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. 2020 Jul 11;19:140. doi: 10.1186/s12934-020-01397-y

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© The Author(s) 2020

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. 1 — SDS-PAGE analysis of the α-glucosidases from Metsnikowia species expressed in E. coli. Non-precipitated cell lysates of the bacteria including the constructions Mg-αGLU-pET28b(+) (lane 1) and Mr-αGLU-pET28b(+) (lane 3) were loaded. Ni-Sepharose purified fractions containing recombinant proteins Mg-αGlu (lane 2) and Mr-αGlu (lane 4) were also evaluated (a). Zymogram analysis using 1 M sucrose as substrate and purified Mg-αGlu (lane 1) or Mr-αGlu (lane 3). Commercial S. cerevisiae invertase was used as positive control (lanes 2 and 4) (b). Proteins in the range of 1–3 μg were loaded in each well. Numbers at the left of panels (a) and (b) indicate the positions of the molecular mass standards in kDa