Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 122, Issue -, Pages 233-239Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2015.09.016
Keywords
Eicosapentaenoyl ethanolamide; Ion pair; Lipozyme 435; Amidation; Synthesis
Funding
- The Natural Science Foundation of Jiangsu Province [BK20150137]
- Fundamental Research Funds for the Central Universities [JUSRP11552]
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Eicosapentaenoyl ethanolamide (EPEA) is a lipid signaling molecule. In this study, an effective process is described to synthesize EPEA by enzymatic amidation using eicosapentaenoic acid ethyl ester (EPA-EE) as acyl donor with lipase as catalyst. The reaction conditions were optimized. When the amidation reaction was conducted at 70 degrees C for 1 h in a solvent-free system with agitation by reacting 2 mmol fatty acid ethyl ester with 3 mmol ethanolamine in presence of 10% Lipozyme 435 as a catalyst, fatty acid ethanolamides was formed at 62.5% molar yield. This was the first time reporting that Lipozyme 435 lipase was used as catalyst for enzymatic amidation. In addition, compared to previous methods using free fatty acid as acyl donor for fatty acid ethanolamide synthesis, study using fatty acid ester as acyl donor is limited and the use of fatty acid ester avoids ion pair formation between free fatty acid and ethanolamine. Finally, we found that Lipozyme 435 lipase had a higher tolerance toward polar ethanolamine as compared to Novozym 435 and Lipozyme RM IM. (C) 2015 Elsevier B.V. All rights reserved.
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