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A Calcium-Ion-Stabilized Lipase from Pseudomonas stutzeri ZS04 and its Application in Resolution of Chiral Aryl Alcohols.
- Source :
- Applied Biochemistry & Biotechnology; Dec2016, Vol. 180 Issue 7, p1456-1466, 11p
- Publication Year :
- 2016
-
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). Ca 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 02732289
- Volume :
- 180
- Issue :
- 7
- Database :
- Complementary Index
- Journal :
- Applied Biochemistry & Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 119881681
- Full Text :
- https://doi.org/10.1007/s12010-016-2179-4