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L2898 Sigma-Aldrich

Lysostaphin from Staphylococcus staphylolyticus

aseptically filled

Synonym: Glycyl-glycine Endopeptidase

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Properties

Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Antibiotics, Antibiotics A to Z, Antibiotics G-M,
Quality Level   200
sterility   aseptically filled
form   powder
specific activity   >500 units/mg protein
mol wt   25 kDa
composition   Protein, 40-70% biuret
Mode of action   cell wall synthesis | interferes
antibiotic activity spectrum   Gram-positive bacteria
storage temp.   −20°C

Description

General description

Chemical structure: peptide

Lysostaphin is mainly liberated as a proenzyme. It is highly stable at pH 4 and temperature 5°C.

Biochem/physiol Actions

Lysostaphin exhibit a lytic action against Staphylococcus aureus. It possesses several functions of three major enzymes, such as, glycylglycine endopeptidase, endo-β-N-acetyl glucosamidase and N-acteyl muramyl-L-alanine amidase. Lysostaphin can be used to treat antibiotic-resistant staphylococcal infections. Lysostaphin being an antistaphylococcal agent, can be used as a preservative in the food industry and in clinical labs for rapid screening.

Lysostaphin is a zinc endopeptidase with a molecular weight of approximately 25 kDa. Because lysostaphin cleaves the polyglycine cross-links in the peptidoglycan layer of the cell wall of Staphylococcus species it has been found useful for cell lysis and also as a potential anti-microbial therapeutic.
pH Optimum for activity: ~7.5

Unit Definition

One unit will reduce the turbidity (A620) of a suspension of Staphylococcus aureus cells from 0.250 to 0.125 in 10 min at pH 7.5 at 37 °C in a 6.0 ml reaction mixture.

Preparation Note

Prepared from L 7386

Safety & Documentation

Safety Information

Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 3
RTECS 
OL5985000
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable

Documents

Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Protocols & Articles

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Peer-Reviewed Papers
15

References

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