4.6 Article

A monolithic lipase reactor for biodiesel production by transesterification of triacylglycerides into fatty acid methyl esters

Journal

BIOTECHNOLOGY AND BIOENGINEERING
Volume 109, Issue 2, Pages 371-380

Publisher

WILEY
DOI: 10.1002/bit.23326

Keywords

biodiesel; transesterification; lipase; soybean oil; fatty acid methyl esters; polymer monolith; design of experiments; response surface methodology; immobilization

Funding

  1. National Institute of Health [GM48364]
  2. Office of Science, Office of Basic Energy Sciences, U.S. Department of Energy [DE-AC02-05CH11231]

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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 2?h to carry out the immobilization of the enzyme. Best conditions for the transesterification of glyceryl tributyrate included a temperature of 37 degrees C and a 10?min 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. Biotechnol. Bioeng. 2012; 109:371380. (c) 2011 Wiley Periodicals, Inc.

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