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. 2017 Jun 16;7:3700. doi: 10.1038/s41598-017-03927-y

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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 impact of X2-CBM3 on the activity of endoglucanase (Endo5A) and xylanase (Xyl11D). (a) Domain organization of fusion construct containing Endo5A and Xyl11D along with X2-CBM3 linked through a Gly-Ser linker, (b) SDS-PAGE profile of fusion enzyme Endo5A-X2-CBM3 (Lane1), native endoglucanase Endo5A (Lane 2), fusion enzyme Xyl11D-X2-CBM3 (Lane 3), and native xylanase Xyl11D (Lane 4); M: molecular weight marker in kDa. (c) Enzyme activity of endoglucanase for native and fusion constructs measured towards insoluble substrates- Avicel and biomass. Enzyme activity for xylanase was not included as the activity of both of its constructs towards insoluble substrate was negligible (see text and Table 4 for details).