A thermostable and organic-solvent tolerant esterase from Pseudomonas putida ECU1011: Catalytic properties and performance in kinetic resolution of α-hydroxy acids

Ma, Bao-Di; Yu, Hui‐Lei; Pan, Jiang; Liu, Jia-Yan; Ju, Xin; Xu, Jian‐He

doi:10.1016/j.biortech.2013.01.089

Cited by 48 publications

(25 citation statements)

References 32 publications

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“…Enzyme activity was assayed spectrophotometrically by measuring the conversion of 1 mM pNPB to p-nitrophenol in 100 mM PB (pH 7.0). One unit of enzyme activity was defined as the amount of enzyme releasing 1 mol of p-nitrophenol per min under the assay conditions (19). For the determination of substrate specificity, the following substrates were tested: p-nitrophenyl (pNP) acetate (C 2 acyl group), pNP propionate (C 3 acyl group), pNP butyrate (C 4 acyl group), pNP caproate (C 6 acyl group), pNP caprylate (C 8 acyl group), pNP-decanoate (C 10 acyl group), pNP-laurate (C 12 acyl group), and pNP-palmitate (C 16 acyl group).…”

Section: Methodsmentioning

confidence: 99%

Newly Identified Thermostable Esterase from Sulfobacillus acidophilus: Properties and Performance in Phthalate Ester Degradation

Zhang

Fan

Qiu

et al. 2014

Appl Environ Microbiol

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EstS1, a newly identified thermostable esterase from Sulfobacillus acidophilus DSM10332, was heterologously expressed in Escherichia coli and shown to enzymatically degrade phthalate esters (PAEs) to their corresponding monoalkyl PAEs. The optimal pH and temperature of the esterase were found to be 8.0 and 70°C, respectively. The half-life of EstS1 at 60°C was 15 h, indicating that the enzyme had good thermostability. The specificity constant (k cat /K m ) of the enzyme for p-nitrophenyl butyrate was as high as 6,770 mM ؊1 s ؊1 . The potential value of EstS1 was demonstrated by its ability to effectively hydrolyze 35 to 82% of PAEs (10 mM) within 2 min at 37°C, with all substrates being completely degraded within 24 h. At 60°C, the time required for complete hydrolysis of most PAEs was reduced by half. To our knowledge, this enzyme is a new esterase identified from thermophiles that is able to degrade various PAEs at high temperatures.

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Section: Methodsmentioning

confidence: 99%

Newly Identified Thermostable Esterase from Sulfobacillus acidophilus: Properties and Performance in Phthalate Ester Degradation

Zhang

Fan

Qiu

et al. 2014

Appl Environ Microbiol

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“…Previously, a number of methods have been applied to separate ClMA enantiomers by diastereomeric salt resolution, liquid–liquid extraction, and enantioselective enzymatic hydrolysis of the corresponding nitrile compounds . In addition, some studies had reported that excellent enzyme enantioselectivities could be obtained from esterase‐catalyzed hydrolysis of ( R,S )‐CIMA esters in aqueous or biphasic solutions . Methyl ( R )‐2‐chloromandelate was obtained by the reduction of methyl‐2‐chlorobenzoylformate using whole cells of Saccharomyces cerevisiae .…”

Section: Introductionmentioning

confidence: 99%

Experiment and simulation on kinetic resolution of (R,S)‐2‐chloromandelic acid by enzymatic transesterification

Yuan

Kang

Zhang

et al. 2019

Biotechnology Progress

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Optically pure 2‐chloromandelic acid (ClMA) is a very important chiral drug intermediate for synthesis of (S)‐clopidogrel, belonging to the platelet aggregation inhibitor. Enantioselective resolution of (R,S)‐2‐chloromandelic acid was carried out in organic solvent through irreversible transesterification catalyzed by lipase AK with vinyl acetate acting as the acyl donor. Effects of various conditions on enantioselectivity and activity of lipase were investigated, including organic solvents, temperature, water content, substrate ratio, enzyme loading, and reaction time. Based on homogeneous reaction and Ping‐Pong bi‐bi mechanism, a quantitative model was constructed to simulate and optimize the reaction process. Under the optimal conditions, excellent results were obtained with high conversion of (R)‐2‐ClMA (c R, ≥98.85%) and large enantiomeric excess of substrate (ee s, ≥98.15%). There is a good agreement between predicted values and experiment data, which indicates that the established method is a powerful tool for optimization of the enantioselective transesterification process for enantiomers separation.

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“…Many bacterial esterase genes have been cloned and expressed, such as from Pseudoalteromonas sp. 643A [4], Oenococcus oeni [12], P. arctica [13], Thermoanaerobacter tengcongensis [14], Pseudomonas putida [15] and Geobacillus thermodenitrificans T2 [16]. Several esterase genes have also been isolated and cloned from metagenomic libraries such as fermented compost [17], soil [18], and intertidal flat sediment [19].…”

Section: Introductionmentioning

confidence: 99%

Biochemical Characterization of a First Fungal Esterase from Rhizomucor miehei Showing High Efficiency of Ester Synthesis

Liu

Yan

et al. 2013

PLoS ONE

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BackgroundEsterases with excellent merits suitable for commercial use in ester production field are still insufficient. The aim of this research is to advance our understanding by seeking for more unusual esterases and revealing their characterizations for ester synthesis.Methodology/Principal FindingsA novel esterase-encoding gene from Rhizomucor miehei (RmEstA) was cloned and expressed in Escherichia coli. Sequence analysis revealed a 975-bp ORF encoding a 324-amino-acid polypeptide belonging to the hormone-sensitive lipase (HSL) family IV and showing highest similarity (44%) to the Paenibacillus mucilaginosus esterase/lipase. Recombinant RmEstA was purified to homogeneity: it was 34 kDa by SDS-PAGE and showed optimal pH and temperature of 6.5 and 45°C, respectively. The enzyme was stable to 50°C, under a broad pH range (5.0–10.6). RmEstA exhibited broad substrate specificity toward p-nitrophenol esters and short-acyl-chain triglycerols, with highest activities (1,480 U mg−1 and 228 U mg−1) for p-nitrophenyl hexanoate and tributyrin, respectively. RmEstA efficiently synthesized butyl butyrate (92% conversion yield) when immobilized on AOT-based organogel.ConclusionRmEstA has great potential for industrial applications. RmEstA is the first reported esterase from Rhizomucor miehei.

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A thermostable and organic-solvent tolerant esterase from Pseudomonas putida ECU1011: Catalytic properties and performance in kinetic resolution of α-hydroxy acids

Cited by 48 publications

References 32 publications

Newly Identified Thermostable Esterase from Sulfobacillus acidophilus: Properties and Performance in Phthalate Ester Degradation

Newly Identified Thermostable Esterase from Sulfobacillus acidophilus: Properties and Performance in Phthalate Ester Degradation

Experiment and simulation on kinetic resolution of (R,S)‐2‐chloromandelic acid by enzymatic transesterification

Biochemical Characterization of a First Fungal Esterase from Rhizomucor miehei Showing High Efficiency of Ester Synthesis

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