Studies on the Chemo- and Enantio-selectivity of the Enzymatic Monoacylations of Amino Alcohols.

Kanerva, Liisa T.; Kosonen, Markus; Vänttinen, Eero; Huuhtanen, Tuomas T.; Dahlqvist, Martti; Kady, M. M.; Christensen, S. Brøgger

doi:10.3891/acta.chem.scand.46-1101

Cited by 32 publications

(17 citation statements)

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“…It was found that most lipases catalyze both the amidation and the esterification of alkanolamines, however, in either case the predominant final product is the amide, formed not only via amidation but also via esterification and subsequent acyl migration from the alcohol to the amine, the thermodynamically more favored position (Fodor and Kiss, 1950). Acyl migration was observed to be faster in the shorter chain alkanolamines (C3) than the longer (C6) ones (Kanerva et al, 1992). Acyl migration was not studied in the case of ethanolamine as the rearrangement was thought to be too fast to be monitored.…”

Section: Introductionmentioning

confidence: 97%

“…Applied to our system, the alkanolamide would be formed predominantly via lipasecatalyzed esterification followed by spontaneous acyl migration (Scheme 1). Since the acyl migration step is too fast to be monitored (Kanerva et al, 1992), the reaction appears to proceed via direct amidation. Lipozyme 1 TL IM showed almost no catalytic activity for either reaction, while Lipozyme 1 RM IM showed moderate activity in the esterification reaction, but not for the amidation.…”

Section: Rate Of Amidation Versus Esterificationmentioning

confidence: 99%

“…An important issue in early investigations was chemo-selectivity, since alkanolamines are susceptible for acylation both at the amine and alcoholic group (Furutani et al, 1996;Kanerva et al, 1992). It was found that most lipases catalyze both the amidation and the esterification of alkanolamines, however, in either case the predominant final product is the amide, formed not only via amidation but also via esterification and subsequent acyl migration from the alcohol to the amine, the thermodynamically more favored position (Fodor and Kiss, 1950).…”

Section: Introductionmentioning

confidence: 99%

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Solvent‐free enzymatic synthesis of fatty alkanolamides

Tufvesson

Annerling

Hatti‐Kaul

et al. 2006

Biotech & Bioengineering

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An environmentally benign and volume efficient process for enzymatic production of alkanolamides is described. Immobilized Candida antarctica lipase B, Novozym435, was used to catalyze the condensation of lauric acid with monoethanolamine. The reaction temperature of 90 degrees C was required to keep the reactants in a liquid state. Stepwise addition of the amine minimized problems caused by the formation of a highly viscous amine/fatty acid ion-pair. The enzyme was both very active and stable under the reaction conditions, with about half of the activity remaining after 2 weeks. The maximum amide yield obtained when using equimolar amounts of the reactants was 75%, which could be increased to 95% upon water removal. Special precautions to avoid co-distillation of the amine were required. Two different strategies to avoid the amine loss are presented.

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Section: Introductionmentioning

confidence: 97%

Section: Rate Of Amidation Versus Esterificationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Solvent‐free enzymatic synthesis of fatty alkanolamides

Tufvesson

Annerling

Hatti‐Kaul

et al. 2006

Biotech & Bioengineering

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“…Alkanolamines are susceptible to acylation both at the amine and hydroxyl group [47,48]. However, the main product during a lipase-catalysed reaction is the amide, owing to spontaneous acyl migration from alcohol to the amine, the thermodynamically more favourable position (Figure 8.4).…”

Section: Alkanolamidesmentioning

confidence: 99%

Synthesis of Surfactants Using Enzymes

Adlercreutz

Hatti‐Kaul

2010

Surfactants From Renewable Resources

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“…The lipase-catalysed O-acylation of w-amino alcohols [HO(CH 2 ) n NH 2 ] was previously well recognised although fast spontaneous O3N acyl migration was shown to lead to the formation of the N-acylated final product with n 2 and 3. [16,17] On this basis, preferred O-acylation can also be suggested for the enantioselective acylation of 2-amino-1-butanol by PPL although only the formation of the N-monoacylated and N,O-diacylated products were reported. [18] It is common to the above-mentioned O3N acyl migrations that the amino group situates at the position b or g to the formed ester function.…”

Section: Introductionmentioning

confidence: 99%

Chemo‐ and Enantioselective Acyl Transfers by Lipases and Acylase I: Preparative Applications in Hydroxymethylpiperidine Chemistry

Lundell¹,

Lehtinen²,

Kanerva³

2003

Adv Synth Catal

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The lipase-and acylase I-catalysed acylation of bifunctional 2-and 3-hydroxymethylpiperidines (1 and 2) and the alcoholysis of the corresponding diacylated counterparts 7 and 8 have been studied. Lipase AK from Pseudomonas fluorescens allowed the preparative-scale resolution of 7 in neat butanol at 50% conversion whereas the 3-regioisomer 8 reacted with negligible enantioselectivity (E 7). The lipase-and acylase I-catalysed acylations of 1 and 2 in organic solvents proceeded with low enantioselectivity. On the other hand, more than 90% of 1 and 2 were transformed to amino esters 3 and 4, respectively, in a highly chemoselective Oacylation with 2,2,2-trifluoroethyl butanoate in the presence of Candida antarctica lipase A in TBME. The O-protected product 3 in the reaction mixture was readily available to another transformation at the piperidine nitrogen although 3 was not separated due to intramolecular O3N acyl migration. The tendency for acyl migration was much less significant in the case of 4.

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Studies on the Chemo- and Enantio-selectivity of the Enzymatic Monoacylations of Amino Alcohols.

Cited by 32 publications

References 0 publications

Solvent‐free enzymatic synthesis of fatty alkanolamides

Solvent‐free enzymatic synthesis of fatty alkanolamides

Synthesis of Surfactants Using Enzymes

Chemo‐ and Enantioselective Acyl Transfers by Lipases and Acylase I: Preparative Applications in Hydroxymethylpiperidine Chemistry

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