Isolation and Characterization of Two Protease-Producing Mutants from Staphylococcus aureus
AUTOR(ES)
Rydén, Ann-Christine
RESUMO
Two mutants with increased protease production were isolated after nitrosoguanidine treatment of Staphylococcus aureus 8325N. The wild type produces low amounts of extracellular proteolytic activity. The enzyme was inducible and could only be detected if casein or preferably skim milk powder was used as inducer. The optimal pH, salt concentration, and media for enzyme production were determined. The mutants differed from the wild type in several phenotypic characters. The pattern of extracellular deoxyribonuclease and alkaline phosphatase differed between the mutants and the wild type. Several carbohydrates such as lactose, galactose, and mannitol were not utilized by the mutants, probably owing to a block in the uptake. Glucose could, however, be utilized by the mutants. Reversion frequency to wild type with regard to carbohydrate utilization was spontaneously high, and all revertants regained the parental pattern irrespective of the carbohydrate used for selection. The results suggest that a single locus may control the excretion of extracellular enzymes and carbohydrate uptake in S. aureus.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=246386Documentos Relacionados
- Use of a Packed-Column Bioreactor for Isolation of Diverse Protease-Producing Bacteria from Antarctic Soil
- Ecology and nature of immunoglobulin A1 protease-producing streptococci in the human oral cavity and pharynx.
- Isolation and characterization of lysozyme-sensitive mutants of Staphylococcus aureus.
- Similar proportions of immunoglobulin A1 (IgA1) protease-producing streptococci in initial dental plaque of selectively IgA-deficient and normal individuals.
- Isolation and Characterization of a Kanamycin Resistance Plasmid from Staphylococcus aureus