Recent advances in the use of enzyme-catalysed reactions in organic synthesis

Turner, Nicholas J.

doi:10.1039/np9890600625

Cited by 35 publications

(3 citation statements)

References 138 publications

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“…The stereospecificity of the enzymic reduction may depend on growth conditions, which would be in keeping with the observation that carbon source can influence the enzymes produced by a microorganism and this can in turn lead to a difference in the stereochemical course of the reduction (8). The identification of a stereoselective reductase enzyme in A. longipes cultures is also of potential economic importance since there is growing interest in the utilization of enzymes in the production of chiral molecules for the pharmaceutical and agrochemical industries (9). Bruker AC-400 spectrometer, using CDC13 as solvent with TMS as internal standard.…”

mentioning

confidence: 60%

Stereoselective Reduction of Radicinin by Liquid Cultures of Alternaria longipes

Sheridan¹,

Smyth²,

Canning³

et al. 1992

J. Nat. Prod.

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mentioning

confidence: 60%

Stereoselective Reduction of Radicinin by Liquid Cultures of Alternaria longipes

Sheridan¹,

Smyth²,

Canning³

et al. 1992

J. Nat. Prod.

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“…Enzymes play a crucial role in chemical transformations important to the pharmaceutical, chemical, agriculture and food processing industries because of their ability to produce chirally pure and complex molecules with interesting chemical and biological properties. They offer a number of advantages over conventional chemical catalysts [1,2].…”

Section: Ldh (Lactate Dehydrogenase)mentioning

confidence: 99%

Protein engineering applications of industrially exploitable enzymes: Geobacillus stearothermophilus LDH and Candida methylica FDH

Karagüler

Sessions

Bi̇nay

et al. 2007

Biochemical Society Transactions

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Enzymes have become important tools in several industries due to their ability to produce chirally pure and complex molecules with interesting biological properties. The NAD(+)-dependent LDH (lactate dehydrogenase) [bsLDH [Geobacillus stearothermophilus (formerly Bacillus stearothermophilus) LDH] from G. stearothermophilus and the NAD(+)-dependent FDH (formate dehydrogenase) [cmFDH (Candida methylica FDH)] enzyme from C. methylica are particularly crucial enzymes in the pharmaceutical industry and are related to each other in terms of NADH use and regeneration. LDH catalyses the interconversion of pyruvate (oxo acid) and lactate (alpha-hydroxy acid) using the NADH/NAD(+) pair as a redox cofactor. Employing LDH to reduce other oxo acids can generate chirally pure alpha-hydroxy acids of use in the production of pharmaceuticals. One important use of FDH is to regenerate the relatively expensive NADH cofactor that is used by NAD(+)-dependent oxidoreductases such as LDH. Both LDH and FDH from organisms of interest were previously cloned and overproduced. Therefore they are available at a low cost. However, both of these enzymes show disadvantages in the large-scale production of chirally pure compounds. We have applied two routes of protein engineering studies to improve the properties of these two enzymes, namely DNA shuffling and site-directed mutagenesis. Altering the substrate specificity of bsLDH by DNA shuffling and changing the coenzyme specificity of cmFDH by site-directed mutagenesis are the most successful examples of our studies. The present paper will also include the details of these examples together with some other applications of protein engineering regarding these enzymes.

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“…As a further benefit the products are no racemic mixtures but usually only one stereoisomer. These are the main advantages of using enzymes in new industrial flavor manufacture processes [2][3][4].…”

Section: Introductionmentioning

confidence: 99%

Synthesis of alkyl esters by cutinase in miniemulsion and organic solvent media

Barros

Fonseca

Cabral

et al. 2009

Biotechnology Journal

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High conversion yields of 95 % at equilibrium after 8h of reaction in iso-octane for pentanoic acid (C 5 ) with ethanol at equimolar concentration (0.1M) was achieved.Additionally, this work also shows that a significant and unexpected change in cutinase selectivity occurred for longer chain length carboxylic acids (C 8 -C 10 ) in miniemulsion system comparing with organic solvent (iso-octane) and previous studies in reverse micellar systems where a selectivity towards short chain fatty acids ( C 4 -C 6 ) was observed. The possibility to work with higher concentration of substrates ,without inhibitiory effect on enzyme, was another advantage of miniemulsion system.

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Recent advances in the use of enzyme-catalysed reactions in organic synthesis

Cited by 35 publications

References 138 publications

Stereoselective Reduction of Radicinin by Liquid Cultures of Alternaria longipes

Stereoselective Reduction of Radicinin by Liquid Cultures of Alternaria longipes

Protein engineering applications of industrially exploitable enzymes: Geobacillus stearothermophilus LDH and Candida methylica FDH

Synthesis of alkyl esters by cutinase in miniemulsion and organic solvent media

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