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Abstract <p>Lipases are versatile biocatalysts widely applied in hydrolysis and synthesis reactions, yet bacterial acidophilic and solvent-tolerant lipases remain poorly characterized. In this study, an acid- and organic solvent-resistant lipase (LipC) and its cognate foldase (LifB) from <i>Burkholderia gladioli</i> Bsp-1 were cloned and heterologously expressed in <i>Escherichia coli</i>. Soluble and catalytically active LipC was obtained only upon co-expression with LifB, demonstrating a strict foldase-dependent folding requirement. Phylogenetic analysis classified LipC as a LipA-type bacterial lipase. Biochemical characterization revealed that LipC exhibited maximal activity at pH 3.5 and showed remarkable stability under acidic conditions, retaining more than 70% of its activity after prolonged incubation at pH 4.0. The enzyme displayed optimal activity at 55 ℃ and maintained moderate thermal stability. Notably, LipC retained high activity in nonpolar organic solvents, with significant activation observed in n-hexane and cyclohexane. Substrate specificity and kinetic analysis indicated a preference for medium-chain fatty acid esters, with the highest catalytic efficiency toward p-nitrophenyl caprate (C10). Collectively, these results identify LipC as a foldase-dependent bacterial lipase combining acidophilic behavior and solvent tolerance, expanding the current understanding of bacterial lipases and highlighting their potential relevance for biocatalysis under acidic and nonaqueous conditions.</p> Key points <p>•&#xa0;<i>LipC is a foldase-dependent bacterial lipase requiring LifB for functional expression</i>.</p> <p>•&#xa0;<i>LipC exhibits strong acidophilicity with optimal activity at pH 3.5</i>.</p> <p>•&#xa0;<i>LipC is highly activated by nonpolar solvents such as n-hexane and cyclohexane</i>.</p>

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Co-expression, purification, and characterization of an acidophilic and n-hexane-tolerant lipase with its foldase from Burkholderia gladioli Bsp-1

  • 期刊论文

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  • 发表日期：

    2026年3月28日

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  • Zhu Jing,
  • Zuo Xiaoqiong,
  • Mai Lanqiu,
  • Qin Yan,
  • Xian Liang,
  • Li Yi,
  • Wang Qingyan

摘要

Abstract

Lipases are versatile biocatalysts widely applied in hydrolysis and synthesis reactions, yet bacterial acidophilic and solvent-tolerant lipases remain poorly characterized. In this study, an acid- and organic solvent-resistant lipase (LipC) and its cognate foldase (LifB) from Burkholderia gladioli Bsp-1 were cloned and heterologously expressed in Escherichia coli. Soluble and catalytically active LipC was obtained only upon co-expression with LifB, demonstrating a strict foldase-dependent folding requirement. Phylogenetic analysis classified LipC as a LipA-type bacterial lipase. Biochemical characterization revealed that LipC exhibited maximal activity at pH 3.5 and showed remarkable stability under acidic conditions, retaining more than 70% of its activity after prolonged incubation at pH 4.0. The enzyme displayed optimal activity at 55 ℃ and maintained moderate thermal stability. Notably, LipC retained high activity in nonpolar organic solvents, with significant activation observed in n-hexane and cyclohexane. Substrate specificity and kinetic analysis indicated a preference for medium-chain fatty acid esters, with the highest catalytic efficiency toward p-nitrophenyl caprate (C10). Collectively, these results identify LipC as a foldase-dependent bacterial lipase combining acidophilic behavior and solvent tolerance, expanding the current understanding of bacterial lipases and highlighting their potential relevance for biocatalysis under acidic and nonaqueous conditions.

Key points

• LipC is a foldase-dependent bacterial lipase requiring LifB for functional expression.

• LipC exhibits strong acidophilicity with optimal activity at pH 3.5.

• LipC is highly activated by nonpolar solvents such as n-hexane and cyclohexane.