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A Calcium-Ion-Stabilized Lipase from Pseudomonas stutzeri ZS04 and its Application in Resolution of Chiral Aryl Alcohols
- Qin, Song, Zhao, Yangyang, Wu, Bin, He, Bingfang
- Applied biochemistry and biotechnology 2016 v.180 no.7 pp. 1456-1466
- Pseudomonas stutzeri, alcohols, bacteria, biocatalysis, biocatalysts, calcium, carboxylic ester hydrolases, dimethyl sulfoxide, drugs, enantiomers, engineering, esterification, hydrophilicity, hydrophobicity, pH, polluted soils, soil sampling, solvents, substrate specificity, temperature, thermal stability
- An extracellular organic solvent-tolerant lipase-producing bacterium was isolated from oil-contaminated soil samples and was identified taxonomically as Pseudomonas stutzeri, from which the lipase was purified and exhibited maximal activity at temperature of 50 °C and pH of 9.0. Meanwhile, the lipase was stable below or at 30 °C and over an alkaline pH range (7.5–11.0). Ca²⁺ could significantly improve the lipase thermal stability which prompts a promising application in biocatalysis through convenient medium engineering. The lipase demonstrated striking features such as distinct stability to the most tested hydrophilic and hydrophobic solvents (25 %, v/v), and DMSO could activate the lipase dramatically. In the enzyme-catalyzed resolution, lipase ZS04 manifested excellent enantioselective esterification toward the (R)-1-(4-methoxyphenyl)-ethanol (MOPE), a crucial chiral intermediate in pharmaceuticals as well as in other analogs with strict substrate specificity and theoretical highest conversion yield. This strong advantage over other related schemes made lipase ZS04 a promising biocatalyst in organic synthesis and pharmaceutical applications.