Kinetic resolution of 2-substituted esters catalyzed by a lipase ex. Pseudomonas fluorescens

Kalaritis, Panos; Regenye, R. W.; Partridge, John J.; Coffen, David L.

doi:10.1021/jo00290a007

Cited by 100 publications

(19 citation statements)

References 3 publications

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“…One way to probe the active site of a lipase is with chiral fatty acids, but few instances of stereoselection using acids bearing an asymmetric center have been reported thus far (ref. 2, and references therein}. We felt that a series of configurationally pure methyl branched fatty acids would prove useful for this purpose and, therefore, have synthesized a set of methylbranched octanoic acids {3,4}.…”

Section: Lipids 26 295-300 {1991)mentioning

confidence: 99%

Methyl‐branched octanoic acids as substrates for lipase‐catalyzed reactions

Sonnet

Baillargeon

1991

Lipids

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Hydrolyses of racemic methyl-branched octanoic acid thiolesters are described using six commercial lipases as catalysts. Branching at positions 2, 4 and 5 greatly reduced activity; branching at the 3-position virtually eliminated activity. The reactivities of the racemic branched thiolesters relative to the unbranched ester were very similar for each lipase preparation examined. In reactions involving configurationally pure 2-methyloctanoic acids, the S-enantiomer reacted faster both in esterification of aliphatic alcohols and in hydrolyses of aliphatic alcohol esters with all of the lipases examined. Stereobiases in hydrolyses of the octanoic acid esters branched at other positions were low and variable. In sharp contrast to the hydrolyses of the thiolesters of 2-methyloctanoic acid, two aryl esters of 2-methyloctanoic acid catalyzed by R. miehei lipase hydrolyzed with a bias for the R-configuration. A view of the ester-enzyme complex is offered to explain the relative rates of reaction of the racemic esters.

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Section: Lipids 26 295-300 {1991)mentioning

confidence: 99%

Methyl‐branched octanoic acids as substrates for lipase‐catalyzed reactions

Sonnet

Baillargeon

1991

Lipids

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“…In previous studies, enzymatic resolution and asymmetric reduction were used in the biological production of ( R )-HPBA. Compared with enzymatic resolution catalyzed by hydrolases, especially lipases [4] , [9] , [13] , asymmetric bio-reduction of 2-oxo-4-phenylbutyric acid (OPBA) by dehydrogenases is more desirable because of its excellent stereoselectivity and high theoretical yield up to 100% [1] , [14] . For practical production of ( R )-HPBA from OPBA through bio-reduction, highly efficient reductases and cofactor regeneration systems are needed.…”

Section: Introductionmentioning

confidence: 99%

Efficient Production of (R)-2-Hydroxy-4-Phenylbutyric Acid by Using a Coupled Reconstructed d-Lactate Dehydrogenase and Formate Dehydrogenase System

Sheng

Zheng

et al. 2014

PLoS ONE

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Background(R)-2-Hydroxy-4-phenylbutyric acid [(R)-HPBA] is a key precursor for the production of angiotensin-converting enzyme inhibitors. However, the product yield and concentration of reported (R)-HPBA synthetic processes remain unsatisfactory.Methodology/Principal FindingsThe Y52L/F299Y mutant of NAD-dependent d-lactate dehydrogenase (d-nLDH) in Lactobacillus bulgaricus ATCC 11842 was found to have high bio-reduction activity toward 2-oxo-4-phenylbutyric acid (OPBA). The mutant d-nLDHY52L/F299Y was then coexpressed with formate dehydrogenase in Escherichia coli BL21 (DE3) to construct a novel biocatalyst E. coli DF. Thus, a novel bio-reduction process utilizing whole cells of E. coli DF as the biocatalyst and formate as the co-substrate for cofactor regeneration was developed for the production of (R)-HPBA from OPBA. The biocatalysis conditions were then optimized.Conclusions/SignificanceUnder the optimum conditions, 73.4 mM OPBA was reduced to 71.8 mM (R)-HPBA in 90 min. Given its high product enantiomeric excess (>99%) and productivity (47.9 mM h−1), the constructed coupling biocatalysis system is a promising alternative for (R)-HPBA production.

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“…Nevertheless, the disadvantages of chemical nitrile hydrolysis come from drastic nitrile hydrolysis reaction conditions causing racemization, decomposition, or side reactions (8). The other efficient one appears to be the production of enantiomerically pure ethyl 2‐hydroxy‐4‐phenylbutyrate or 2‐hydroxy‐4‐phenylbutanoic acid via the kinetic resolution of corresponding racemic 2‐hydroxy esters using lipase (10). It was reported that the enantioselective hydrolysis ( R , S )‐ethyl 2‐hydroxy‐4‐phenylbutyrate was catalyzed by the lipase from Psedomonas cepacia in a two‐phase system consisting of aqueous buffer and organic solvent solubilizing the ester substrate, and its production was carried out in a diafiltration reactor (11).…”

Section: Introductionmentioning

confidence: 99%

“…The first process is the synthesis of enantiomerically pure cyanohydrins using ( R )‐ or ( S )‐specific hydroxynitrilases with subsequent chemical nitrile hydrolysis (7−9). The two‐step process efficiently produces this class of compounds owing to the broad substrate spectra of the hydroxynitrilases (8, 10). Nevertheless, the disadvantages of chemical nitrile hydrolysis come from drastic nitrile hydrolysis reaction conditions causing racemization, decomposition, or side reactions (8).…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Enantiopure ( S)-2-Hydroxyphenylbutanoic Acid Using Novel Hydroxy Acid Dehydrogenase from Enterobacter sp. BK2K

Kim

Yun

et al. 2008

Biotechnol Progress

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Enterobacter sp. BK2K, screened from soil samples, can enantioselectively reduce 2-oxo-4-phenylbutanoic acid into (S)-2-hydroxy-4-phenylbutanoic acid. alpha-Hydroxy acid dehydrogenase (HADH) (specific activity 62.6 U/mg) was purified from the crude extract of Enterobacter sp. BK2K, and its gene was cloned and functionally expressed in E. coli BL21. The optimal pH and temperature for the HADH activity were 6.5 and 30 degrees C, respectively. The purified enzyme catalyzes the reduction of various aromatic and aliphatic 2-oxo carboxylic acids to the corresponding (S)-2-hydoxy carboxylic acids using NADH as cofactor. For example, the Km and kcat/Km for 2-oxo-4-phenylbutaonoic acid in the presence of 2 mM NADH were 6.8 mM and 350 M-1 min-1, respectively. For practical applications, a NADH recycle system employing the recombinant formate dehydrogenase from E. coli K12 was coupled with HADH in E. coli BL21. Using the recombinant HADH (110 U of 11 U/mg crude cell extract) and formate dehydrogenase (670 U of 67 U/mg crude cell extract) in 10 mL of 500 mM phosphate buffer (pH 6.5), 96 mM of (S)-phenyllactic acid (> 94% ee) and 95 mM of (S)-2-hydroxy-4-phenylbutanoic acid (> 94% ee) were produced in quantitative yields from 100 mM of phenylpyruvate and 2-oxo-4-phenylbutanoic acid.

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Kinetic resolution of 2-substituted esters catalyzed by a lipase ex. Pseudomonas fluorescens

Cited by 100 publications

References 3 publications

Methyl‐branched octanoic acids as substrates for lipase‐catalyzed reactions

Methyl‐branched octanoic acids as substrates for lipase‐catalyzed reactions

Efficient Production of (R)-2-Hydroxy-4-Phenylbutyric Acid by Using a Coupled Reconstructed d-Lactate Dehydrogenase and Formate Dehydrogenase System

Synthesis of Enantiopure ( S)-2-Hydroxyphenylbutanoic Acid Using Novel Hydroxy Acid Dehydrogenase from Enterobacter sp. BK2K

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