications for this enzyme in industrial processes and biotechnology.