Kinetic study on esterification of palmitic acid catalyzed by glycine-based crosslinked protein coated microcrystalline lipase
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Author list: Raita M., Kiatkittipong W., Laosiripojana N., Champreda V.
Publisher: Elsevier
Publication year: 2015
Journal: Chemical Engineering Journal (1385-8947)
Volume number: 278
Start page: 19
End page: 23
Number of pages: 5
ISSN: 1385-8947
Languages: English-Great Britain (EN-GB)
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Abstract
Enzymatic esterification of fatty acid-rich feedstocks represents an efficient and eco-friendly catalytic process for production of biodiesel. In this study, the reaction kinetics on esterification of palmitic acid with methanol using the heterogeneous glycine-based crosslinked protein coated microcrystalline lipase (CL-PCMC-LIP/Gly) was studied. The maximum FAME yield of over 95% based on a molar basis was achieved at 15% (w/w) enzyme dosage with a 4:1 [MeOH]/[FFA] molar ratio after incubation at 50 ฐC for 1 h in the presence of tert-butanol as a co-solvent. According to the rate equation based on the Ping Pong Bi Bi mechanism model with methanol inhibition, the maximum velocity of the reaction was 4.8 ื 10-3 M/min while the Michaelis-Menten's constants for palmitic acid (Km,PA) and methanol (Km,MeOH) were 2.2 M and 1.4 M, respectively with the inhibition constant of methanol (Ki,MeOH) of 32.6 M. The turnover number (kcat) of CL-PCMC-LIP/Gly was 2.7 min-1 under the optimized experimental condition. The reaction kinetics result provides an important basis for further up-scaling study of the enzymatic esterification process for biodiesel synthesis. ฉ 2015 Elsevier B.V.
Keywords
Palmitic acid
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