Abstract
Enzymatic coupling of aminopolyols and medium-chain length fatty acids was carried out via the reverse action of a fungal lipase. Model reactants and catalysts were glucamine (1-amino-1-deoxysorbitol=AmS), pelargonic (nonanoic) acid, and Lipozyme IM-20. These reactants were selected since aminosorbitol is both a precursor for deoxynojirimycin (dietetic inhibitor for glucosidase) and forN-methylglucamine (an antileishmanial drug when complexed with antimony), and pelargonic acid is known to generate biotin-vitamers in some bacteria. The reaction proceeded in the presence of dry or water-saturated apolar organic solvents such as hexane and carbon tetrachloride. Increased molar ratio of acyl donor to acyl acceptor allowed the esterification and the amidation reactions to proceed with no need of solvent addition. A broad specificity was found for Lypozyme reverse action in terms of both acyl acceptors and donors.
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