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. 2021 Mar 4;20:60. doi: 10.1186/s12934-021-01550-1

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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. 5 — SDS-PAGE analysis of d-allulose 3-epimerase (DaeB). Lane 1: Pellet of B. subtilis transformed with vector; lane 2: Crude cell extract of B. subtilis transformed with vector; Lane 3: Pellet of B. subtilis expressing DaeB; Lane 4: Crude cell extract of B. subtilis expressing DaeB; Lane 5: Purified DaeB protein; Lane M: Protein marker (a). Western blot of DaeB protein using monoclonal anti-polyhistidine and antimouse IgG alkaline phosphatase antibody (b). Native-PAGE analysis of DaeB protein (c). Determination of native molecular mass of DaeB protein by gel filtration. The column was calibrated with standard proteins- Ribonuclease (13.7 kDa), Ovalbumin (44 kDa), Conalbumin (75 kDa) and Aldolase (158 kDa). DaeB is labeled with green square (d)