A novel lipase enzyme panel exhibiting superior activity and selectivity over lipase B from Candida antarctica for the kinetic resolution of secondary alcohols

O’Neill, Maeve; Beecher, Denis; Mangan, David; Rowan, Andrew S.; Monte, Agnieszka; Sroka, Stefan; Modregger, Jan; Hundle, Bhupinder S.; Moody, Thomas S.

doi:10.1016/j.tetasy.2012.03.013

Cited by 10 publications

(2 citation statements)

References 18 publications

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“…To avoid a series of complex purification steps and inclusion body formation in E. coli, and to facilitate subsequent enzyme immobilization, Pichia pastoris with the potent alcohol oxidase (AOX) promoter was used for expression. Moreover, P. pastoris can be applied in food and pharmaceutical industries [3,8]. Protein engineering is an effective way to design and reconstruct an enzyme.…”

Section: Introductionmentioning

confidence: 99%

Facile One-Pot Immobilization of a Novel Thermostable Carboxylesterase from Geobacillus uzenensis for Continuous Pesticide Degradation in a Packed-Bed Column Reactor

et al. 2020

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The novel carboxylesterase gene (est741) was cloned from Geobacillus uzenensis. The optimal pH and temperature of Est741 were 8.0 and 50 °C. Through site-directed mutation, the optimum temperature of the mutant M160K(EstM160K) was increased from 50 to 60 °C, and showed enhanced T1/2 of 2.5 h at 70 °C in comparison to the wild type (1.3 h). EstM160K was successfully expressed Pichia pastoris and EstM160K fermentation broth was directly immobilized on epoxy-functionalized supports via a one-pot strategy to obtain the immobilized enzyme lx-EstM160K. Additionally, lx-EstM160K showed enhanced T1/2 of 36.8 h at 70 °C in comparison to free enzyme. lx-EstM160K could degrade various pyrethroid pesticides. After 40 min reaction with 50 U of the lx-EstM160K, the malathion removal was 95.8% with a malathion concentration of 20 mg/L. When 2.5 g lx-EstM160K was added to the 10 mL column reactor with the concentration of bifenthrin was 500 mg/L and the transfer rate of the pump was 0.7 mL/min, the degradation rate of lx-EstM160K to bifenthrin was 90.4%. lx-EstM160K exhibited high operational stability and maintained 72% initial activity after ten batches of continuous reaction for bifenthrin pesticide biodegradation.

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Section: Introductionmentioning

confidence: 99%

Facile One-Pot Immobilization of a Novel Thermostable Carboxylesterase from Geobacillus uzenensis for Continuous Pesticide Degradation in a Packed-Bed Column Reactor

et al. 2020

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“…[32][33][34] Representative examples of lipases used for acyl transfer are lipase from P. cepacia (Amano PS), lipase-B from Candida antarctica (CAL-B), Candida rugosa (CRL), and P. fluorescens (PFL). 32,33 While secondary alcohols undergo acylation with better selectivity, [37][38][39][40][41][42][43][44][45][46][47] primary -OHs are generally less discriminated by lipases unless in the vicinity of sterically demanding groups. [48][49][50][51][52][53][54][55][56][57][58][59] Several strategies have been attempted to overcome this, such as the use of chiral or sterically demanding acyl donors, 56,60 optimization of solvation conditions, 61 or through sequential resolutions.…”

Section: Introductionmentioning

confidence: 99%

1‐Hydroxymethyl‐7‐oxabicyclo[2.2.1]hept‐2‐ene skeleton in enantiopure form through enzymatic kinetic resolution

Reddy

Manheri

2019

Chirality

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Lipase-catalysed enantioselective acetylation and deacetylation routes were investigated to prepare 1,5,6-trisubstituted 7-oxabicyclo[2.2.1]hept-2-ene skeleton in enantio-pure form. The racemic alcohol (6) used in acetylation reaction was accessed through Diels-Alder reaction of TBDMS-protected furfuryl alcohol with maleic anhydride, followed by reduction-benzylation-desilylation sequence. After systematic screening of lipases and solvents, Candida antarctica B on acrylic resin in pentane was identified as the best system that gave >98% ee towards the (+) acetate with 40% conversion, in 30 minutes. Absolute stereochemistry of this product was confirmed by X-ray diffraction analysis of its 3,5-dinitrobenzoate derivative (9). Enantioselective deacetylation of the racemic acetate of this starting material was then studied with the same set of lipases. After various optimization studies, Candida antarctica B in toluene as the solvent was found to be the most effective that gave 49% conversion with >99% ee towards the (+)-alcohol (8) at the end of 18 hours.

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Application of Enzymes in Kinetic Resolutions, Dynamic Kinetic Resolutions and Deracemization Reactions

Humphrey¹,

Ahmed

Ghanem

et al. 2014

Separation of Enantiomers

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A novel lipase enzyme panel exhibiting superior activity and selectivity over lipase B from Candida antarctica for the kinetic resolution of secondary alcohols

Cited by 10 publications

References 18 publications

Facile One-Pot Immobilization of a Novel Thermostable Carboxylesterase from Geobacillus uzenensis for Continuous Pesticide Degradation in a Packed-Bed Column Reactor

Facile One-Pot Immobilization of a Novel Thermostable Carboxylesterase from Geobacillus uzenensis for Continuous Pesticide Degradation in a Packed-Bed Column Reactor

1‐Hydroxymethyl‐7‐oxabicyclo[2.2.1]hept‐2‐ene skeleton in enantiopure form through enzymatic kinetic resolution

Application of Enzymes in Kinetic Resolutions, Dynamic Kinetic Resolutions and Deracemization Reactions

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