An organic solvent and thermally stable lipase from Burkholderia ambifaria YCJ01: Purification, characteristics and application for chiral resolution of mandelic acid

作者：Yao, Changjin; Cao, Yan; Wu, Shanshan; Li, Shuang; He, Bingfang^*

来源：Journal of Molecular Catalysis B: Enzymatic , 2013, 85-86: 105-110.

DOI：10.1016/j.molcatb.2012.08.016

• Organic solvent stability
• Lipase
• Burkholderia ambifaria
• Chiral resolution
• Mandelic acid

A solvent-tolerant bacterium Burkholderia ambifaria YCJ01 was newly isolated by DMSO enrichment of the medium. The lipase from the strain YCJ01 was purified to homogeneity with apparent molecular mass of 34 kDa determined by SOS-PAGE. The purified lipase exhibited maximal activity at a temperature of 60 degrees C and a pH of 7.5. The lipase was very stable below 55 degrees C for 7 days (remaining 80.3% initial activity) or at 30 degrees C for 60 days. PMSF significantly inhibited the lipase activity, while EDTA had no effect on the activity. Strikingly, the lipase showed distinct super-stability to the most tested hydrophilic and hydrophobic solvents (25%, v/v) for 60 days, and different optimal pH in contrast with the alkaline lipase from B. cepacia S31. The lipase demonstrated excellent enantioselective transesterification toward the S-isomer of mandelic acid with a theoretical conversion yield of 50%. ee(p) of 99.9% and ee(s) of 99.9%, which made it an exploitable biocatalyst for organic synthesis and pharmaceutical industries.

• 出版日期2013-1
• 单位南京工业大学