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. 2020 May 15;3:62. doi: 10.1038/s42004-020-0305-2

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© The Author(s) 2020

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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Fig. 3 — EstA variants with substitutions in the cleavage site (R70A, S71A and I72A) were created (a) to elucidate the contribution of these residues. The cleavage of these variants with aAbPPO4 was monitored and compared to the cleavage of wild type (WT) EstA (b). HPLC analyses of the hydrolysis products showed a higher increase in MHET and Ta after hydrolysis with the truncated (ΔEstA) compared to the full-length EstA. Measurements were performed in triplicates and the standard deviation is given in the error bars (c). EstA hydrolysed PET more efficiently when cleaved by tyrosinases (d).