A New Enzymatic Reaction: Enzyme Catalyzed Ammonolysis of Carboxylic Esters

Zoete, M. C. De; Dalen, A. C. Kock‐Van; Rantwijk, Fred van; Sheldon, Roger A.

doi:10.3109/10242429409065240

Cited by 45 publications

(13 citation statements)

References 8 publications

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“…202 The background to this approach is that enantioselectivities in the kinetic resolution of mandelic acid via (trans)esterification are low. Aminolysis (or ammoniolysis) may improve the resolution, as has been shown in some cases, 203,204 presumably due to a shift of the rate-determining step. CaLB resolved 19 in conventional media with quite modest E ratios, 4 ] was added to the medium.…”

Section: Lipases and Esterasesmentioning

confidence: 92%

Biocatalysis in Ionic Liquids

2007

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Fred van Rantwijk (1943) studied organic chemistry at the Delft University of Technology, where he remained as a staff member. He received his Ph.D. in 1980, for work under the guidance of Professor H. van Bekkum. Since the late 1980s he has been working on the application of enzymes in organic synthesis. His particular research interests are the use of enzymes in nonnatural reactions and nonnatural media, enzyme immobilization, and transformations using multi-enzyme systems.Roger Sheldon (1942) received a Ph.D. in organic chemistry from the University of Leicester (U.K.) in 1967. This was followed by postdoctoral studies with Prof. Jay Kochi in the U.S. From 1969 to 1980 he was with Shell Research in Amsterdam, and from 1980 to 1990 he was R&D Director of DSM Andeno. In 1991 he moved to his present position as Professor of biocatalysis and organic chemistry at the Delft University of Technology (The Netherlands). His primary research interests are in the application of catalytic methodologiesshomogeneous, heterogeneous, and enzymaticsto organic synthesis, particularly in relation to fine chemicals production. He developed the concepts of E factors and atom utilization for assessing the environmental impact of chemical processes.

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Section: Lipases and Esterasesmentioning

confidence: 92%

Biocatalysis in Ionic Liquids

2007

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“…In nearly anhydrous medium (using NH 2 OH и HCl and triethyl amine, data not shown) no reaction was observed at all with any of the enzymes apart from a small amount of hydrolysis. The inability to acylate hydroxylamine in the absence of water is rather surprising because, e.g., C. antarctica lipase B (Novozym 435) is known to be active at very low water activity in ammoniolysis (De Zoete et al, 1993, 1994a, 1995 as well as in transesterification (Woudenberg-van Oosterom et al, 1996). The initial reaction rate, using C. antarctica lipase B and 0.5 M hydroxylamine, increased with the water concentration and peaked at 1.75 M water (data not shown).…”

Section: Hydroxylaminolysis Of Ethyl Octanoatementioning

confidence: 98%

“…For example, carbohydrates (Woudenberg, et al, 1996), alkyl amines (Quiros et al, 1993;Zaks and Klibanov, 1985), ammonia (De Zoete et al, 1993, 1994a, 1995a,b, 1996Garcia et al, 1993), and hydrogen peroxide (Björkling et al, 1990(Björkling et al, , 1992 have been successfully used as acyl acceptors.…”

Section: Introductionmentioning

confidence: 99%

Lipase and esterase-catalyzed acylation of hetero-substituted nitrogen nucleophiles in water and organic solvents

Hacking

Akkus

Rantwijk

et al. 2000

Biotechnol. Bioeng.

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“…In early studies, secondary amides were produced by reacting FA esters or TG with alkylamines (6,7). Work then progressed through the lipase-catalyzed ammoniolysis of FA esters with ammonia for the production of primary fatty amides (8)(9)(10)(11)(12)(13) to the direct amidation of FA with ammonia (14).…”

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confidence: 99%

Characterization of primary fatty amides produced by lipase‐catalyzed amidation of hydroxylated fatty acids

Levinson

Kuo

Weisleder

2005

J Americ Oil Chem Soc

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A novel hydroxylated primary fatty amide was produced from lesquerolic acid by direct amidation with ammonia catalyzed by immobilized Pseudozyma (Candida) antarctica lipase B (Novozym 435) in organic solvent. The amides of ricinoleic acid and oleic acid were also produced for comparison. The hydroxy FA were transformed at comparable rates to that of oleic acid. The rate of amide formation was greater for the longerchain lesquerolic acid than for ricinoleic acid. All products exhibited characteristic primary-amide mass spectrum peaks with a base peak at m/z 59 and a strong ion fragment at m/z 72. Other peaks present are consistent with cleavage on either side of the hydroxyl position. The mass spectra, together with 1 H and 13 C NMR data, suggest that the products of lipase-catalyzed direct amidation of ricinoleic acid and lesquerolic acid are 12-hydroxy-9(Z)-octadecenamide and 14-hydroxy-11(Z)-eicosenamide, respectively.Paper no. J11020 in JAOCS 82, 501-504 (July 2005).

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A New Enzymatic Reaction: Enzyme Catalyzed Ammonolysis of Carboxylic Esters

Cited by 45 publications

References 8 publications

Biocatalysis in Ionic Liquids

Biocatalysis in Ionic Liquids

Lipase and esterase-catalyzed acylation of hetero-substituted nitrogen nucleophiles in water and organic solvents

Characterization of primary fatty amides produced by lipase‐catalyzed amidation of hydroxylated fatty acids

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