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. 2021 Jul 23;20:143. doi: 10.1186/s12934-021-01635-x

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© The Author(s) 2021

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 4 — Purification of 6 × His-SUMO-LG fusion protein and rLG. A The 6 × His-SUMO-LG fusion protein purified by affinity chromatography and detected by Tricine-SDS-PAGE. Lane 1: Low range prestained protein marker; Lane 2: fermentation supernatant; Lane 3: penetrable apex; Lanes 4–8: The fermentation supernatant was eluted in 10 mM, 50 mM, 80 mM, 150 mM, and 250 mM imidazole. B Tricine-SDS-PAGE analysis of the 6 × His-SUMO-LG protein cleaved by SUMO protease. Lane 1: Low range prestained protein marker; Lane 2: 6 × His-SUMO-LG without cleavage; Lane 3: 6 × His-SUMO-LG cleaved by SUMO protease. C Tricine-SDS-PAGE analysis of the rLG. Lane 1: Low range prestained protein marker; Lane 2: rLG. D MALDI-TOF mass spectrum of purified rLG