Characterization of Lipases from Staphylococcus aureus and Staphylococcus epidermidis Isolated from Human Facial Sebaceous Skin

Abstract

Two staphylococcal lipases were obtained from Staphylococcus epidermidis S2 and Staphylococcus aureus S11 isolated from sebaceous areas on the skin of the human face. The molecular mass of both enzymes was estimated to be 45 kDa by SDS-PAGE. S2 lipase displayed its highest activity in the hydrolysis of olive oil at 32 o C and pH 8, whereas S11 lipase showed optimal activity at 31 o C and pH 8.5. The S2 lipase showed the property of cold-adaptation, with activation energy of 6.52 kcal/mol. In contrast, S11 lipase's activation energy, at 21 kcal/mol, was more characteristic of mesophilic lipases. S2 lipase was stable up to 45 o C and within the pH range from 5 to 9, whereas S11 lipase was stable up to 50 o C and from pH 6 to 10. Both enzymes had high activity against tributyrin, waste soybean oil, and fish oil. Sequence analysis of the S2 lipase gene showed an open reading frame of 2,067 bp encoding a signal peptide (35 aa), a pro-peptide (267 aa), and a mature enzyme (386 aa); the S11 lipase gene, at 2,076 bp, also encoded a signal peptide (37 aa), pro-peptide (255 aa), and mature enzyme (399 aa). The two enzymes maintained amino acid sequence identity of 98-99% with other similar staphylococcal lipases. Their microbial origins and biochemical properties may make these staphylococcal lipases isolated from facial sebaceous skin suitable for use as catalysts in the cosmetic, medicinal, food, or detergent industries.

Biochemical characterization and molecular modeling of a unique lipase from Staphylococcus arlettae JPBW‐1

“…A molecular weight of 45 kDa was estimated for S. arlettae lipase (comprising ∼410 residues). The molecular weight of S. arlettae lipase was similar to that obtained from Mucor hiemalis (45 kDa) and S. aureus lipase was estimated to be 45 kDa by SDS‐PAGE . Most microbial lipases have a molecular weight ranging from 19 to 60 kDa and are classified as belonging to the α/β hydrolase family with an active site formed by the catalytic triad of Ser, Asp, or Glu, and His residues .…”

Purification and Characterization of Extracellular Lipase from Staphylococcus epidermidis (MTCC 10656)

“…Most of the bacterial lipases were reported to be active at neutral pH and were found to be stable over a broad pH range of 4 to 11 (Dharmsthiti et al 1998;Dong et al 1999). The optimum pH values of lipases obtained from Staphylococcus aureus and Staphylococcus epidermidis were reported as 8 and 8.5 respectively (Troller and Bozeman, 1970;Xie et al, 2012).…”

“…Temperature range for most of the bacterial lipases was reported as 30-60°C (Dharmsthiti and Luchai 1999;Sunna et al, 2002). Temperature optima for lipase produced by staphylococcus species was reported as 32°C by Xie et al, in 2012. …”

“…(Dong et al, 1999), Staphylococcus sp. (Xie et al, 2012), and Chromobacterium sp. (Petra et al, 2001).…”

Lipolytic activity of Staphylococcus aureus from human wounds, animals, foods, and food-contact surfaces in Brazil

“…The pathogenesis of infections caused by S. aureus depends on the production of surface proteins involved in bacterial adhesion to host tissues and of extracellular proteins such as catalase, thermonuclease, coagulase, and lipase [5]. S. aureus is known as a potential lipase-producing, opportunistic pathogenic bacterium that is able to interfere with the immune host defense by eliminating granulocyte chemotaxis and reducing phagocytosis [5][6][7].…”