Lysostaphine from Staphylococcus staphylolyticus

Purified extracellular lysostaphin from S. staphylolyticus SAE0091 undergoes strict quality control testing to ensure the absence of detectable levels of contaminating DNA using 35 cycles PCR amplification of 16S and 18S rDNA using universal primer sets.
Lysostaphin is a zinc metalloenzyme isolated from a bacterial culture of Staphylococcus staphylolyticus. It has specific lytic action against other Staphylococcus species, including S. aureus.1,2 Lysostaphin has
hexosaminidase, amidase, and endopeptidase activities. It cleaves polyglycine crosslinks in the cellular wall which leads to cell lysis of Staphylococcus species, but not of other bacterial genera. [Pharmaceuticals 2010, 3(4), 1139-1161]
Lysostaphin is a single polypeptide chain of 246 amino acids, a molecular mass of 26,926 Da, isoelectric point of 9.5, (5) and an activity pH optimum of 7.5.(6)

La lysostaphine est une endopeptidase à zinc d'un poids moléculaire de 25 kDa environ. Comme la lysostaphine clive les réticulations de type polyglycine dans la couche de peptidoglycane de la paroi cellulaire de Staphylococcus, elle s'est révélée utile pour la lyse cellulaire et comme potentiel agent thérapeutique anti-microbien.
pH optimal en termes d'activité : ~7,5

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.

Supplied as a lyophilized powder containing 50–70% protein with the balance primarily as NaCl.

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.