The first hydroxynitrile lyase catalysed cyanohydrin formation in ionic liquids

Gaisberger, Richard; Fechter, Martin; Griengl, Herfried

doi:10.1016/j.tetasy.2004.06.028

Cited by 48 publications

(25 citation statements)

References 36 publications

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“…4 Another new option is the application of ionic liquids, which has successfully been used for (R)-PaHNL-and (S)-HbHNL catalyzed reactions, introduced by Griengl and co-workers in 2004. 31 It is also necessary to state the potential and application of CLEAs (cross-linked enzyme aggregates), which display an enhanced stability to organic solvents and can be easily reused. 32 These four HNLs are being used in preparative scales: (R)-PaHNL (from almonds), (S)-SbHNL (from Sorghum), (S)-MeHNL (Cassava) and (S)-HbHNL (rubber tree).…”

Section: Examples Of Chemicalsmentioning

confidence: 99%

Hydroxynitrile Lyases: Insights into Biochemistry, Discovery, and Engineering

2011

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Hydroxynitrile lyases are valuable enzymes for asymmetric synthesis of cyanohydrins. These hydroxyl and nitrileÀcontaining compounds are being used in production of very useful pharmaceuticals, agrochemicals, and other biologically active compounds using chemical or chemoenzymatic follow-up reactions in industry. Although a huge amount of information exists on the reaction parameters of these enzymes, including stability to pH and organic solvents, yield, reaction time, and valuable data on the enantiopurity of their products, cyanohydrins, there is a lack of update on the biochemistry, discovery, and engineering of the HNLs. Therefore, in the Introduction, we will have a look into these enzymes, cyanohydrins, and aldoxime-nitrile pathways. A brief view of functional groups and several examples of cyanohydrin-based chemicals and pharmaceuticals will also be described. Then we will present characteristics of many S-and R-selective HNLs with comparative tables for several enzymatic properties under biochemistry section. The methods of screening and discovery of these enzymes both from nature and a library of mutants will be described as well as their potential in the synthesis of chemicals. Cloning and expression of new HNLs will also be described under the discovery section. A pool of successful applications of protein engineering methods and the subsequent improvement in the properties of mutant HNLs will be reviewed in detail afterward.

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Section: Examples Of Chemicalsmentioning

confidence: 99%

Hydroxynitrile Lyases: Insights into Biochemistry, Discovery, and Engineering

2011

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“…The observed activities were similar to those achieved in traditional organic solvents, but the stability of the enzyme was markedly enhanced. Following this pioneering work, the potential application of lipase, [14][15][16][17] protease, 18,19 esterase, 20,21 amidase, 22 epoxide hydrolase, 23 peroxidase, 24 alcohol dehydrogenase, 25 or hydroxynitrile lyase 26,27 in IL-containing systems was explored, and many enzymes were demonstrated to be active in ILs, showing comparable or even higher activity, selectivity, and stability than in organic solvents. For example, the replacement of typical organic solvents by ILs in the lipase-catalyzed asymmetric acylation of amines with carboxylic acids has led to increased reaction rate and higher enantioselectivity.…”

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confidence: 99%

Efficient kinetic resolution of (R,S)‐1‐trimethylsilylethanol via lipase‐mediated enantioselective acylation in ionic liquids

Lou

Zong

2006

Chirality

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Efficient enantioselective acylation of (R,S)-1-trimethylsilylethanol {(R,S)-1-TMSE} with vinyl acetate catalyzed by immobilized lipase from Candida antarctica B (i.e., Novozym 435) was successfully conducted in ionic liquids (ILs). A remarkable enhancement in the initial rate and the enantioselectivity of the acylation was observed by using ILs as the reaction media when compared to the organic solvents tested. Also, the activity, enantioselectivity, and thermostability of Novozym 435 increased with increasing hydrophobicity of ILs. Of the six ILs examined, the IL C4MIm.PF6 gave the fastest initial rate and the highest enantioselectivity, and was consequently chosen as the favorable medium for the reaction. The optimal molar ratio of vinyl acetate to (R,S)-1-TMSE, water activity, and reaction temperature range were 4:1, 0.75, and 40 -50 degrees C, respectively, under which the initial rate and the enantioselectivity (E value) were 27.6 mM/h and 149, respectively. After a reaction time of 6 h, the ee of the remaining (S)-1-TMSE reached 97.1% at the substrate conversion of 50.7%. Additionally, Novozym 435 was effectively recycled and reused in C4MIm.PF6 for five consecutive runs without substantial lose in activity and enantioselectivity. The preparative scale kinetic resolution of (R,S)-1-TMSE in C4MIm.PF6 is shown to be very promising and useful for the industrial production of enantiopure (S)-1-TMSE.

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“…It is therefore not surprising that during the last years several examples have been described for the utilisation of ionic liquids as solvent systems for enzymecatalysed reactions and even an in-vitro application of the hydroxynitrile lyases from Prunus amygdalus and Hevea brasiliensis for the synthesis of (R)-or (S)-mandelonitrile has been described. [10,11] Nevertheless, there are still only very few examples for the utilisation of ionic liquids as solvent systems for whole-cell biotranformation reactions. Most of these studies described the (often asymmetric) reduction of ketones by different yeasts.…”

Section: Discussionmentioning

confidence: 99%

Application of a Recombinant Escherichia coli Whole‐Cell Catalyst Expressing Hydroxynitrile Lyase and Nitrilase Activities in Ionic Liquids for the Production of (S)‐Mandelic Acid and (S)‐Mandeloamide

Baum

Rantwijk

2012

Adv Synth Catal

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The conversion of benzaldehyde and cyanide into mandelic acid and mandeloamide by a recombinant Escherichia coli strain which simultaneously expressed an (S)-hydroxynitrile lyase (oxynitrilase) from cassava (Manihot esculenta) and an aryl-A C H T U N G T R E N N U N G acetonitrilase from Pseudomonas fluorescens EBC191 was studied. Benzaldehyde exhibited a pronounced inhibitory effect on the nitrilase activity in concentrations ! 25 mM. Therefore, it was tested if two-phase systems consisting of a buffered aqueous phase and the ionic liquid 1-butyl-1-pyrrolidinium bis(trifluoromethanesulfonyl)imide (BMpl NTf 2 ) or 1-butyl-3-methylimidazolium hexafluorophosphate (BMim PF 6 ) could be used for the intended biotransformation. The distribution coefficients of the substrates, intermediates and products of the reaction were determined and it was found that BMpl NTf 2 and BMim PF 6 were highly efficient as substrate reservoirs for benzaldehyde. The recombinant E. coli strain was active in the presence of BMpl NTf 2 or BMim PF 6 phases and converted benzaldehyde and cyanide into mandelic acid and mandeloamide. The two-phase systems allowed the conversion of benzaldehyde dissolved in the ionic liquids to a concentration of 700 mM with product yields (= sum of mandelic acid and mandeloamide) of 87-100%. The cells were slightly more effective in the presence of BMpl NTf 2 than in the presence of BMim PF 6 . In both two-phase systems benzaldehyde and cyanide were converted into (S)-mandeloamide and (S)-mandelic acid with enantiomeric excesses ! 94%. The recombinant E. coli cells formed, in the two-phase systems with ionic liquids and increased substrate concentrations, higher relative amounts of mandelo-A C H T U N G T R E N N U N G amide than in a purely aqueous system with lower substrate concentrations.

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The first hydroxynitrile lyase catalysed cyanohydrin formation in ionic liquids

Cited by 48 publications

References 36 publications

Hydroxynitrile Lyases: Insights into Biochemistry, Discovery, and Engineering

Hydroxynitrile Lyases: Insights into Biochemistry, Discovery, and Engineering

Efficient kinetic resolution of (R,S)‐1‐trimethylsilylethanol via lipase‐mediated enantioselective acylation in ionic liquids

Application of a Recombinant Escherichia coli Whole‐Cell Catalyst Expressing Hydroxynitrile Lyase and Nitrilase Activities in Ionic Liquids for the Production of (S)‐Mandelic Acid and (S)‐Mandeloamide

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