An enzymatic reactor with lipase immobilized on a monolithic polymer support has been prepared and used to catalyze the transesterification of triacylglycerides into the fatty acid methyl esters commonly used for biodiesel. A design of experiments procedure was used to optimize the monolithic reactor with variables including control of the surface polarity of the monolith via variations in the length of the hydrocarbon chain in alkyl methacrylate monomer, time of grafting of 1-vinyl-4,4-dimethylazlactone used to activate the monolith, and time used for the immobilization of porcine lipase. Optimal conditions involved the use of a poly(stearyl methacrylate-co-ethylene dimethacrylate) monolith, grafted first with vinylazlactone, then treated with lipase for 2h to carry out the immobilization of the enzyme. Best conditions for the transesterification of glyceryl tributyrate included a temperature of 37°C and a 10min residence time of the substrate in the bioreactor. The reactor did not lose its activity even after pumping through it a solution of substrate equaling 1,000 reactor volumes. This enzymatic reactor was also used for the transesterification of triacylglycerides from soybean oil to fatty acid methyl esters thus demonstrating the ability of the reactor to produce biodiesel. © 2011 Wiley Periodicals, Inc.
Bibliographical noteKAUST Repository Item: Exported on 2020-10-01
Acknowledgements: Contract grant sponsor: National Institute of Health GM48364Experimental and characterization work performed at the Molecular Foundry, Lawrence Berkeley National Laboratory and F.S. were supported by the Office of Science, Office of Basic Energy Sciences, U.S. Department of Energy, under Contract No. DE-AC02-05CH11231. Financial support of this research by a grant of the National Institute of Health (GM48364) is gratefully acknowledged.
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology