Efficient adsorption of lysostaphin on bacterial cells of lysostaphin-resistant Staphylococcus aureus mutant

Microbiol Immunol. 1993;37(1):29-34. doi: 10.1111/j.1348-0421.1993.tb03175.x.

Abstract

A simple and efficient method for the purification of staphylolytic endopeptidase (lysostaphin) contained in culture supernatant of Staphylococcus simulans biovar staphylolyticus strain by adsorption of the enzyme on bacterial cells of lysostaphin-resistant S. aureus mutant was successfully devised. Lysostaphin was sufficiently absorbed on the heat-killed mutant cells derived from S. aureus Cowan I and efficiently eluted by 3 M KSCN. Enzyme preparation obtained by a single procedure of the affinity purification was pure enough for practical use. The yield of the enzyme was 25 mg from 1 liter culture and recovery rate was 64%.

MeSH terms

  • Adsorption
  • Blotting, Western
  • Drug Resistance, Microbial / genetics
  • Electrophoresis, Polyacrylamide Gel
  • Lysostaphin / isolation & purification*
  • Lysostaphin / pharmacokinetics
  • Lysostaphin / pharmacology
  • Mutation
  • Staphylococcus aureus / drug effects
  • Staphylococcus aureus / genetics
  • Staphylococcus aureus / metabolism

Substances

  • Lysostaphin