Neat lipase-catalysed kinetic resolution of racemic 1-phenylethanol and a straightforward modelling of the reaction
Autor: | Zsófia Varga, Ágnes Szécsényi, Ildikó Kmecz, Edit Székely |
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Rok vydání: | 2017 |
Předmět: |
biology
Tributyrin 010405 organic chemistry Lipase b Atmospheric temperature range 010402 general chemistry biology.organism_classification 01 natural sciences Biochemistry Catalysis 0104 chemical sciences Kinetic resolution chemistry.chemical_compound chemistry biology.protein Glycerol Organic chemistry Candida antarctica Lipase Biotechnology Initial rate |
Zdroj: | Biocatalysis and Biotransformation. 35:427-433 |
ISSN: | 1029-2446 1024-2422 |
DOI: | 10.1080/10242422.2017.1360292 |
Popis: | Enzymatic kinetic resolution of racemic 1-phenylethanol catalysed by immobilized Candida antarctica lipase B was investigated in a neat system at the temperature range of 30–70 °C. Synthetic triglycerides, namely glycerol triacetate and glycerol tributyrate, were applied as the esterification agents. Both esterification agents were efficient regarding to the enantioselectivity (>1000). Initial rate of reaction and the kinetic constants were influenced by the applied esterification agent significantly. A detailed modelling approach is presented and verified in the temperature range on 30–60 °C for the tributyrin system. |
Databáze: | OpenAIRE |
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