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. 2018 Nov 8;11:305. doi: 10.1186/s13068-018-1297-3

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© The Author(s) 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 4 — Characterization of Kdc4427 and Adh4428. A Characterization of Kdc4427 and comparison with corresponding ARO10. a E. coli BL09 and E. coli BL11 cells were cultivated, and their cell growth (OD₆₀₀) and 2-PE production titers were compared. b Phenylpyruvate decarboxylase from Kdc4427 and ARO10 in recombinant E. coli BL21(DE3) whole cells. The conversion of 1 g/L phenylpyruvate to 2-PE. B Characterization of Adh4428 and comparison with corresponding ADH2. a E. coli BL12 and E. coli BL09 cells were cultivated, and their cell growth (OD₆₀₀) and 2-PE production titers were compared. b Phenylpyruvate dehydrogenase from Adh4428 and ADH2 in recombinant E. coli BL21(DE3) whole cells. The conversion of 1 g/L phenylacetaldehyde to 2-PE