Kinetic modeling of lipase catalyzed hydrolysis of (R/S)-1-methoxy-2-propyl-acetate as a model reaction for production of chiral secondary alcohols

Berendsen, W.R.; Gendrot, G.; Resnick, Sol M.; Reuß, Michael

doi:10.1016/j.jbiotec.2005.07.006

Cited by 23 publications

(17 citation statements)

References 22 publications

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“…3 in which the line of K 4 is almost superposition with that of K 5 , and the corresponding parameters is shown in Table 2. The active energy reported in Table 2 is of the same magnitude as those found previously for other reactions catalyzed by lipase [11,24,25]. As shown in Fig.…”

Section: Kinetic Experiments and Modelingsupporting

confidence: 82%

Kinetic study of enantioselective hydrolysis of (R, S)-ketoprofen ethyl ester using immobilized T. laibacchii lipase

Zhang

Liu

2011

Biochemical Engineering Journal

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Section: Kinetic Experiments and Modelingsupporting

confidence: 82%

Kinetic study of enantioselective hydrolysis of (R, S)-ketoprofen ethyl ester using immobilized T. laibacchii lipase

Zhang

Liu

2011

Biochemical Engineering Journal

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“…Novel biotechnological applications have been successfully established using lipase for the synthesis of biopolymers and biodiesel, the production of enantiopure pharmaceuticals, agro-chemicals and fl avor compounds [1][2][3][4][5][6]. The advantages of enzymatic hydrolysis over a chemical process are less energy requirement and higher quality of obtained product.…”

Section: Introductionmentioning

confidence: 99%

Extracellular lipase of Aspergillus niger NRRL3; production, partial purification and properties

Adham

Ahmed

2009

Indian J Microbiol

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Four strains of Aspergillus niger were screened for lipase production. Each was cultivated on four different media differing in their contents of mineral components and sources of carbon and nitrogen. Aspergillus niger NRRL3 produced maximal activity (325U/ml) when grown in 3% peptone , 0.05% MgSO 4 .7H 2 O, 0.05% KCl, 0.2% K 2 HPO 4 and 1% olive oil:glucose (0.5:0.5). A. niger NRRL3 lipase was partially purifi ed by ammonium sulphate precipitation. The majority of lipase activity (48%) was located in fraction IV precipitated at 50-60% of saturation with a 18-fold enzyme purifi cation. The optimal pH of the partial purifi ed lipase preparation for the hydrolysis of emulsifi ed olive oil was 7.2 and the optimum temperature was 60°C. At 70°C, the enzyme retained more than 90% of its activity. Enzyme activity was inhibited by Hg 2+ and K + , whereas Ca 2+ and Mn 2+ greatly stimulated its activity. Additionally, the formed lipase was stored for one month without any loss in the activity.

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“…In order to identify the global minimum, more than one set of initial guesses of the kinetic constants were used to check if a better fit had not been overlooked. These initial guesses and constraints for the parameter values were selected based on prior experience with kinetic resolution reactions (Berendsen et al, 2006a(Berendsen et al, , 2006b.…”

Section: Model Identification and Parameter Estimationmentioning

confidence: 99%

“…Kinetic resolution may be achieved via hydrolysis, esterification, or transesterification mode (Baumann et al, 2000;Berendsen et al, 2006a;Rotticci, 2000). The reduced solubility of many potential compounds in aqueous solution and the concomitant change in pH during conversion are typical bottlenecks of the hydrolysis mode.…”

Section: Introductionmentioning

confidence: 99%

A kinetic study of lipase‐catalyzed reversible kinetic resolution involving verification at miniplant‐scale

Berendsen

Gendrot

Freund

et al. 2006

Biotech & Bioengineering

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Lipase-catalyzed kinetic resolution of racemates is a popular method for synthesis of chiral synthons. Most of these resolutions are reversible equilibrium limited reactions. For the first time, an extensive kinetic model is proposed for kinetic resolution reactions, which takes into account the full reversibility of the reaction, substrate inhibition by an acyl donor and an acyl acceptor as well as alternative substrate inhibition by each enantiomer. For this purpose, the reversible enantioselective transesterification of (R/S)-1-methoxy-2-propanol with ethyl acetate catalyzed by Candida antarctica lipase B (CAL-B) is investigated. The detailed model presented here is valid for a wide range of substrate and product concentrations. Following model discrimination and the application of Haldane equations to reduce the degree of freedom in parameter estimation, the 11 free parameters are successfully identified. All parameters are fitted to the complete data set simultaneously. Six types of independent initial rate studies provide a solid data basis for the model. The effect of changes in substrate and product concentration on reaction kinetics is discussed. The developed model is used for simulations to study the behavior of reaction kinetics in a fixed bed reactor. The typical plot of enantiomeric excess versus conversion of substrate and product is evaluated at various initial substrate mixtures. The model is validated by comparison with experimental results obtained with a fixed bed reactor, which is part of a fully automated state-of-the-art miniplant.

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Kinetic modeling of lipase catalyzed hydrolysis of (R/S)-1-methoxy-2-propyl-acetate as a model reaction for production of chiral secondary alcohols

Cited by 23 publications

References 22 publications

Kinetic study of enantioselective hydrolysis of (R, S)-ketoprofen ethyl ester using immobilized T. laibacchii lipase

Kinetic study of enantioselective hydrolysis of (R, S)-ketoprofen ethyl ester using immobilized T. laibacchii lipase

Extracellular lipase of Aspergillus niger NRRL3; production, partial purification and properties

A kinetic study of lipase‐catalyzed reversible kinetic resolution involving verification at miniplant‐scale

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