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. 2017 Jun 6;7:2816. doi: 10.1038/s41598-017-02559-6

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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 optimum temperature (a) and Ph (b) for recombinant CmLOX18. The effects of pH and temperature on the enzymatic activity of recombinant CmLOX18 were determined using linoleic acid (LA) as substrates. The recombinant CmLOX18 proteins displayed the highest catalytic activity at pH 4.5 (a) respectively. The optimum temperatures for CmLOX18 were observed at 30 °C (b), respectively. The maximum activity was estimated as 100%. Means ± SD were obtained from three independent measurements.