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

Handle URI:
http://hdl.handle.net/10754/561880
Title:
A monolithic lipase reactor for biodiesel production by transesterification of triacylglycerides into fatty acid methyl esters
Authors:
Urban, Jiří T.; Švec, František; Frechet, Jean ( 0000-0001-6419-0163 )
Abstract:
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.
KAUST Department:
Chemical Science Program; Physical Sciences and Engineering (PSE) Division
Publisher:
Wiley-Blackwell
Journal:
Biotechnology and Bioengineering
Issue Date:
26-Sep-2011
DOI:
10.1002/bit.23326
PubMed ID:
21915852
PubMed Central ID:
PMC3240714
Type:
Article
ISSN:
00063592
Sponsors:
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.
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3240714
Appears in Collections:
Articles; Physical Sciences and Engineering (PSE) Division; Chemical Science Program

Full metadata record

DC FieldValue Language
dc.contributor.authorUrban, Jiří T.en
dc.contributor.authorŠvec, Františeken
dc.contributor.authorFrechet, Jeanen
dc.date.accessioned2015-08-03T09:33:10Zen
dc.date.available2015-08-03T09:33:10Zen
dc.date.issued2011-09-26en
dc.identifier.issn00063592en
dc.identifier.pmid21915852en
dc.identifier.doi10.1002/bit.23326en
dc.identifier.urihttp://hdl.handle.net/10754/561880en
dc.description.abstractAn 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.en
dc.description.sponsorshipContract 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.en
dc.publisherWiley-Blackwellen
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3240714en
dc.subjectBiodieselen
dc.subjectDesign of experimentsen
dc.subjectFatty acid methyl estersen
dc.subjectImmobilizationen
dc.subjectLipaseen
dc.subjectPolymer monolithen
dc.subjectResponse surface methodologyen
dc.subjectSoybean oilen
dc.subjectTransesterificationen
dc.titleA monolithic lipase reactor for biodiesel production by transesterification of triacylglycerides into fatty acid methyl estersen
dc.typeArticleen
dc.contributor.departmentChemical Science Programen
dc.contributor.departmentPhysical Sciences and Engineering (PSE) Divisionen
dc.identifier.journalBiotechnology and Bioengineeringen
dc.identifier.pmcidPMC3240714en
dc.contributor.institutionDepartment of Chemistry, University of California, Berkeley, CA 94720, United Statesen
dc.contributor.institutionThe Molecular Foundry, E.O. Lawrence Berkeley National Laboratory, Berkeley, CA, United Statesen
kaust.authorFrechet, Jeanen
All Items in KAUST are protected by copyright, with all rights reserved, unless otherwise indicated.