Enantioselective hydrolysis of (R,S)-Naproxen methyl ester using Candida rugosa lipase with calix[4]arene derivatives

Akceylan, Ezgi; Akoz, Enise; Şahin, Özlem

doi:10.1007/s10847-014-0452-0

Cited by 5 publications

(4 citation statements)

References 19 publications

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“…This conformational change can occur as a result of the displacement of its polypeptide functional group, which could facilitate the access of S-enantiomer of the racemic mixture to the active center of the enzyme. [1][2][3]10,24 The ions of buffer solutions could change the solubility of the enzyme; it may cause the enzyme to be more hydrophobic or more hydrophilic, or may alter the enzyme configuration by attraction and repulsion forces. Therefore, it has a significant effect on enzyme performance.…”

Section: Effect Of Phmentioning

confidence: 99%

“…1,2 In addition, based on registration of new chiral drugs, the production of enantiomerically pure compounds are permitted. The reason is that one of the two enantiomers is often more biologically active than the other or may cause undesired side effects.…”

Section: Introductionmentioning

confidence: 99%

“…The reason is that one of the two enantiomers is often more biologically active than the other or may cause undesired side effects. 1,2 In addition, based on registration of new chiral drugs, the production of enantiomerically pure compounds are permitted. This fact has led to great efforts to develop efficient methods to obtain enantiomerically pure compounds in recent years.…”

Section: Introductionmentioning

confidence: 99%

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Enantioselective synthesis of (S)‐naproxen using immobilized lipase on chitosan beads

et al. 2017

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S-naproxen by enantioselective hydrolysis of racemic naproxen methyl ester was produced using immobilized lipase. The lipase enzyme was immobilized on chitosan beads, activated chitosan beads by glutaraldehyde, and Amberlite XAD7. In order to find an appropriate support for the hydrolysis reaction of racemic naproxen methyl ester, the conversion and enantioselectivity for all carriers were compared. In addition, effects of the volumetric ratio of two phases in different organic solvents, addition of cosolvent and surfactant, optimum pH and temperature, reusability, and inhibitory effect of methanol were investigated. The optimum volumetric ratio of two phases was defined as 3:2 of aqueous phase to organic phase. Various water miscible and water immiscible solvents were examined. Finally, isooctane was chosen as an organic solvent, while 2-ethoxyethanol was added as a cosolvent in the organic phase of the reaction mixture. The optimum reaction conditions were determined to be 35 °C, pH 7, and 24 h. Addition of Tween-80 in the organic phase increased the accessibility of immobilized enzyme to the reactant. The optimum organic phase compositions using a volumetric ratio of 2-ethoxyethanol, isooctane and Tween-80 were 3:7 and 0.1% (v/v/v), respectively. The best conversion and enantioselectivity of immobilized enzyme using chitosan beads activated by glutaraldehyde were 0.45 and 185, respectively.

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Section: Effect Of Phmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Enantioselective synthesis of (S)‐naproxen using immobilized lipase on chitosan beads

et al. 2017

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“…Thus, covalent immobilization improves storage stability of enzyme. In fact, covalent bond makes modification in three dimensional structure of the enzyme, which leads to conformation change of the active center [27][28][29].…”

Section: Stability Tests and Leakage Of Immobilized Amylasementioning

confidence: 99%

Textural and Structural Characterizations of Mesoporous Chitosan Beads for Immobilization of Alpha-Amylase: Diffusivity and Sustainability of Biocatalyst

Darzi

Gilani

Farrokhi

et al. 2019

IJE

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In the present study, textural and structural characterizations of chitosan bead for immobilization of alpha amylase in detail by N2 adsorption-desorption, Microspore Analysis (MP), Barrett-Joyner-Halenda (BJH) plots and Field Emission Scanning Electron Microscope (FESEM) observations were investigated. Pore structure observation revealed chemical activation of chitosan bead by glutaraldehyde can change both the isotherm type of adsorption and pores shape. In consistence with textural analysis, the high value of pore volume distribution with range of mesopores region indicated the porosity of activated chitosan bead was uniformly increased. Intra-particle diffusion model designated that 97.6% of amylase was adsorbed inside the mesopores of activated chitosan bead owing to increase in kid (rate constant) and reduce of boundary layer effect on diffusion process. In addition, the stability experiments (pH, storage and thermal stability), enzyme leakage, Ca 2+ and salt concentration effects were evaluated for immobilized amylase and compared with its free activities. Ca 2+ concentration of 1 mM shows an excellent impact on relative activity of amylase on its free and immobilized forms. NaCl experiments indicated that 84% of amylase was covalently immobilized on activated chitosan beads. Further, the Michaelis-Menten kinetic coefficients, Km (~0.4mg/ml) and, Vmax(~227 U/mg Enzyme), point out strong affinity and high activity of immobilized enzym.

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Calixarenes in Organo and Biomimetic Catalysis

Sayın

2016

Calixarenes and Beyond

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Enantioselective hydrolysis of (R,S)-Naproxen methyl ester using Candida rugosa lipase with calix[4]arene derivatives

Cited by 5 publications

References 19 publications

Enantioselective synthesis of (S)‐naproxen using immobilized lipase on chitosan beads

Enantioselective synthesis of (S)‐naproxen using immobilized lipase on chitosan beads

Textural and Structural Characterizations of Mesoporous Chitosan Beads for Immobilization of Alpha-Amylase: Diffusivity and Sustainability of Biocatalyst

Calixarenes in Organo and Biomimetic Catalysis

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