Magnetic nanoparticles supported ionic liquids for lipase immobilization: Enzyme activity in catalyzing esterification

• Published in: Journal of molecular catalysis. B, Enzymatic Vol. 58; no. 1; pp. 103 - 109
• Main Authors: Jiang, Yangyang, Guo, Chen, Xia, Hansong, Mahmood, Iram, Liu, Chunzhao, Liu, Huizhou
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.06.2009; Elsevier
• Subjects: Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Esterification; Fundamental and applied biological sciences. Psychology; Ionic liquids; Lipase immobilization; Magnetic nanoparticle; Methods. Procedures. Technologies; Magnetic nanoparticle; Ionic liquids; Esterification; Lipase immobilization; Support; Enzyme; Nanoparticle; Immobilization; Triacylglycerol lipase; Esterases; Carboxylic ester hydrolases; Ionic liquid; Magnetic; Enzymatic activity; Hydrolases
• ISSN: 1381-1177; 1873-3158
• DOI: 10.1016/j.molcatb.2008.12.001

Candida rugosa lipase was immobilized on magnetic nanoparticles supported ionic liquids having different cation chain length (C 1, C 4 and C 8) and anions (Cl −, BF 4 − and PF 6 −). Magnetic nanoparticles supported ionic liquids were obtained by covalent bonding of ionic liquids–silane on magnetic silica nanoparticles. The particles are superparamagnetic with diameter of about 55 nm. Large amount of lipase (63.89 mg/(100 mg carrier)) was loaded on the support through ionic adsorption. Activity of the immobilized lipase was examined by the catalysis of esterification between oleic acid and butanol. The activity of bound lipase was 118.3% compared to that of the native lipase. Immobilized lipase maintained 60% of its initial activity even when the temperature was up to 80 °C. In addition, immobilized lipase retained 60% of its initial activity after 8 repeated batches reaction, while no activity was detected after 6 cycles for the free enzyme.