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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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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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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DOI: https://doi.org/10.1007/s00449-015-1489-1