Immobilization to improve the properties of Pseudomonas fluorescens lipase for the kinetic resolution of 3-aryl-3-hydroxy esters

Brem, Jürgen; Turcu, Mihaela C.; Paizs, Csaba; Lundell, Katri; Toşa, Monica-Ioana; Irimie, Florin Dan; Kanerva, Liisa T.

doi:10.1016/j.procbio.2011.10.020

Cited by 23 publications

(22 citation statements)

References 39 publications

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“…In addition to natural polymers, synthetic polymers form a large and varied group of the enzyme carriers (Kumar and Kanwar 2011;Brem et al 2011). Effectively, any polymerization can be designed to prepare a polymer with the customized properties.…”

Section: Organic Carriersmentioning

confidence: 99%

“…Eupergit supports are copolymers, of which a main component is poly(methacryl amide), while Sepabeads are polystyrenic adsorbents. Commercially available are also Celite (Kumar and Kanwar 2011) and Celite 545 silica carriers (Brem et al 2011). Their main component is diatomaceous earth, which is the sedimentary rock formed as a result of diatoms exoskeletons deterioration.…”

Section: Commercial Productsmentioning

confidence: 99%

“…Lipases catalyse the hydrolysis of esters formed by short-and long-chain alcohols, mono-and multi-hydroxides, and saturated and unsaturated carboxylic acids of short and long chains. The catalysts based on lipases are used in the reactions of esterification or transesterification of different substrates (Brem et al 2011;Liu et al 2013;Yu and Fang 2013), and in the process of biodiesel production (Salis et al 2010;Mendes et al 2011;Tran et al 2012). A wide use of this group of proteins and their affinity to many carriers permit their immobilization on many organic and inorganic carriers.…”

Section: Immobilized Enzymesmentioning

confidence: 99%

“…By contrast, among inorganic carriers widely used there are different silicas, such as mesoporous silicas (Gustafsson et al 2012), e.g. SBA-15 or MSU-H (Yu and Fang 2013), vesicular silica (Wu et al 2012), fumed silica (Kramer et al 2010), silanized silica (Zheng et al 2012), silica sol-gel film (Lee et al 2010) and commercial silica-based products Celite (Brem et al 2011) and Celite 545 (Kumar and Kanwar 2011;see Fig. 5).…”

Section: Immobilized Enzymesmentioning

confidence: 99%

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Enzyme immobilization by adsorption: a review

2014

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Endowed with unparalleled high catalytic activity and selectivity, enzymes offer enormous potential as catalysts in practical applications. These applications, however, are seriously hampered by enzymes' low thermal and chemical stabilities. One way to improve these stabilities is the enzyme immobilization. Among various tested methods of this process that make use of different enzyme-carrier interactions, immobilization by adsorption on solid carriers has appeared most common. According to these findings, in this review we present a comparative analysis of the literature reports on the recent trends in the immobilization of the enzymes by adsorption. This thorough study was prepared in order to provide a deeper understanding of the process. Both carriers, carrier modifiers and procedures developed for effective adsorption of the enzymes are discussed. The review may thus be helpful in choosing the right adsorption scheme for a given enzyme to achieve the improvement of its stability and activity for a specific application.

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Section: Organic Carriersmentioning

confidence: 99%

Section: Commercial Productsmentioning

confidence: 99%

Section: Immobilized Enzymesmentioning

confidence: 99%

Section: Immobilized Enzymesmentioning

confidence: 99%

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Enzyme immobilization by adsorption: a review

2014

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“…Consequently, this biocatalyst might not be a suitable candidate for repeated use. Biocatalysts obtained through sol-gel entrapment, on the other hand, do not have this disadvantage and have proved in our previous work 27,35,38 and in other studies 11,15,39 remarkable recycling stability. …”

mentioning

confidence: 65%

Tailored sol–gel immobilized lipase preparates for the enzymatic kinetic resolution of heteroaromatic alcohols in batch and continuous flow systems

et al. 2017

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Tailored immobilized lipases from Candida antarctica B and Pseudomonas fluorescens, with improved thermal and operational stability, were prepared through fine tuning of the structure of the sol-gel matrix, using various binary or ternary precursor mixtures for the EKR of various chiral heteroaromatic secondary alcohols with benzofuran, benzo [b]thiophen, phenothiazine and 2-phenylthiazol moieties.The operational stability in batch process was studied for five selected systems by performing reuse experiments, using the conversion, enantiomeric excesses and enantiomeric ratio as parameters, demonstrating the dependence of the sol-gel lipase preparate performance on the structure of both biocatalyst and substrate. The resolution of the benzofuranic substrates with the best performing biocatalysts was studied in continuous-flow mode, using the productivity as a criterion. The specific reaction rates under continuous-flow operation (r flow ) were higher than those obtained in batch mode (r batch ) in both cases, sustaining its usefulness for further process development.

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Exploration of the expeditious potential of Pseudomonas fluorescens lipase in the kinetic resolution of racemic intermediates and its validation through molecular docking

et al. 2017

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A profoundly time-efficient chemoenzymatic method for the synthesis of (S)-3-(4-chlorophenoxy)propan-1,2-diol and (S)-1-chloro-3-(2,5-dichlorophenoxy)propan-2-ol, two important pharmaceutical intermediates, was successfully developed using Pseudomonas fluorescens lipase (PFL). Kinetic resolution was successfully achieved using vinyl acetate as acylating agent, toluene/hexane as solvent, and reaction temperature of 30°C giving high enantioselectivity and conversion. Under optimized condition, PFL demonstrated 50.2% conversion, enantiomeric excess of 95.0%, enantioselectivity (E = 153) in an optimum time of 1 hour and 50.3% conversion, enantiomeric excess of 95.2%, enantioselectivity (E = 161) in an optimum time of 3 hours, for the two racemic alcohols, respectively. Docking of the R-and S-enantiomers of the intermediates demonstrated stronger H-bond interaction between the hydroxyl group of the R-enantiomer and the key binding residues of the catalytic site of the lipase, while the S-enantiomer demonstrated lesser interaction. Thus, docking study complemented the experimental outcome that PFL preferentially acylated the R form of the intermediates. The present study demonstrates a cost-effective and expeditious biocatalytic process that can be applied in the enantiopure synthesis of pharmaceutical intermediates and drugs.

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Immobilization to improve the properties of Pseudomonas fluorescens lipase for the kinetic resolution of 3-aryl-3-hydroxy esters

Cited by 23 publications

References 39 publications

Enzyme immobilization by adsorption: a review

Enzyme immobilization by adsorption: a review

Tailored sol–gel immobilized lipase preparates for the enzymatic kinetic resolution of heteroaromatic alcohols in batch and continuous flow systems

Exploration of the expeditious potential of Pseudomonas fluorescens lipase in the kinetic resolution of racemic intermediates and its validation through molecular docking

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