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. 2017 Jul 28;7:6764. doi: 10.1038/s41598-017-07119-6

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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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Enzyme kinetics of LOx-PU coated sites and GOx-PU coated sites towards lactate (blue line) and glucose (orange line) detection. Grey line represents the response of the sentinel site. (A) Representative calibration showing responses of LOx-GOx MBA to successive additions of lactate and glucose. The final concentrations after each addition was 0.05, 0.1, 0.2, 0.5, 1, 2, 3, 5, 7.5, 10, 15 and 20 mM for lactate and 0.125, 0.5, 1, 2, 4, 8,12, 20, 28, 44 and 60 mM for glucose. (B,C) Calibration plot of the average steady-state current as a function of lactate (B) and glucose (C) concentration. Data were fitted to the Michaelis–Menten equation by using non-linear regression analysis. Inserts: Linear regression of the response of the LOx-PU coated sites (B) and GOx-PU coated sites (C) to lactate and glucose, respectively.