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<p>The marine bacterium <i>Alcanivorax borkumensis</i> degrades alkanes derived from phytoplankton, natural hydrocarbon seeps and oil spills. We study the biosynthesis and function of a glycine-glucolipid biosurfactant from <i>A. borkumensis</i> for alkane degradation and identify a gene cluster encoding a nonribosomal peptide synthetase, glycosyltransferase and phosphopantetheinyl transferase. Analyses of <i>A. borkumensis</i> mutants and expression studies reveal that the nonribosomal peptide synthetase catalyzes the synthesis of the aglycone (tetra-<span>d</span>-3-hydroxydecanoyl-glycine) from glycine and <span>d</span>-3-hydroxydecanoyl-CoA, to which a glucose moiety is added by the glycosyltransferase. Deficiency in glycine-glucolipid impairs the ability of mutant cells to attach to the oil–water interface, compromises growth on hexadecane and affects carbon storage. The glycine-glucolipid is essential for biofilm formation on oil droplets and uptake of alkanes. The high incidence of <i>Alcanivorax</i> at oil-polluted sites can in part be explained by the accumulation of the glycine-glucolipid on the cell surface, effectively making the cells themselves act as biosurfactants.</p><p></p>

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Biosurfactant biosynthesis by Alcanivorax borkumensis and its role in oil biodegradation

  • 期刊论文

  • 发表日期：

    2025年5月9日

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  • Jiaxin Cui,
  • Maximilian Fassl,
  • Vaisnavi Vasanthakumaran,
  • Maya Marita Dierig,
  • Georg Hölzl,
  • Tobias Karmainski,
  • Till Tiso,
  • Sonja Kubicki,
  • Stephan Thies,
  • Lars M. Blank,
  • Karl-Erich Jaeger,
  • Peter Dörmann

摘要

The marine bacterium Alcanivorax borkumensis degrades alkanes derived from phytoplankton, natural hydrocarbon seeps and oil spills. We study the biosynthesis and function of a glycine-glucolipid biosurfactant from A. borkumensis for alkane degradation and identify a gene cluster encoding a nonribosomal peptide synthetase, glycosyltransferase and phosphopantetheinyl transferase. Analyses of A. borkumensis mutants and expression studies reveal that the nonribosomal peptide synthetase catalyzes the synthesis of the aglycone (tetra-d-3-hydroxydecanoyl-glycine) from glycine and d-3-hydroxydecanoyl-CoA, to which a glucose moiety is added by the glycosyltransferase. Deficiency in glycine-glucolipid impairs the ability of mutant cells to attach to the oil–water interface, compromises growth on hexadecane and affects carbon storage. The glycine-glucolipid is essential for biofilm formation on oil droplets and uptake of alkanes. The high incidence of Alcanivorax at oil-polluted sites can in part be explained by the accumulation of the glycine-glucolipid on the cell surface, effectively making the cells themselves act as biosurfactants.