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. 1968 Oct;96(4):1006–1010. doi: 10.1128/jb.96.4.1006-1010.1968

Lipolytic Esterases in Staphylococci

B A Saggers 1, G T Stewart 1
PMCID: PMC252411  PMID: 5685988

Abstract

Staphylococci split a wide range of lipid substrates by production of an enzyme complex with two main components (i) a lipase acting optimally on fat-soluble glycerides, and (ii) an esterase acting optimally on water-soluble esters. The action is dependent upon carbon chain length, interfacial dispersion, solubility, and pH of substrate and end products. The esterase is less susceptible to organophosphorus inhibitors than mammalian esterases. There is no apparent correlation between lipolysis and markers of pathogenicity such as production of coagulase and toxin, but the possession of a flexible lipolytic mechanism might account for the persistence of staphylococci in the fatty secretions of mammalian skin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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