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[Purification of protease from staphylococcus aureus (author's transl)]
Zentralblatt Fur Bakteriologie, Parasitenkunde, Infektionskrankheiten Und Hygiene. Erste Abteilung Originale. Reihe A: Medizinische Mikrobiologie Und Parasitologie
|July 1, 1977
Summary
Most Staphylococcus aureus strains exhibit protease activity, which was isolated and purified from M 135 cultures. This study characterizes the enzyme
Area of Science:
- Microbiology
- Enzymology
Context:
- Staphylococcus aureus is a common pathogen in humans and animals.
- Protease production by S. aureus can contribute to its virulence and tissue damage.
Purpose:
- To investigate the prevalence of protease activity in Staphylococcus aureus isolates.
- To isolate, purify, and characterize a specific protease from S. aureus M 135.
Summary:
- 80% of Staphylococcus aureus isolates from humans, cattle, and dogs showed protease activity.
- A protease from S. aureus M 135 was purified using ammonium sulfate precipitation, Ultrogel filtration, and isoelectric focusing.
- The purified protease has a molecular weight of approximately 29,000 Da, an isoelectric point of pH 4.6, and optimal activity between pH 7.5-8.3.
- Enzyme activity was influenced by metal ions, being inhibited by EDTA, Cu2+, and Zn2+, and enhanced by Mn2+.
Impact:
- Characterization of S. aureus protease provides insights into bacterial pathogenesis.
- Understanding protease function can aid in developing targeted antimicrobial strategies.
- The purified enzyme serves as a valuable tool for further biochemical and medical research.