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. 2017 Jun 24;10:164. doi: 10.1186/s13068-017-0854-5

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© The Author(s) 2017

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. 7 — Hemiacetal oxidation activity of K. marxianus alcohol dehydrogenases. KmADH1–7 were heterologously overexpressed in S. cerevisiae BY 4742. Cell lysate assays showed that KmAdh7 exhibits activity toward synthesis of ethyl acetate from hemiacetal. Enzyme expression was confirmed by Western blot using anti-c-MYC and anti-GAPDH antibodies. Bars and error bars represent the arithmetic mean and standard deviation of triplicate samples