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Immobilization of Pseudomonas fluorescens lipase onto magnetic nanoparticles for resolution of 2-octanol
- Source :
- Applied biochemistry and biotechnology. 168(3)
- Publication Year :
- 2011
-
Abstract
- The lipase from Pseudomonas fluorescens (Lipase AK, AKL) was immobilized onto the magnetic Fe3O4 nanoparticles via hydrophobic interaction. Enzyme loading and immobilization yield were determined as 21.4 ± 0.5 mg/g and 49.2 ± 1.8 %, respectively. The immobilized AKL was successfully used for resolution of 2-octanol with vinyl acetate used as acyl donor. Effects of organic solvent, water activity, substrate ratio, and temperature were investigated. Under the optimum conditions, the preferred isomer for AKL is the (R)-2-octanol and the highest enantioselectivity (E = 71.5 ± 2.2) was obtained with a higher enzyme activity (0.197 ± 0.01 μmol/mg/min). The results also showed that the immobilized lipase could be easily separated from reaction media by the magnetic steel and remained 89 % of its initial activity as well as the nearly unchanged enantioselectivity after five consecutive cycles, indicating a high stability in practical operation.
- Subjects :
- 2-Octanol
Octanols
Water activity
Bioengineering
Pseudomonas fluorescens
Applied Microbiology and Biotechnology
Biochemistry
Hydrophobic effect
chemistry.chemical_compound
Vinyl acetate
Lipase
Magnetite Nanoparticles
Molecular Biology
Chromatography
biology
Hydrolysis
Temperature
Substrate (chemistry)
Stereoisomerism
General Medicine
biology.organism_classification
Enzymes, Immobilized
chemistry
Yield (chemistry)
biology.protein
Biotechnology
Subjects
Details
- ISSN :
- 15590291
- Volume :
- 168
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Applied biochemistry and biotechnology
- Accession number :
- edsair.doi.dedup.....0a7f593a9217e3d31d53c446af1bcbc9