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. 2018 May 23;8:8075. doi: 10.1038/s41598-018-26104-1

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© The Author(s) 2018

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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Characterization of the exo-acting mannuronan (M) lyase Nonul2377. (A) Representative degradation kinetic revealing the poly-M substrate specificity. Incubation on standard alginate substrates was conducted, at least, with two independent production of enzymes. (B) The exolytic mode of action of the enzymes was visualized using size-exclusion chromatography. Δ: 4-deoxy-L-erythro-5-hexoseulose uronic acid.