Immobilization of Lecitase® ultra on recyclable polymer support: application in resolution of trans-methyl (4-methoxyphenyl)glycidate in organic solvents

Kumaraguru, Thenkrishnan; Harini, Tirunagari; Basetty, Shalini

doi:10.1016/j.tetasy.2017.10.006

Cited by 11 publications

(13 citation statements)

References 41 publications

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“…On the other hand, dos Santos et al [ 29 ] showed that depending on the type of functional groups present on the surface of the carrier and the immobilization method, the pH optimum of the LU profiles ranges from 6.0 to 9.0 and the pH activity profile also varies. Lecitase® Ultra immobilized on epoxy-activated polymer DILBEAD-VWR modified by polyethyleneimine showed a shift of the pH optimum towards the alkaline reaction, probably due to the presence of amino groups on the carrier surface [ 30 ]. Wu et al [ 12 ] analyzed lipases other than Lecitase® Ultra (i.e., Candida rugosa -derived lipases) and immobilized these enzymes on BC disks.…”

Section: Resultsmentioning

confidence: 99%

“…The immobilization of LU to cellulose triacetate also increased the temperature stability of the enzyme, especially at 50 and 60 °C [ 36 ]. However, immobilization of Lecitase® Ultra on epoxy-activated polymer (DILBEAD-VWR) did not significantly affect the stability of the enzyme at high temperature [ 30 ]. The rationale for the increase in thermal stability of immobilized enzymes observed by majority of researchers is drop of these proteins’ flexibility, i.e., their ability to undergo changes in molecular structure.…”

Section: Resultsmentioning

confidence: 99%

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Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization

Drozd

Szymańska

Rakoczy

et al. 2018

Appl Biochem Biotechnol

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Bacterial cellulose spheres subjected to amination and inlaid modification with superparamagnetic molecules were analyzed with regard to possibility of their application as an immobilization carrier of Lecitase® Ultra (LU) enzyme. The starting point to obtain the carrier was synthesis of bacterial cellulose spheres performed in shaking cultures of Komagataeibacter xylinus. These spheres were subsequently subjected to a multi-stage modification to increase the efficiency of the immobilization process and to separate product from the reaction medium. Maximal yield of Lecitase® Ultra immobilization equaled 70%. It was also found that immobilization process did not affect the pH and LU temperature optimum. Moreover, immobilized enzyme exhibited similar temperature stability profile as its native form. The immobilization process did not significantly affect the enzyme K value. The immobilized enzyme retained over 70% of its initial activity after 8 cycles of use. The immobilized enzyme displayed good storage stability and retained 80% of its initial activity after 4 weeks at 4 °C. The potential application of such modified cellulose-based carrier may be correlated with lower costs of process thanks to higher enzyme's reusability in comparison to unbound enzyme. Moreover, data presented in the current study may serve as proof of a concept of cellulose-based carrier utilization for immobilization of enzymes other than LU and of high industrial importance.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization

Drozd

Szymańska

Rakoczy

et al. 2018

Appl Biochem Biotechnol

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“…Lecitase™ Ultra has been also employed for this goal and there are few reports concerning the application of Lecitase™ Ultra-catalyzed enantioselective hydrolysis of esters for the production of some important chiral drug intermediates. These applications covered the resolution of esters of 2-hydroxyacids with a phenyl ring including mandelates [33][34][35][36][37][38], resolution of glycidate esters [35,39,40], and N-acetyl-α-amino acid methyl esters [35]. Another example of an application in asymmetric synthesis was Lecitase™ Ultra-catalyzed regioselective hydrolysis of prochiral dimethyl 3-phenylglutarate [41].…”

Section: Introductionmentioning

confidence: 99%

“…As Lecitase™ Ultra is commercially available only in its free form as the water solution, many attempts have been made to prepare an immobilized form of this enzyme for different purposes, for example, by entrapment in gelatin hydrogel [47] or in different calcium alginates [48], immobilization on the derivatives of cellulose [49,50], polystyrene resin [51], styrene-divinylbenzene beads [37,52], magnetic nanoparticles [53], or by encapsulation in AOT(bis(2-ethylhexyl) sulfosuccinate sodium salt)/isooctane reverse micelles [54]. In the processes of the kinetic resolution of racemates catalyzed by immobilized Lecitase™ Ultra, the best results were obtained using gelatin [35,39], various derivatives of agarose [33,36,38,41,55], hexyl-and butyl-toyopearl [34], or epoxy activated polymer Dilbead VWR coated with polyethylenimine (PEI) and crosslinked with glutaraldehyde [40].…”

Section: Introductionmentioning

confidence: 99%

Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters

et al. 2020

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The influence of buffer type, co-solvent type, and acyl chain length was investigated for the enantioselective hydrolysis of racemic 4-arylbut-3-en-2-yl esters using Lecitase™ Ultra (LU). Immobilized preparations of the Lecitase™ Ultra enzyme had significantly higher activity and enantioselectivity than the free enzyme, particularly for 4-phenylbut-3-en-2-yl butyrate as the substrate. Moreover, the kinetic resolution with the immobilized enzyme was achieved in a much shorter time (24–48 h). Lecitase™ Ultra, immobilized on cyanogen bromide-activated agarose, was particularly effective, producing, after 24 h of reaction time in phosphate buffer (pH 7.2) with acetone as co-solvent, both (R)-alcohols and unreacted (S)-esters with good to excellent enantiomeric excesses (ee 90–99%). These conditions and enzyme were also suitable for the kinetic separation of racemic (E)-4-phenylbut-3-en-2-yl butyrate analogs containing methyl substituents on the benzene ring (4b,4c), but they did not show any enantioselectivity toward (E)-4-(4’-methoxyphenyl)but-3-en-2-yl butyrate (4d).

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“…LU was also successfully applied to the modifications of acyl chains in phospholipids by acidolysis or transesterification with fatty acids or their esters, respectively [25][26][27][28]. In the area of asymmetric synthesis, it was used for the enantioselective hydrolysis of some racemic mixtures, including mandelic acid derivatives [29], glycidate esters [30,31], α-aminoacids [32], and 4-arylbut-3-en-2-yl esters [33,34].…”

Section: Introductionmentioning

confidence: 99%

Enantioselective Transesterification of Allyl Alcohols with (E)-4-Arylbut-3-en-2-ol Motif by Immobilized Lecitase™ Ultra

et al. 2020

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Lecitase™ Ultra was immobilized on four different supports and tested for the first time as the biocatalyst in the kinetic resolution of racemic allyl alcohols with the (E)-4-arylbut-3-en-2-ol system in the process of transesterification. The most effective biocatalyst turned out to be the enzyme immobilized on agarose activated with cyanogen bromide (LU-CNBr). The best results (E > 200, ees and eep = 95–99%) were obtained for (E)-4-phenylbut-3-en-2-ol and its analog with a 2,5-dimethylphenyl ring whereas the lowest ee of kinetic resolution products (90%) was achieved for the substrate with a 4-methoxyphenyl substituent. For all substrates, (R)-enantiomers were esterified faster than their (S)-antipodes. The results showed that LU-CNBr is a versatile biocatalyst, showing high activity and enantioselectivity in a wide range of organic solvents in the presence of commonly used acyl donors. High operational stability of LU-CNBr allows it to be reused in three subsequent reaction cycles without negative effects on the efficiency and enantioselectivity of transesterification. This biocatalyst can become attractive to the commercial lipases in the process of the kinetic resolution of allyl alcohols.

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Immobilization of Lecitase® ultra on recyclable polymer support: application in resolution of trans-methyl (4-methoxyphenyl)glycidate in organic solvents

Cited by 11 publications

References 41 publications

Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization

Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization

Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters

Enantioselective Transesterification of Allyl Alcohols with (E)-4-Arylbut-3-en-2-ol Motif by Immobilized Lecitase™ Ultra

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