Enzymatic syntheses of N-lauroyl-β-alanine homologs in organic media |
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Authors: | Taeko Izumi Yoshihiro Yagimuma Masanori Haga |
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Affiliation: | (1) Department of Materials Science and Engineering, Faculty of Engineering, Yamagata University, 4-Choume, Jonan, 992 Yonezawa, Japan |
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Abstract: | Enyzmatic amidation of the primary amines β-alanine ethyl ester and 3-aminopropionitrile with methyl laurate by means of immobilized lipase (Candida antarctica lipase, CAL) resulted in the formation in good yield of N-lauroyl-β-alanine ethyl ester and 3-(N-lauroylamino)-propionitrile, respectively. When 3-amino-propionitrile was used as substrate, diisopropyl ether was a suitable solvent. Changing the reaction temperature (12–80°C) did not affect the yields, and room temperature was a suitable temperature for this reaction. In the investigation of reaction conditions, the use of equimolar amounts (5 mmol) of substrate and ester, along with 0.5 g of CAL, in diisopropyl ether gave the best yield (99.3%) after 24 h of incubation at 24°C. The enzyme activity in the amidation reaction did not decrease even after six uses. With β-alanine ethyl ester hydrochloride as substrate, diisopropyl ether was unsuited as a solvent owing to the low solubility of the substrate in this solvent. In this reaction, the best yield (82.0%) was attained by using dioxane as solvent. CAL achieved higher extents of amide synthesis with long-chain than with short-chain ester substrates. The enzyme accepted only nonbulky primary amines as substrates. |
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Keywords: | Candida antarctica lipase enzymatic amidation N-lauroyl-β -alanine 3-(N-lauroylamino)propionitrile |
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