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Preparation and characterization of Pseudomonas putida esterase immobilized on magnetic nanoparticles

Paper ID Volume ID Publish Year Pages File Format Full-Text
18669 42732 2006 7 PDF Available
Title
Preparation and characterization of Pseudomonas putida esterase immobilized on magnetic nanoparticles
Abstract

A recombinant esterase from Pseudomonas putida IFO12996 covalently bound to magnetic nanoparticles via glutaraldehyde coupling reaction was studied. Magnetic nanoparticles Fe3O4 prepared by coprecipitation of Fe2+ and Fe3+ ions in ammonia solution and they were subsequently treated with 3-aminopropyltriethoxysilane (APES) to obtain amino-silane coated particles. The amino functional group on the particle surface and the amino group of the esterase was coupled with glutaraldehyde. X-ray diffraction (XRD) patterns indicated the particle before and after binding to esterase were pure Fe3O4. Transmission electron microscopy (TEM) showed that the particle with mean diameter of 11.9 nm and binding to esterase did not significantly change its size. Fourier transform infrared (FTIR) spectroscopy confirmed the esterase bound to the particles and the measurement of protein content revealed that the weight ratio of the esterase bound to the magnetic nanoparticles was 0.058 which was about four esterase molecules per particle. The kinetic analysis data indicated that the immobilized esterase retained 63% of its original activity and it exhibited similar thermal and pH stability as free esterase. The immobilized esterase hydrolyzed methyl dl-β-acetylthioisobutyrate (dl-MATI) to give d-β-acetylthioisobutyric acid (DAT) with enatiometric excess value of 97.2% and enantioselectivity value (E-value) of 245. It retained 84% of activity and 40% of conversion after being used for 10 cycles.

Keywords
d-β-Acetylthioisobutyric acid; Captopril; Magnetic nanoparticle
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Preparation and characterization of Pseudomonas putida esterase immobilized on magnetic nanoparticles
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 5, 4 September 2006, Pages 1089–1095
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