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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.