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Lipase Immobilized on the Hydrophobic Polytetrafluoroethene Membrane with Nonwoven Fabric and Its Application in Intensifying Synthesis of Butyl Oleate

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Abstract

The synthesis of butyl oleate was studied in this paper with immobilized lipase. Five types of membrane were used as support to immobilize Rhizopus arrhizus lipase by following a procedure combining filtration and protein cross-linking. Results showed that hydrophobic polytetrafluoroethene membrane with nonwoven fabric (HO-PTFE-NF) was the favorite choice in terms of higher protein loading, activity, and specific activity of immobilized lipase. The factors including solvent polarity, lipase dosage, concentration, and molar ratio of substrate and temperature were found to have significant influence on conversion. Results showed that hexane (logP = 3.53) was a favorable solvent for the biosynthesis of butyl oleate in our studies. The optimal conditions were experimentally determined of 50 U immobilized lipase, molar ratio of oleic acid to butanol of 1.0, substrate concentration of 0.12 mol/L, temperature of 37 °C, and reaction time of 2 h. The conversion was beyond 91% and decreased slightly after 18 cycles. Lipase immobilization can improve the conversion and the repeated use of immobilized lipase relative to free lipase.

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Acknowledgements

The authors are grateful to the National High Technology Research and Development Program of China (863) (NO.2007AA06Z310) and the Foundation of Beijing University of Chemical Technology for financial support.

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Authors and Affiliations

  1. State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, China

    Shu-Guang Wang, Wei-Dong Zhang, Zheng Li, Zhong-Qi Ren & Hong-Xia Liu

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  1. Shu-Guang Wang
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  2. Wei-Dong Zhang
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  5. Hong-Xia Liu
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Correspondence to Wei-Dong Zhang.

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Wang, SG., Zhang, WD., Li, Z. et al. Lipase Immobilized on the Hydrophobic Polytetrafluoroethene Membrane with Nonwoven Fabric and Its Application in Intensifying Synthesis of Butyl Oleate. Appl Biochem Biotechnol 162, 2015–2026 (2010). https://doi.org/10.1007/s12010-010-8977-1

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