Enzymatic regioselective production of chloramphenicol esters

Bizerra, Ayla Márcia Cordeiro; Montenegro, Tasso G. C.; Lemos, Telma L. G.; Oliveira, Maria C. F. de; Mattos, Marcos Carlos de; Lavandera, Iván; Gotor‐Fernández, Vicente; Gonzalo, Gonzalo de; Gotor, Vicente

doi:10.1016/j.tet.2011.02.070

Cited by 17 publications

(17 citation statements)

References 37 publications

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“…Among all biocatalytic processes, lipase reactions have many advantages owing to their high regioselectivity and mild incubation conditions, and maximize the efficiency of trivial processes in comparison to chemical methods [5][6][7]. Recently, it was reported that lipase can serve as a catalyst to regioselectively produce chloramphenicol derivatives.…”

Section: Introductionmentioning

confidence: 99%

“…Among chloramphenicol derivatives, chloramphenicol palmitate has been studied only in a few works. Bizerra et al obtained a yield of 98% using Candida antarctica lipase B at 0.25 M chloramphenicol, and Wang et al demonstrated that an imprinted lipase nanogel (Lipozyme TL 100L, Novozymes UK Ltd, Nottingham, UK) can have a yield of 99% within 12 h at 20 • C [5,9]. However, the lipases discussed above are commercially available enzymes.…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of a Novel ESTBAS Esterase from Bacillus altitudinis onto an Epoxy Resin: Characterization and Regioselective Synthesis of Chloramphenicol Palmitate

et al. 2019

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Novel gene estBAS from Bacillus altitudinis, encoding a 216-amino acid esterase (EstBAS) with a signal peptide (SP), was expressed in Escherichia coli. EstBASΔSP showed the highest activity toward p-nitrophenyl hexanoate at 50 °C and pH 8.0 and had a half-life (T1/2) of 6 h at 50 °C. EstBASΔSP was immobilized onto a novel epoxy resin (Lx-105s) with a high loading of 96 mg/g. Fourier transform infrared (FTIR) spectroscopy showed that EstBASΔSP was successfully immobilized onto Lx-105s. In addition, immobilization improved its enzymatic performance by widening the tolerable ranges of pH and temperature. The optimum temperature of immobilized EstBASΔSP (Lx-EstBASΔSP) was higher, 60 °C, and overall thermostability improved. T1/2 of Lx-EstBASΔSP and free EstBASΔSP at 60 °C was 105 and 28 min, respectively. Lx-EstBASΔSP was used as a biocatalyst to synthesize chloramphenicol palmitate by regioselective modification at the primary hydroxyl group. Conversion efficiency reached 94.7% at 0.15 M substrate concentration after 24 h. Lx-EstBASΔSP was stable and could be reused for seven cycles, after which it retained over 80% of the original activity.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Immobilization of a Novel ESTBAS Esterase from Bacillus altitudinis onto an Epoxy Resin: Characterization and Regioselective Synthesis of Chloramphenicol Palmitate

et al. 2019

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“…It is noteworthy that the study of the reuse of CAL-B in esterification with vinyl palmitate was performed. As a result, it was observed that after 3 h of reaction, there was complete conversion during 10 cycles of reuse of the enzyme [ 36 ]. The same strategy was used on the synthesis of Thiamphenicol esters from (1 R ,2 R )-(−)-Thiamphenicol, an antibiotic analogue of chloramphenicol with veterinary applications.…”

Section: Esterification Approachmentioning

confidence: 99%

Recent Advances in Lipase-Mediated Preparation of Pharmaceuticals and Their Intermediates

Carvalho

Fonseca

Mattos

et al. 2015

IJMS

123

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Biocatalysis offers an alternative approach to conventional chemical processes for the production of single-isomer chiral drugs. Lipases are one of the most used enzymes in the synthesis of enantiomerically pure intermediates. The use of this type of enzyme is mainly due to the characteristics of their regio-, chemo- and enantioselectivity in the resolution process of racemates, without the use of cofactors. Moreover, this class of enzymes has generally excellent stability in the presence of organic solvents, facilitating the solubility of the organic substrate to be modified. Further improvements and new applications have been achieved in the syntheses of biologically active compounds catalyzed by lipases. This review critically reports and discusses examples from recent literature (2007 to mid-2015), concerning the synthesis of enantiomerically pure active pharmaceutical ingredients (APIs) and their intermediates in which the key step involves the action of a lipase.

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“…Unfortunately, it can also produce liver and kidney function inhibition, grey baby syndrome, aplastic anemia and so on. Meanwhile the bitterness of chloramphenicol cannot be accepted by most people [ 6 ], so different chloramphenicol derivatives have been produced minimize this bitterness [ 1 ] such as chloramphenicol succinate or chloramphenicol palmitate esters produced by means of regio- or stereoselective chemical [ 7 ] and enzymatic methods [ 8 ]. Among all catalytic enzymes, lipases catalyze transesterification reactions on hydroxyl groups with high regioselectivity and mild reaction conditions [ 9 , 10 , 11 ].…”

Section: Introductionmentioning

confidence: 99%

Transesterification Synthesis of Chloramphenicol Esters with the Lipase from Bacillus amyloliquefaciens

Dong

Lin

et al. 2017

Molecules

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This work presents a synthetic route to produce chloramphenicol esters by taking advantage the high enantio- and regio-selectivity of lipases. A series of chloramphenicol esters were synthesized using chloramphenicol, acyl donors of different carbon chain length and lipase LipBA (lipase cloned from Bacillus amyloliquefaciens). Among acyl donors with different carbon chain lengths, vinyl propionate was found to be the best. The influences of different organic solvents, reaction temperature, reaction time, enzyme loading and water content on the synthesis of the chloramphenicol esters were studied. The synthesis of chloramphenicol propionate (0.25 M) with 4.0 g L−1 of LipBA loading gave a conversion of ~98% and a purity of ~99% within 8 h at 50 °C in 1,4-dioxane as solvent. The optimum mole ratio of vinyl propionate to chloramphenicol was increased to 5:1. This is the first report of B. amyloliquefaciens lipase being used in chloramphenicol ester synthesis and a detailed study of the synthesis of chloramphenicol propionate using this reaction. The high enzyme activity and selectivity make lipase LipBA an attractive catalyst for green chemical synthesis of molecules with complex structures.

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Enzymatic regioselective production of chloramphenicol esters

Cited by 17 publications

References 37 publications

Immobilization of a Novel ESTBAS Esterase from Bacillus altitudinis onto an Epoxy Resin: Characterization and Regioselective Synthesis of Chloramphenicol Palmitate

Immobilization of a Novel ESTBAS Esterase from Bacillus altitudinis onto an Epoxy Resin: Characterization and Regioselective Synthesis of Chloramphenicol Palmitate

Recent Advances in Lipase-Mediated Preparation of Pharmaceuticals and Their Intermediates

Transesterification Synthesis of Chloramphenicol Esters with the Lipase from Bacillus amyloliquefaciens

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