Conversion of levulinic acid to 2-butanone by acetoacetate decarboxylase from Clostridium acetobutylicum
| Autor: | Kyoungseon Min, Byoung-In Sang, Seil Kim, Youngsoon Um, Taewoo Yum, Yunje Kim |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Clostridium acetobutylicum
biology Carboxy-Lyases Chemistry Decarboxylation Temperature Enzyme Activators Substrate (chemistry) General Medicine Hydrogen-Ion Concentration biology.organism_classification Applied Microbiology and Biotechnology Butanones Levulinic Acids Recombinant Proteins chemistry.chemical_compound Acetoacetate decarboxylase Biocatalysis Yield (chemistry) Escherichia coli Levulinic acid Organic chemistry Methylene blue Biotechnology |
| Zdroj: | Applied Microbiology and Biotechnology. 97:5627-5634 |
| ISSN: | 1432-0614 0175-7598 |
| Popis: | In this study, a novel system for synthesis of 2-butanone from levulinic acid (γ-keto-acid) via an enzymatic reaction was developed. Acetoacetate decarboxylase (AADC; E.C. 4.1.1.4) from Clostridium acetobutylicum was selected as a biocatalyst for decarboxylation of levulinic acid. The purified recombinant AADC from Escherichia coli successfully converted levulinic acid to 2-butanone with a conversion yield of 8.4-90.3 % depending on the amount of AADC under optimum conditions (30 °C and pH 5.0) despite that acetoacetate, a β-keto-acid, is a natural substrate of AADC. In order to improve the catalytic efficiency, an AADC-mediator system was tested using methyl viologen, methylene blue, azure B, zinc ion, and 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as mediators. Among them, methyl viologen showed the best performance, increasing the conversion yield up to 6.7-fold in comparison to that without methyl viologen. The results in this study are significant in the development of a renewable method for the synthesis of 2-butanone from biomass-derived chemical, levulinic acid, through enzymatic decarboxylation. |
| Databáze: | OpenAIRE |
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