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. 2017 Sep 12;7:11425. doi: 10.1038/s41598-017-11542-0

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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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(a) The surface of ULam111 displaying a straight topology. The additional loop of ZgLamA is red. (b) Superposition of the structures of ULam111 (green), BglF from Nocardiopsis sp. strain F96 (salmon), TmLam (cyan), and PfLamA from hyperthermophile Pyrococcus furiosus (magenta). The disulfide linkage of Cys31-Cys34 is shown as red sticks. The black dashed cycles showed different structures between ULam111 and other GH16 family enzymes. (c) Relative activity of ULam111 mutant toward laminarin. The activity of wild-type ULam111 is represented as 100 and the error bars are standard deviations (n = 3).