Lipase-catalyzed hydrolytic resolution of (R,S)-3-hydroxy-3-phenylpropionates in biphasic media

Cho, Shu-Hhin; Wang, Pei-Yun; Tsai, Shau‐Wei

doi:10.1016/j.jtice.2010.09.005

Cited by 16 publications

(8 citation statements)

References 21 publications

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“…In the lipase‐catalytic process, the catalytic triad forms a tetrahedral transition state with the substrate through hydrogen bonds and this is the key step for the catalytic process, determining the rate and selectivity of the reaction. Extreme pH can disrupt enzyme tertiary structure and the hydrogen bonds may be broken, which results in catalytic activity loss . It is reported that the optimal pH for CRL is about 7.0 and the optimal pH of 6.60 identified in this paper is consistent with the previous work.…”

Section: Resultssupporting

confidence: 90%

“…Extreme pH can disrupt enzyme tertiary structure and the hydrogen bonds may be broken, which results in catalytic activity loss. 44,46 It is reported that the optimal pH for CRL is about 7.0 47,48 and the optimal pH of 6.60 identified in this paper is consistent with the previous work. Based on the above results, 39 ∘ C and pH 6.60 were selected as the optimum temperature and pH.…”

Section: Effect Of Temperature and Phsupporting

confidence: 92%

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Lipase‐catalyzed hydrolysis of (+,‐)‐2‐(4‐methylphenyl) propionic methyl ester enhanced by hydroxypropyl‐β‐cyclodextrin

Liu

Zhang

et al. 2018

J of Chemical Tech & Biotech

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BACKGROUND Enzymatic kinetic resolution is an attractive technology for production of enantiomerically pure compounds. The objective of this research is to investigate the enantioselective hydrolysis of (+,‐)‐2‐(4‐methylphenyl) propionic methyl ester (2‐(4‐MP)PPAME) to (+)‐2‐(4‐methylphenyl) propionic acid ((+)‐2‐(4‐MP)PPA) catalyzed by enzyme in an aqueous medium. RESULTS Lipase AY from candida rugosa (CRL) was screened as the best lipase. Novozym 435 IM and lipopan S BG show higher catalytic activity but the enantioselectivity is very low. By addition of hydroxypropyl‐β‐cyclodextrin (HP‐β‐CD) to the aqueous system, an increased substrate conversion of 45.28% was obtained, the high enantiomeric excess remaining compared with the conversion of 28.05% without HP‐β‐CD. Response surface methodology and central composite design were employed to model and optimize the reaction system. CONCLUSION Under the optimal conditions including pH of 6.60, 12.5 mg mL−1 enzyme, 35 mmol L−1 HP‐β‐CD, 0.06 mmol substrate, temperature 39°C, agitation speed 400 rpm and 40 h reaction time, the substrate conversion was up to 40.32% and the optical purity of the product (+)‐2‐(4‐methylphenyl) propionic acid was up to 95.22%. © 2018 Society of Chemical Industry

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Section: Resultssupporting

confidence: 90%

Section: Effect Of Temperature and Phsupporting

confidence: 92%

Lipase‐catalyzed hydrolysis of (+,‐)‐2‐(4‐methylphenyl) propionic methyl ester enhanced by hydroxypropyl‐β‐cyclodextrin

Liu

Zhang

et al. 2018

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

show abstract

“…The catalytic triad forms a tetrahedral transition state with the substrate by hydrogen bonding, which is the key step in determining reaction rate and selectivity in the lipase‐catalyzed process. The decrease in the catalytic activity of the enzyme at higher pH values is due to the destruction of the tertiary structure of the enzyme and hydrogen bonding . The imidazole moiety of His plays an important role in the reaction and its configuration is affected by pH .…”

Section: Resultsmentioning

confidence: 99%

“…However, it is very common that the reaction has low conversion because of the poor solubility of substrates in the aqueous systems . Various strategies have been offered to solve the problem, including modification of enzyme, protein engineering and medium engineering. These strategies require lots of experiences and experiments.…”

Section: Introductionmentioning

confidence: 99%

Simulation and optimization of Novozym 40086 kinetic resolution of α‐cyclopentylphenylacetic acid enantiomers

Zhang

Cheng

et al. 2019

J of Chemical Tech & Biotech

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BACKGROUND: Enzymatic resolution of enantiomers by hydrolysis is a popular method, yet most enantiomers have low solubility in the aqueous phase, resulting in low conversion. Notwithstanding this, the simulation and optimization of the reaction process by modelling has been reported only rarely. Thus, PEG was added to the aqueous phase and a mathematical model was established to obtain optimal conditions. RESULTS: The effects of various parameters were investigated to build an optimized reaction system. The results indicated that temperature and pH had little effect on enantiomeric excess, but they had significant effect on conversion. Conversion was enhanced by 85% with the addition of PEG 400. Kinetic studies showed that pentanol competitively inhibited enzyme activity. A mathematical model was developed, and forward and reverse reactions were taken into consideration. Through simulation and optimization of model, the optimum conditions were obtained as follows: 10 mg mL −1 Novozym 40086, 10 mmol L −1 substrate, 30% PEG 400, temperature 45 ∘ C, pH 6.5 and reaction time 36 h. CONCLUSION: Chiral resolution of -cyclopentylphenylacetic acid enantiomer (CPPA) was achieved by Novozym 40086 enantioselective hydrolysis of the CPPA ester. Under optimum conditions, ee p and c s were 95.83% and 88.52%, respectively. The relative errors between predicted values and experimental values were <5%, confirming that the model could accurately predict the enzymatic resolution reaction.

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“…Lipase (E.C.3.1.1.3) is an enzyme that catalyzes both the hydrolysis of esters (Bora et al, 2011;Cho et al, 2011), and under certain conditions the synthesis of esters (Akanbi et al, 2015). Since the reaction is reversible, it can be used in many applications, such as food, chemicals, pharmaceuticals, biosensors, pesticides, leather, cosmetics, biodiesel, and detergents (Akanbi et al, 2015;Hasan et al, 2006;Berchmans and Hirata, 2008;Bisen et al, 2010;Zang et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Characterization of Aspergillus Niger 65i6 lipase from solid-state fermentation using Jatropha seed cake medium

et al. 2017

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Jatropha curcas seed cake contains a high amount of protein, and consequently has very high potential as a medium for lipase production. The objective of this research was to characterize lipase from Aspergillus niger 6516, which was produced by solid-state fermentation on Jatropha curcas seed cake as the medium. The effects of pH and temperature on enzyme activity were evaluated, along with substrate specificity and enzyme stability. Fermentation was performed at a water concentration of 63% and temperature of 30 °C for 7 days. The results showed that the optimum pH and temperature for Aspergillus niger 6516 lipase activities were 8.0 and 40 °C, respectively. The lipase had the substrate specificity to hydrolyze long-chain fatty acids and was stable in polar organic solvents. The lipase had a molecular weight, Km and v max about 19 kDa, 0.27 µmol/ml, and 52.63 µmol/ml/min, respectively. The results also suggested that the produced lipase from Aspergillus niger 6516 was an alkaline lipase. Based on these results, we conclude that Jatropha seed cake is a suitable medium for lipase production.

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Lipase-catalyzed hydrolytic resolution of (R,S)-3-hydroxy-3-phenylpropionates in biphasic media

Cited by 16 publications

References 21 publications

Lipase‐catalyzed hydrolysis of (+,‐)‐2‐(4‐methylphenyl) propionic methyl ester enhanced by hydroxypropyl‐β‐cyclodextrin

Lipase‐catalyzed hydrolysis of (+,‐)‐2‐(4‐methylphenyl) propionic methyl ester enhanced by hydroxypropyl‐β‐cyclodextrin

Simulation and optimization of Novozym 40086 kinetic resolution of α‐cyclopentylphenylacetic acid enantiomers

Characterization of Aspergillus Niger 65i6 lipase from solid-state fermentation using Jatropha seed cake medium

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