“…Table 2 shows that the hydrolysis of racemic 1-phenylethyl acetate (rac-2) in aqueous media took place with all the three forms of CaLB resulting in high conversions (50, 50 and 41 %) after 2 h reaction time. In the hydrolytic reaction commercial immobilized CaLBs showed high selectivity and activity (E [ 200 and c = 50 %), which slightly lower (but still acceptable) when the PLA-entrapped CaLB biocatalysts (E [ 100 and c = 41 %) was used [33]. It should be noted that similar selectivity (E [ 100) was determined in case of non-immobilized CaLB form.…”
Section: Recycling Study Of Immobilized Biocatalystsmentioning
confidence: 51%
“…According to the previous results, a high degree of enantiomeric ratio (E [ 100) enables the preparation of both enantiomeric forms [i.e. (R)-2 and (S)-1] in appropriate enantiomeric purity (ee [ 95 %) and productivity (yield [ 45 %, based on the racemic substrate) [33].…”
Section: Comparison Of Lipase Encapsulation Within Pva and Pla Electrmentioning
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).
“…Table 2 shows that the hydrolysis of racemic 1-phenylethyl acetate (rac-2) in aqueous media took place with all the three forms of CaLB resulting in high conversions (50, 50 and 41 %) after 2 h reaction time. In the hydrolytic reaction commercial immobilized CaLBs showed high selectivity and activity (E [ 200 and c = 50 %), which slightly lower (but still acceptable) when the PLA-entrapped CaLB biocatalysts (E [ 100 and c = 41 %) was used [33]. It should be noted that similar selectivity (E [ 100) was determined in case of non-immobilized CaLB form.…”
Section: Recycling Study Of Immobilized Biocatalystsmentioning
confidence: 51%
“…According to the previous results, a high degree of enantiomeric ratio (E [ 100) enables the preparation of both enantiomeric forms [i.e. (R)-2 and (S)-1] in appropriate enantiomeric purity (ee [ 95 %) and productivity (yield [ 45 %, based on the racemic substrate) [33].…”
Section: Comparison Of Lipase Encapsulation Within Pva and Pla Electrmentioning
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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