Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Characterization of Lipases from Staphylococcus aureus and Staphylococcus epidermidis Isolated from Human Facial Sebaceous Skin

  • Xie, Winny (Division of Biotechnology, The Catholic University of Korea) ;
  • Khosasih, Vivia (Division of Biotechnology, The Catholic University of Korea) ;
  • Suwanto, Antonius (Faculty of Biotechnology, Atma Jaya Catholic University of Indonesia) ;
  • Kim, Hyung-Kwoun (Division of Biotechnology, The Catholic University of Korea)
  • Received : 2011.07.27
  • Accepted : 2011.09.15
  • Published : 2012.01.28
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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 $32^{\circ}C$ and pH 8, whereas S11 lipase showed optimal activity at $31^{\circ}C$ 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 $45^{\circ}C$ and within the pH range from 5 to 9, whereas S11 lipase was stable up to $50^{\circ}C$ 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.

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