Hydrolysis Of Naproxen Methyl Ester Research Articles

Lipase-catalyzed naproxen methyl ester hydrolysis in water-saturated ionic liquid: significantly enhanced enantioselectivity and stability

The lipase selective hydrolysis of Naproxen methyl ester was explored in both water-saturated isooctane and water-saturated ionic liquid 1-butyl-3-methylimidazolium hexafluoro-phoshate ([bmim]PF6) to see any significant differences in terms of enantioselectivity and stability between two different classes of reaction media. It is shown that polar and hydrophobic of [bmim]PF6 made it an unearthly reaction medium for hydrolysis of Naproxen methyl ester. It not only decreases the equilibrium constant (K) and enhances the enantiomeric ratio (E), consequently improves the equilibrium conversion (CEq) of the hydrolysis reaction and enantiomeric excess of product (eep), but also maintains the lipase activity. Because the lipase would not dissolve in the 1-butyl-3-methylimidazolium hexafluoro-phoshate, it can be filtrated up from 1-butyl-3-methylimidazolium hexafluoro-phoshate and recycled for several runs. The stability of lipase was improved due to the higher solubility of methanol in 1-butyl-3-methylimidazolium hexafluoro-phoshate than in isooctane.

Investigation of lipase-catalysed hydrolysis of naproxen methyl ester: use of NMR spectroscopy methods to study substrate–enzyme interaction

(±)-2-(6-Methoxy-2-naphthyl)propionic acid methyl ester (methyl ester of Naproxen), the precursor of therapeutically important nonsteroidal anti-inflammatory drugs (NSAIDs) was enantioselectively hydrolysed using as biocatalyst Candida rugosa lipase. In research aimed at studing the structure–activity relationship (SAR), NMR spectroscopy methods were employed to identify which Naproxen molecular moiety was essential to the substrate–enzyme interaction. The experimental results, in agreement with previous computer modelling studies and reported kinetic data, gave new information on the enzyme–substrate complex formation in solution.

Efficient microbial elimination of methanol inhibition for Naproxen resolution by a lipase

To eliminate methanol inhibition of the activity of a lipase, methanotrophic bacteria, which can convert methanol into water and CO2, were introduced to the reaction of enantioselective hydrolysis of Naproxen methyl ester catalysed by lipase from Candida rugosa. Both the activity and stability of lipase were improved by the removal of methanol by the bacteria.

Improvement of the enantioselectivity of lipase-catalyzed naproxen ester hydrolysis in organic solvent

A method is presented to improve the enantioselectivity of lipase-catalyzed hydrolysis of naproxen methyl ester in water-saturated isooctane. It is shown that coupling of the enantioselective hydrolysis of Naproxen methyl ester with the photo-dissociation methanol leads to the photocatalytic conversion of methanol into water, by which the equilibrium constant ( K) of the lipase-catalyzed hydrolysis was changed. The equilibrium yield and enantiomeric excess are increased. Because the lipase would not dissolve in the organic solvent, it was adsorbed on photocatalyst particles, which may facilitate the isolation of enzyme from reaction system.