title: Immobilization of Pseudomonas fluorescens lipase onto magnetic nanoparticles for resolution of 2-octanol.
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.
authors: Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun 130021, People's Republic of China.
authors: Er-na
authors: EN
authors: Xun
authors: Xiao-li
authors: XL
authors: Lv
authors: Wei
authors: W
authors: Kang
authors: Jia-xin
authors: JX
authors: Wang
authors: Hong
authors: H
authors: Zhang
authors: Lei
authors: L
authors: Wang
authors: Zhi
authors: Z
authors: Wang
mesh_terms: D004800:Enzymes, Immobilized / Q000737:chemistry; D006868:Hydrolysis; D008049:Lipase / Q000737:chemistry*; D058185:Magnetite Nanoparticles / Q000737:chemistry*; D000442:Octanols / Q000737:chemistry*; D011551:Pseudomonas fluorescens / Q000201:enzymology*; D013237:Stereoisomerism; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D058185:Magnetite Nanoparticles; D000442:Octanols; C067943:2-octanol; D008049:Lipase