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Kinetics of enzymatic transesterification and thermal deactivation using immobilized Burkholderia lipase as catalyst

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Abstract

The most effective way of enzymatic synthesis of biodiesel is through lipase-catalyzed transesterification, while its performance and economic feasibility should still be improved. In this study, lipase produced by an isolated Burkholderia sp. was immobilized on microsize Celite materials functionally modified with long alkyl groups. The specific activity of the immobilized lipase was 1,154 U/g. The methanolysis of olive oil catalyzed by the immobilized lipase obeyed Ping Pong Bi Bi model with an estimated V max, K m,TG, K m,M and K i,M value of 0.61 mol/(L min), 7.93 mol/L, 1.01 mol/L, and 0.24 mol/L, respectively. The activation energy of the enzymatic reaction is estimated as 15.51 kJ/mol. The immobilized lipase exhibits high thermal stability with thermal deactivation energy of 83 kJ/mol and a long half-life. The enthalpy, Gibb’s free energy, and entropy of the immobilized lipase were in the range of 80.02–80.35 kJ/mol, 88.35–90.13 kJ/mol, and −28.22 to −25.11 J/(mol K), respectively.

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Acknowledgments

This study was financially supported by the Research Grants (NSC99-2221-E-006-137-MY3 and NSC102-3113-P-006-016-) from Taiwan’s National Science Council. The Top University grants (also known as the “5-year-50-billion” grant) supported by Ministry of Education, Taiwan are also greatly appreciated.

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Authors and Affiliations

  1. Department of Chemical Engineering, National Cheng Kung University, Tainan, 701, Taiwan

    Dang-Thuan Tran & Jo-Shu Chang

  2. Center for Bioscience and Biotechnology, National Cheng Kung University, Tainan, Taiwan

    Jo-Shu Chang

  3. Research Center for Energy Technology and Strategy Center, National Cheng Kung University, Tainan, Taiwan

    Jo-Shu Chang

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  1. Dang-Thuan Tran
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  2. Jo-Shu Chang
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Correspondence to Jo-Shu Chang.

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Tran, DT., Chang, JS. Kinetics of enzymatic transesterification and thermal deactivation using immobilized Burkholderia lipase as catalyst. Bioprocess Biosyst Eng 37, 481–491 (2014). https://doi.org/10.1007/s00449-013-1017-0

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