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. 2020 Dec 3;13:197. doi: 10.1186/s13068-020-01843-4

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© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. 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 in a credit line to the data.

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Fig. 5 — Enzymatic oxidation of monolignols by recombinant PtoLAC14 protein. a Quantification of PtoLAC14 activity in E. coli, with ABTS as the substrate. b The purified recombinant PtoLAC14 protein analyzed by SDS-PAGE. c The activity of purified recombinant PtoLAC14 protein, with coniferyl alcohol and sinapyl alcohol as the substrate. d Kinetic properties of PtoLAC14 in vitro. Km and Vmax were determined by linear regression of v against v/s (Eadie–Hofstee plot) with at least five data points. The data are mean values from three independent measurements