MOESM1 of Redesign of a novel d-allulose 3-epimerase from Staphylococcus aureus for thermostability and efficient biocatalytic production of d-allulose

Additional file 1: Table S1. Primers used for the construction of recombinant SaDAE. Figure S1. Multiple sequence alignment of amino acid sequence for the SaDAE with D-allulose 3-epimerase, L-ribulose 3-epimerase, and D-tagatose 3-epimerase from various strains. Figure S2. Purification of SaDAE by anion-exchange (a) and size-exclusion chromatography (b). Protein markers of conalbumin (75.0Â kDa) and aldolase (158.0Â kDa) were used. (c) MALDI-TOF spectra of SaDAE. Figure S3. (a) CD spectrum of SaDAE and (b) secondary structure assignments. Figure S4. Products confirmation of the enzymatic conversion using HPLC. (a) D-allulose (b) d-fructose (c) D-sorbose (d) D-tagatose. Figure S5. Structure comparison of SaDAE (yellow) with ketose 3-epimerases from different family. Figure S6. Multiple sequence alignment of amino acid D-allulose 3-epimerase, L-ribulose 3-epimerase, and D-tagatose 3-epimerase from different strains