Mild and efficient enzymatic oximolysis by supported Pseudomonas cepacia lipases

Pseudonomas cepacia lipase supported on ceramic particles (lipase PS-C) and diatomite (lipase PS-D) catalyzed the acylation of aldoximes and ketoximes. Aliphatic oximes reacted faster than aromatic oximes and polar solvents enhanced the reaction rate. For lipase PS-C, THF was a superior solvent, whi...

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Bibliographic Details
Published in:Journal of molecular catalysis. B, Enzymatic Enzymatic, 2000-10, Vol.10 (5), p.535-538
Main Authors: Salunkhe, Manikrao M, Nair, Ranjeet V
Format: Article
Language:English
Subjects:
Acylation
Bacteria
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Catalysis
Ceramic materials
Composition effects
Esters
Ethers
Fundamental and applied biological sciences. Psychology
Lipase PS-C
Lipase PS-D
Methods. Procedures. Technologies
Organic solvents
Oxime esters
Rate constants
Recyclability
Solvent effect
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Summary:Pseudonomas cepacia lipase supported on ceramic particles (lipase PS-C) and diatomite (lipase PS-D) catalyzed the acylation of aldoximes and ketoximes. Aliphatic oximes reacted faster than aromatic oximes and polar solvents enhanced the reaction rate. For lipase PS-C, THF was a superior solvent, while for lipase PS-D 1,4-dioxane was the ideal solvent. The amount of enzyme required to catalyze this reaction was optimized. It was found that for lipase PS-C or lipase PS-D, 50 mg was the optimum amount to catalyze 1.0 mmol of substrate.
ISSN:1381-1177
1873-3158
DOI:10.1016/S1381-1177(00)00096-5