Facile conversion of racemic ibuprofen to (S)-ibuprofen

Chávez‐Flores, David; Salvador, James M.

doi:10.1016/j.tetasy.2012.02.014

Cited by 19 publications

(24 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, there is a drawback when an excess amount of DMSO is used, where the activity of lipase will significantly reduce during the course of the reaction. Such a result follows the work reported by Chavez‐Flores and co‐workers …”

Section: Resultssupporting

confidence: 92%

See 1 more Smart Citation

Effect of co‐solvent addition on the reaction kinetics of the lipase‐catalyzed resolution of ibuprofen ester

Gonawan¹,

Yon²,

Kamaruddin³

et al. 2012

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND: The addition of co‐solvent is not limited to enhancing the catalytic rate, it could also assist in situ racemization in the dynamic kinetic resolution of racemic compounds by increasing the reactivity of the base catalyst employed. In the current work, reaction media with the presence of DMSO were investigated in Candida rugosa lipase (EC 3.1.1.3)‐catalyzed hydrolysis of ibuprofen ester that focuses on the thermodynamic effect, reaction stability and implication for the kinetic parameters. RESULTS: The introduction of 2% DMSO increased the reaction rate, conversion, and enantioselectivity of the Candida rugosa lipase‐mediated resolution. However, the performance of the particular enzymatic reaction was reduced when a higher DMSO concentration was added. At lower reaction temperatures, the medium with 2% DMSO exhibited an increase in enantioselectivity, which was attributed to a higher activation energy difference between the fast‐ and slow‐reacting enantiomers compared with the water‐isooctane medium. Additionally, the presence of DMSO had a significant effect on the kinetic parameters, shown by a lower value of Michaelis constant compared with that of a normal reaction without DMSO, which resulted in a fast reaction rate. Finally, inhibition due to the uncompetitive substrate inhibitor was reduced, while the non‐competitive product inhibitor consequently increased. CONCLUSION: This work has demonstrated that only 2% of DMSO can be tolerated by the free Candida rugosa lipase in the resolution of ibuprofen ester. However, it is still able to give significant positive effects on the hydrolysis rate, kinetic parameters and enantioselectivity as well as reaction stability. © 2012 Society of Chemical Industry

show abstract

Section: Resultssupporting

confidence: 92%

“…Such a result follows the work reported by Chavez-Flores and co-workers. 20 Figure 2 shows the effect of substrate concentration against the conversion of ibuprofen ester. In the present investigation, two reaction media were studied, namely; water-isooctane (1 : 1) and water-isooctane (1 : 1) with 2% (v/v) DMSO.…”

Section: Resultsmentioning

confidence: 99%

Effect of co‐solvent addition on the reaction kinetics of the lipase‐catalyzed resolution of ibuprofen ester

Gonawan¹,

Yon²,

Kamaruddin³

et al. 2012

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

show abstract

“…Also, some hydrophilic esters are more soluble and biodisponible than the original drug [9]. Fischer esterification reactions are commonly catalyzed by acids, for example, for ibuprofen and ketoprofen [7,10].…”

Section: Introductionmentioning

confidence: 99%

Esterification of glycerol and ibuprofen in solventless media catalyzed by free CALB: Kinetic modelling

Ravelo

Fuente

Blanco

et al. 2015

Biochemical Engineering Journal

View full text Add to dashboard Cite

“…Recent examples are the CAL-B-catalyzed transesterification of oxazinones [67] and azlactones [68] using Et 3 N, the hydrolysis of ibuprofen methyl ester employing lipase from Candida rugosa (CRL) at basic pH, [69] and the CAL-B-mediated hydrolysis of methyl 2,3-dihydrobenzo[b]furan-3-carboxylate derivatives in the presence of a diazaphosphorine base. [70] Recently, another interesting approach was proposed by Wiggins and Bielawski, [71] who employed ultrasonication to racemize poly(methylacrylate) chains with binol as pendant groups (Scheme 7a).…”

Section: Using Lipases and Esterasesmentioning

confidence: 99%

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

Díaz‐Rodríguez¹,

Lavandera

Gotor³

2015

CGC

View full text Add to dashboard Cite

Abstract. In recent years the usefulness of enzymatic systems to obtain a single stereoisomerically pure compound starting from a racemate has been expanded. Moreover, current advances in protein engineering, molecular biology and modeling tools are the basis to improve the catalytic properties of enzymes to face novel synthetic challenges. Also, medium engineering and novel immobilization methods of (bio)catalysts are enhancing the productivity of biocatalytic processes making them suitable for being scalable. The development of multienzymatic protocols and the combination of enzymes with other catalysts are providing a wide range of synthetic possibilities that are expanding the scope of these transformations even at industrial scale. Herein we will describe an overview of recent (chemo)enzymatic deracemizations, focusing on the strategy employed (dynamic kinetic resolution, stereoinversion, cyclic deracemization or enantioconvergent process), the type of substrate (e.g., alcohols, amines, carboxylic acid derivatives or carbonylic compounds), and the biocatalyst(s) used.

show abstract

Facile conversion of racemic ibuprofen to (S)-ibuprofen

Cited by 19 publications

References 11 publications

Effect of co‐solvent addition on the reaction kinetics of the lipase‐catalyzed resolution of ibuprofen ester

Effect of co‐solvent addition on the reaction kinetics of the lipase‐catalyzed resolution of ibuprofen ester

Esterification of glycerol and ibuprofen in solventless media catalyzed by free CALB: Kinetic modelling

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

Contact Info

Product

Resources

About