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. 2016 Feb 4;15:27. doi: 10.1186/s12934-016-0424-8

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© Guo et al. 2016

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. 3 — HPLC analysis of reaction products from E. coli [pET28a] (1), heat denatured protein extracts derived from E. coli [pET28a-Oc4CL1] (2) and crude protein extracts of E. coli [pET28a-Oc4CL1] (3) using trans-cinnamic acid (a), ρ-coumaric acid (b), caffeic acid (c), and ferulic acid (d) as the substrates. R2, X2, C2, A2, R1, X1, C1 and A1 refer to substrates trans-cinnamic acid (5), ρ-coumaric acid (6), caffeic acid (7), ferulic acid (8), and their corresponding products trans-cinnamoyl CoA (10), 4-coumaroyl CoA (11), caffeoyl CoA (12) and feruloyl CoA (13), respectively. Detection was set at 270 nm for reaction product of trans-cinnamic acid (5), 320 nm for enzymatic products of ρ-coumaric acid (6), caffeic acid (7) and ferulic acid (8). mAU Milliabsorbance units