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  • Immobilization of Pseudomonas fluorescens lipase onto magnetic nanoparticles for resolution of 2-octanol.

Immobilization of Pseudomonas fluorescens lipase onto magnetic nanoparticles for resolution of 2-octanol.

Applied biochemistry and biotechnology (2012-08-01)
Er-na Xun, Xiao-li Lv, Wei Kang, Jia-xin Wang, Hong Zhang, Lei Wang, Zhi Wang
ABSTRACT

The lipase from Pseudomonas fluorescens (Lipase AK, AKL) was immobilized onto the magnetic Fe(3)O(4) 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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
2-Octanol, ≥97%, FG
Sigma-Aldrich
(S)-(+)-2-Octanol, 99%
Sigma-Aldrich
2-Octanol, 97%
Sigma-Aldrich
(±)-2-Octanol, ReagentPlus®, ≥99.5% (GC)
Sigma-Aldrich
(±)-2-Octanol, ≥96.0% (GC)