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Enzymatic syntheses of N ‐lauroyl‐β‐alanine homologs in organic media
Author(s) -
Izumi Taeko,
Yagimuma Yoshihiro,
Haga Masanori
Publication year - 1997
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-997-0231-9
Subject(s) - propionitrile , diisopropyl ether , chemistry , substrate (aquarium) , lipase , yield (engineering) , solvent , ether , organic chemistry , amide , solubility , reagent , enzyme , acetonitrile , oceanography , materials science , metallurgy , geology
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.