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A lipase with broad solvent stability from Burkholderia cepacia RQ3: isolation, characteristics and application for chiral resolution of 1-phenylethanol

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Abstract

Using both polar and low polar organic solvents (DMSO and toluene) as screening stress, a solvent-stable bacterium Burkholderia cepacia RQ3 was newly isolated. An organic solvent-stable lipase from strain RQ3 was purified in a single step with 50.1 % recovery by hydrophobic chromatography. The purified lipase was homogenous on SDS-PAGE and had an apparent molecular mass of 33 kDa. The gene of lipase RQ3 with an open reading frame of 1095 bp encoding 364-amino acid residues was cloned. The optimal pH and temperature for lipase activity were 9.0 and 40 °C. The lipase was stable in a wide pH range of 6.0–10.0 and at temperature below 50 °C. Strikingly, all the tested hydrophilic and hydrophobic organic solvents significantly extended the half-life of lipase RQ3 compared with that in a solvent-free system, which indicated that lipase RQ3 showed a broad solvent tolerance to various organic solvents. The lipase demonstrated excellent enantioselective transesterification toward the (S)-1-phenylethanol with a theoretical conversion yield of 50 % and ee p of 99.9 %, which made it an exploitable biocatalyst for organic synthesis and pharmaceutical industries.

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Acknowledgments

Financial supports for this research from the National Program on Key Basic Research Project (2011CBA00807), the National High Technology Program Research and Development Program of China (2012AA022205) are gratefully acknowledged.

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Correspondence to Bingfang He.

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Xie, C., Wu, B., Qin, S. et al. A lipase with broad solvent stability from Burkholderia cepacia RQ3: isolation, characteristics and application for chiral resolution of 1-phenylethanol. Bioprocess Biosyst Eng 39, 59–66 (2016). https://doi.org/10.1007/s00449-015-1489-1

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