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Updated: Aug 4, 2026

Detecting Cortex Fragments During Bacterial Spore Germination
Published on: June 25, 2016
[Secreted serine proteinase from the spore-forming bacteria Bacillus intermedius 3-19]
Abstract:
Extracellular serine proteinase has been isolated from the cultural medium of Bacillus intermedius 3-19 using CM-cellulose chromatography and affinity chromatography on bacitracin-Sepharose. The specificity of the proteinase with a wide range of natural and synthetic substrates has been investigated. The greatest activity was observed with tripeptides containing C-terminal Leu or Phe. The enzyme was completely inhibited by diisopropylfluorophosphate and partly inhibited by thiol-specific reagents. It is concluded that B. intermedius proteinase is a thiol-dependent serine proteinase pertaining to the subtilisin group. The amino acid composition of the enzyme has been determined. The enzyme contains one to three 1/2 cysteine residues, one of which is supposedly a Cys residue. The N-terminal amino acid sequences of the protein is AQTVPYGIPQIKAPA-.
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