Immobilization of Pseudomonas fluorescens Lipase onto Magnetic Nanoparticles for Resolution of 2-Octanol

被引：40
|
作者：
Xun, Er-na [1 ]
Lv, Xiao-li [1 ,2 ]
Kang, Wei [1 ,3 ]
Wang, Jia-xin [1 ]
Zhang, Hong [1 ]
Wang, Lei [1 ]
Wang, Zhi [1 ]
机构：
[1] Jilin Univ, Minist Educ, Key Lab Mol Enzymol & Engn, Changchun 130021, Peoples R China
[2] Jilin Univ, Coll Stomatol, Changchun 130041, Peoples R China
[3] Tianjin Vocat Biol Engn Tech Coll, Tianjin 300462, Peoples R China
来源：
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY | 2012年 / 168卷 / 03期
基金：
中国国家自然科学基金;
关键词：
Magnetic nanoparticles; Immobilization; Lipase; 2-Octanol; Resolution; CANDIDA-RUGOSA LIPASE; KINETIC RESOLUTION; ENANTIOSELECTIVITY; (R; S)-2-OCTANOL; ADSORPTION; STABILIZATION; PURIFICATION; PERFORMANCE; IMPROVEMENT; MODULATION;
D O I：
10.1007/s12010-012-9810-9
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 mu 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.
引用
收藏
页码：697 / 707
页数：11
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