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. 2017 Mar 17;16:49. doi: 10.1186/s12934-017-0661-5

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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. 2 — AOX1 mutations and activity in several ancestral and evolved P. pastoris strains. a Aox1 protein domains according to the recently published crystal structure (PDB ID 5HSA) [49]. Amino acid positions mutated in the evolved strains are highlighted. b Alcohol oxidase activity in P. pastoris strains. Activity was determined as described in the “Methods” section. The enzymatic activity of wildtype P. pastoris X-33 on YPM and BMM growth medium was set to 100%. The activity of the wildtype strain on glucose and methanol is shown, as well as the activity of four evolved strains with mutations of the AOX1 gene on methanol as carbon source. YPM (black bars), BMM (grey bars); Values represent averages of two biological and two technical replicates ±standard deviation