Biocatalytic esterification of palm oil fatty acids for biodiesel production using glycine-based cross-linked protein coated microcrystalline lipase
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Author list: Raita M., Laothanachareon T., Champreda V., Laosiripojana N.
Publisher: Elsevier
Publication year: 2011
Journal: Journal of Molecular Catalysis B: Enzymatic (1381-1177)
Volume number: 73
Issue number: #
Start page: 74
End page: 79
Number of pages: 6
ISSN: 1381-1177
eISSN: 1873-3158
Languages: English-Great Britain (EN-GB)
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Abstract
Conversion of feedstocks containing high free fatty acid contents to alkyl esters is limited by the currently used alkali-catalyzed biodiesel synthesis process. In this study, esterification of palm fatty acids to ethyl esters was studied using heterogeneous cross-linked protein coated microcrystalline (CL-PCMC) lipase. Optimization of biocatalyst synthesis by variation of matrix components and organic solvents showed that highly active CL-PCMCs could be prepared from Thermomyces lanuginosus lipase with glycine as the core matrix in acetone. The optimized reaction contained 20% (w/w) glycine-based CL-PCMC-lipase, a 1:4 fatty acid molar equivalence to ethanol in the presence of an equimolar amount of tert-butanol which led to production of 87.2% and 81.4% (mol/mol) of ethyl ester from palmitic acid and industrial palm fatty acid distillate (PFAD), respectively after incubation at 50 ฐC for 6 h. CL-PCMC-lipase is more catalytically efficient than protein coated microcrystalline (PCMC) lipase, Novozymeฎ435 and Lipolase 100T for both free fatty acids and palm fatty acid distillate. The CL-PCMC-lipase showed high operational stability with no significant loss in product yield after 8 consecutive batch cycles. The glycine-based microcrystalline lipase is thus a promising alternative economical biocatalyst for biodiesel production from inexpensive feedstocks with high free fatty acid contents. ฉ 2011 Elsevier B.V. All Rights Reserved.
Keywords
Crosslinked protein coated microcrystals