Min, Kyoungseon Kim, Seil Yum, Taewoo Kim, Yunje Sang, Byoung-In Um, Youngsoon 2024-01-20T12:04:58Z 2024-01-20T12:04:58Z 2021-09-04 2013-06 0175-7598 https://pubs.kist.re.kr/handle/201004/128019 In this study, a novel system for synthesis of 2-butanone from levulinic acid (gamma-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 A degrees C and pH 5.0) despite that acetoacetate, a beta-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. English Springer Verlag Conversion of levulinic acid to 2-butanone by acetoacetate decarboxylase from Clostridium acetobutylicum Article 10.1007/s00253-013-4879-9 1 Applied Microbiology and Biotechnology, v.97, no.12, pp.5627 - 5634 Applied Microbiology and Biotechnology 97 12 5627 5634 N scie scopus 000319609400041 2-s2.0-84878679101 Biotechnology & Applied Microbiology Biotechnology & Applied Microbiology Article OXIDATIVE DECARBOXYLATION TRANSPORTATION FUELS ESCHERICHIA-COLI LACCASE BUTANOL DECOLORIZATION MEDIATORS BIOFUELS STRAW Enzymatic decarboxylation Acetoacetate decarboxylase Levulinic acid 2-Butanone