Lipase-catalyzed kinetic resolution of 2-methylene-substituted cycloalkanols in batch and continuous-flow modes

Tomin, Anna; Hornyánszky, Gábor; Kupai, Katalin; Dorkó, Zsanett; Ürge, László; Darvas, Ferenç; Poppe, László

doi:10.1016/j.procbio.2010.02.006

Cited by 42 publications

(38 citation statements)

References 31 publications

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“…10B) [58]. Similar results were observed in continuous-flow KRs of racemic 1j, 1N and 1P-T with bioimprinted sol-gel lipases [46], of racemic 1j and 1k with sol-gel entrapped Lipase AK [47], as well as of cyclic racemic secondary alcohols 1U, 1X and 1Y with immobilized CaL B and Lipase AK [59] (Fig. 10B).…”

Section: Stereoselective Biotransformations In Continuous-flow Reactorssupporting

confidence: 79%

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From Synthetic Chemistry and Stereoselective Biotransformations to Enzyme Biochemistry – The Bioorganic Chemistry Group at the Budapest University of Technology and Economics

Boros¹,

Hornyánszky²,

Nagy³

et al. 2015

Period. Polytech. Chem. Eng.

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Section: Stereoselective Biotransformations In Continuous-flow Reactorssupporting

confidence: 79%

“…Continuous-flow KRs of alcohols were performed in stainless steel packed-bed reactors filled with different lipase preparations at analytical and at preparative scale (Fig. 10B) [41,46,47,58,59].…”

Section: Stereoselective Biotransformations In Continuous-flow Reactorsmentioning

confidence: 99%

From Synthetic Chemistry and Stereoselective Biotransformations to Enzyme Biochemistry – The Bioorganic Chemistry Group at the Budapest University of Technology and Economics

Boros¹,

Hornyánszky²,

Nagy³

et al. 2015

Period. Polytech. Chem. Eng.

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“…Most of the continuous-mode biocatalytic syntheses of optically active chiral intermediates on a relatively large scale are performed using immobilized lipases in packed-bed reactors [28]. Stainless steel continuous-flow packed-bed bioreactors can be effectively used to study the effects of temperature, pressure and flow rate on stereoselective biotransformations such as lipase-catalyzed kinetic resolutions [29], [30], [31] and [32].…”

Section: Introductionmentioning

confidence: 99%

Hydrophobic adsorption and covalent immobilization of Candida antarctica lipase B on mixed-function-grafted silica gel supports for continuous-flow biotransformations

Boros

Weiser

Márkus

et al. 2013

Process Biochemistry

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HighlightsPhenyl-/aminoalkylsilane-grafted silica gels were used as supports for CaLB.Adsorption onto mixed-function-grafted silica supports resulted in active CaLB.CaLB adsorption and glutardialdehyde cross-linking resulted in enhanced durability.The novel CaLB biocatalysts were used in kinetic resolutions of a secondary alcohol and an amine.The novel CaLBs were robust biocatalysts in continuous-flow biotransformations. AbstractAdsorption onto solid supports has proven to be an easy and effective way to improve the mechanical and catalytic properties of lipases. Covalent binding of lipases onto the support surface enhances the active lifetime of the immobilized biocatalysts. Our study indicates that mesoporous silica gels grafted with various functions are ideal supports for both adsorptive and covalent binding for lipase B from Candida antarctica (CaLB). Adsorption of CaLB on phenyl-functionalized silica gels improved in particular its specific activity, whereas adsorption on aminoalkyl-modified silica gels enabling covalent binding with the proper reagents resulted in only moderate specific activity. In addition, adsorption on silica gels modified by mixtures of phenyl-and aminoalkyl silanes significantly increased the productivity of CaLB. Furthermore, CaLB adsorbed onto a phenyl/aminoalkyl-modified surface and then treated with glutardialdehyde (GDA) as cross-linking agent provided a biocatalyst of enhanced durability. Adsorbed and cross-linked CaLB was resistant to detergent washing that would otherwise physically deactivate adsorbed CaLB preparations. The catalytic properties of our best immobilized CaLB variants, including temperaturedependent behavior were compared between 0 and 70 °C with those of two commercial CaLB biocatalysts in the continuous-flow kinetic resolutions of racemic 1-phenylethanol rac-1a and 1-phenylethanamine rac-1b.

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“…Due to its sensitivity to experimental error E values in the 100-200 range are given as[100, in the range of 200-500 as[200 and above 500 as )200. Effective specific activity of the biocatalyst (U B ) was determined using the equation U B = (n rac 9 c)/ (t 9 m B ) [where n rac (lmol) is the amount of the racemic substrate, t (min) is the reaction time and m B (g) is the mass of biocatalyst] [28]. Effective specific activity of the crude non-immobilized enzyme powder (U E ) was determined using the equation U E = (n rac 9 c)/(t 9 m E ) [where n rac (lmol) is the amount of the racemic substrate, t (min) is the reaction time and m E (g) is the mass of the crude nonimmobilized enzyme powder] [29].…”

Section: Lipase Adsorption On the Electrospun Nanofibersmentioning

confidence: 99%

Electrospun polylactic acid and polyvinyl alcohol fibers as efficient and stable nanomaterials for immobilization of lipases

Sóti

Weiser

Vígh

et al. 2016

Bioprocess Biosyst Eng

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Electrospinning was applied to create easy-tohandle and high-surface-area membranes from continuous nanofibers of polyvinyl alcohol (PVA) or polylactic acid (PLA). Lipase PS from Burkholderia cepacia and Lipase B from Candida antarctica (CaLB) could be immobilized effectively by adsorption onto the fibrous material as well as by entrapment within the electrospun nanofibers. The biocatalytic performance of the resulting membrane biocatalysts was evaluated in the kinetic resolution of racemic 1-phenylethanol (rac-1) and 1-phenylethyl acetate (rac-2). Fine dispersion of the enzymes in the polymer matrix and large surface area of the nanofibers resulted in an enormous increase in the activity of the membrane biocatalyst compared to the non-immobilized crude powder forms of the lipases. PLA as fiber-forming polymer for lipase immobilization performed better than PVA in all aspects. Recycling studies with the various forms of electrospun membrane biocatalysts in ten cycles of the acylation and hydrolysis reactions indicated excellent stability of this forms of immobilized lipases. PLA-entrapped lipases could preserve lipase activity and enantiomer selectivity much better than the PVA-entrapped forms. The electrospun membrane forms of CaLB showed high mechanical stability in the repeated acylations and hydrolyses than commercial forms of CaLB immobilized on polyacrylamide beads (Novozyme 435 and IMMCALB-T2-150).

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Lipase-catalyzed kinetic resolution of 2-methylene-substituted cycloalkanols in batch and continuous-flow modes

Cited by 42 publications

References 31 publications

From Synthetic Chemistry and Stereoselective Biotransformations to Enzyme Biochemistry – The Bioorganic Chemistry Group at the Budapest University of Technology and Economics

From Synthetic Chemistry and Stereoselective Biotransformations to Enzyme Biochemistry – The Bioorganic Chemistry Group at the Budapest University of Technology and Economics

Hydrophobic adsorption and covalent immobilization of Candida antarctica lipase B on mixed-function-grafted silica gel supports for continuous-flow biotransformations

Electrospun polylactic acid and polyvinyl alcohol fibers as efficient and stable nanomaterials for immobilization of lipases

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