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

Zhang, Yuanyuan; Liu, Junhong

doi:10.1016/j.bej.2011.01.005

Cited by 27 publications

(12 citation statements)

References 22 publications

(27 reference statements)

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“…Some lipases, such as lipase B from Candida antarctica, lipase from Trichosporon laibacchii and lipase from Candida rugosa, can catalyze the hydrolysis or transesterification of racemic ketoprofen to obtain an optically pure compound (Ong et al, 2006;Kim et al, 2000;Zhang and Liu, 2011). However, these lipases typically have low stability, and are difficult to separate and reuse, thus limiting their wider application.…”

Section: Introductionmentioning

confidence: 98%

Immobilization of Aspergillus terreus lipase in self-assembled hollow nanospheres for enantioselective hydrolysis of ketoprofen vinyl ester

Wang

Zhang

et al. 2015

Journal of Biotechnology

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Section: Introductionmentioning

confidence: 98%

Immobilization of Aspergillus terreus lipase in self-assembled hollow nanospheres for enantioselective hydrolysis of ketoprofen vinyl ester

Wang

Zhang

et al. 2015

Journal of Biotechnology

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“…7 Until now, the dominant chiral preparation technology in industry has remained enantiomeric separation. A series of methods for enantiomeric separation, such as crystallization, 8,9 chromatography, 10,11 membrane separation, 1,12 enantioselective liquid-liquid extraction (ELLE), [13][14][15] and enzymatic kinetic resolution, [16][17][18][19][20][21][22][23][24][25][26] have been developed. Crystallization is still the most frequently applied technology for the manufacture of active pharmaceutical ingredients (APIs).…”

Section: Introductionmentioning

confidence: 99%

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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“…Due to the excellent regio-, stereo-, and chemoselectivity, an increasing number of lipases have been expressed, purified, and used as biocatalysts to synthesize lots of chiral compounds [9,10]. For instance, naproxen, ibuprofen, suprofen, ketoprofen, propranolol, and their intermediates were produced through lipase-catalyzed reactions [11][12][13][14][15]. In our previous research, a lipase-producing strain Tsukamurella tyrosinosolvents E105 has been screened to catalyze the resolution of racemic ethyl 2-(2-oxopyrrolidin-1-yl) butyrate to (S)-2-(2-oxopyrrolidin-1-yl) butyric acid with over 99 % of ee, which is the key chiral intermediate of LEV [16].…”

Section: Introductionmentioning

confidence: 99%

Purification and Immobilization of a Novel Enantioselective Lipase from Tsukamurella tyrosinosolvents for Efficient Resolution of Ethyl 2-(2-oxopyrrolidin-1-yl) Butyrate

Huang

Ren

et al. 2016

Appl Biochem Biotechnol

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A highly enantioselective lipase from Tsukamurella tyrosinosolvents E105 was purified via ultrasonic extraction, precipitation, and chromatographic steps. The enzyme was purified about 38-fold with the recovery yield of 9 % and was confirmed as a dimer protein consisting of two identical subunits with a molecular mass of 24 kDa. The purified lipase was used to catalyze resolution of racemic ethyl 2-(2-oxopyrrolidin-1-yl) butyrate to (S)-2-(2-oxopyrrolidin-1-yl) butyric acid. The maximum activity of such lipase was obtained at pH 7.5, 35 °C, and the highest relative activity (156.80 %) was observed in the presence of 0.5 mM Co. Subsequently, the lipase was encapsulated within a mixture of 3 % sodium alginate and 0.8 % carrageenan, and then cross-linked with 0.6 % glutaraldehyde to enhance its biocatalytic capability and stability. Comparing with 36.9 % product yield and 97.5 % product ee of free lipase, the highest product yield of 46.3 % and ee of 98.5 % for immobilized lipase were achieved with the presence of 20 mM substrate. In addition, the reusability of immobilized lipase was also investigated, which could maintain 63.7 % of its initial conversion yield after seven repeated batch reactions. Thus, the evaluated enantioselective lipase in this work has a good potential for further industrial application.

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

Cited by 27 publications

References 22 publications

Immobilization of Aspergillus terreus lipase in self-assembled hollow nanospheres for enantioselective hydrolysis of ketoprofen vinyl ester

Immobilization of Aspergillus terreus lipase in self-assembled hollow nanospheres for enantioselective hydrolysis of ketoprofen vinyl ester

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

Purification and Immobilization of a Novel Enantioselective Lipase from Tsukamurella tyrosinosolvents for Efficient Resolution of Ethyl 2-(2-oxopyrrolidin-1-yl) Butyrate

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