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. 2017 Sep 20;7:11991. doi: 10.1038/s41598-017-11819-4

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© The Author(s) 2017

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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The purity of VAMAX1 in the fermentation supernatant. (a) Proteins in 15 µL supernatant taken at the end of the three-phase (3 P) and two-phase (2 P) fermentation strategies were separated by LDS-PAGE and visualized with SimplyBlue SafeStain. (b) Densitometric analysis of the separated proteins using AIDA Image Analyzer. Arrows represent the target protein VAMAX1. Numbered bands/peaks represent impurities that were cut from the gel for analysis by mass spectrometry.