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. 2016 Nov 29;101(6):2319–2331. doi: 10.1007/s00253-016-7993-7

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© The Author(s) 2016

Open Access This 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.

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Fig. 2 — Enzyme concentration dependent activity of unfused P450_BM3 (squares), unfused PTDH (squares), and PTDH-P450_BM3 (circles). The graphs show the relation between enzyme concentration and the initial activities for a oxidation of 0.20 mM NADPH in the presence of 0.4 mM lauric acid as substrate at varying concentrations of either P450_BM3 or PTDH-P450_BM3 and b reduction of NADP⁺ in the presence of 2.0 mM phosphite as substrate at varying concentrations of either PTDH or PTDH-P450_BM3. Concentrations of (PTDH)-P450_BM3 were determined via CO-difference spectra, PTDH concentrations by Waddell’s method. Experiments were performed in triplicate