A Calcium-Ion-Stabilized Lipase from <Emphasis Type="Italic">Pseudomonas stutzeri</Emphasis> ZS04 and its Application in Resolution of Chiral Aryl Alcohols |
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Authors: | Song Qin Yangyang Zhao Bin Wu Bingfang He |
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Institution: | 1.Pharmaceutical College,Nanjing Technology University,Nanjing,China;2.College of Biotechnology and Pharmaceutical Engineering,Nanjing Technology University,Nanjing,China;3.Innovent Biologics Co. Ltd.,Suzhou,China |
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Abstract: | 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. |
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