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Improving Pseudomonas sp. esterase performance by engineering approaches for kinetic resolution of 2-acetoxyphenylacetic acids

Paper ID Volume ID Publish Year Pages File Format Full-Text
3747 185 2011 6 PDF Available
Title
Improving Pseudomonas sp. esterase performance by engineering approaches for kinetic resolution of 2-acetoxyphenylacetic acids
Abstract

The catalytic performance of Pseudomonas sp. ECU1011 esterase (PsE) in the kinetic resolution of (R,S)-2-acetoxyphenylacetic acid (APA) was significantly improved by substrate modification, biocatalyst permeabilization and immobilization. The reaction system was modified, and the sodium salt of the substrate (APA Na), instead of APA, was hydrolyzed in aqueous phase without buffer. Considering the improved substrate solubility and the decreased biocatalyst inactivation, the reaction rate increased 3.7-folds and the spontaneous hydrolysis of the substrate reduced by 48%. During the cell permeabilization, the hydrolytic activity of the whole-cell biocatalyst was increased by 2.3-fold after 2 h of pretreatment with 10% (v/v) toluene. The permeabilized cells were further entrapped in calcium alginate, resulting in 171% activity recovery with a half-life of 123 h at 30 °C. Using the modified reaction system with high reaction rates and the modified biocatalyst with high activity and stability, this biocatalytic process can be transformed into a practical and environmentally friendly bioprocess for the efficient production of (S)-mandelic acid and (S)-o-chloromandelic acid.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Repeated resolution of (R,S)-2-acetoxyphenylacetic acids with a new esterase (PsE) with high enantioselectivity. ► Reaction rate was raised 3.7-folds by using sodium salt of the acidic substrates. ► Spontaneous hydrolysis of substrate is depressed by half in the reformed reaction system. ► Permeabilization and immobilization of whole-cell PsE as provide efficient and stable biocatalysts.

Keywords
Biocatalysis; Bioprocess design; Enantioseparation; Pseudomonas sp. Esterase; Immobilized cells; Mandelic acid; o-Chloromandelic acid
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Improving Pseudomonas sp. esterase performance by engineering approaches for kinetic resolution of 2-acetoxyphenylacetic acids
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 57, 15 November 2011, Pages 63–68
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us