Immobilization of Pseudomonas fluorescens Lipase onto Magnetic Nanoparticles for Resolution of 2-Octanol |
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Authors: | Er-na Xun Xiao-li Lv Wei Kang Jia-xin Wang Hong Zhang Lei Wang Zhi Wang |
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Affiliation: | 1. Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun, 130021, People??s Republic of China 2. College of Stomatology, Jilin University, Changchun, 130041, People??s Republic of China 3. Tianjin Vocational Biological Engineering Technical College, Tianjin developing west district, Tianjin, 300462, People??s Republic of China
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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???mol/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. |
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