Staphylococcus aureus lipase

Staphylococcus aureus lipase epPCR/ shuffling chromogenic assay 12-fold increase in phospholipase activity 38... 

Enzymic interesterification is a recent development of considerable promise. Its advantage over the more conventional procedures lies in the additional control of product composition. The lipase, coated on to a support material (kieselguhr, hydroxylapatite, alumina) in the presence of a little water, supports interesterification at about 40 °C and usually requires 16-70 h for complete reaction but can be shorter depending on catalyst activity. The process may be operated in a batch or continuous manner. The substrate is a natural oil or fat to which may be added a second oil or fat and/or a particular fatty acid or fatty acid mixture. Three types of enzyme are available. One type (from Candida cylindricae, Coryne-bacterium acnes or Staphylococcus aureus) is nonspecific and leads to complete randomization of all acids at all positions. The product is the same as that obtained from the ordinary catalytic process. A second type of lipase (from Aspergillus niger, Mucor favanicus, Rhizopus arrhizus, / . delemar... 

Schulthess B, Bloes DA, Francois P, Girard M, Schrenzel J, Bischofif M, Beiger-Baechi B. The extracellular nuclease, lipase, and protease expression in Staphylococcus aureus. JBacteriol. 2011 193 4954-62. 

Muraoka, T., T. Ando, and H. Okuda. 1982. Purification and Properties of a Novel Lipase from Staphylococcus Aureus 226. Journal of Biochemistry 92 (6) 1933-1939. 

Poly(caprolactone) The poly(caprolactone] is susceptible to degradation by bacterial lipase and hence in the presence of bacteria such as Staphylococcus aureus, the poly(caprolactone] shell gets degraded resulting in the hydrolysis of the core and release of the drug [68]. 

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