Fig. 6
From: A novel strategy for protein production using non-classical secretion pathway in Bacillus subtilis
Cleavage of fusion proteins by enterokinase. The B. subtilis 1A751 cells harboring pMA5R16E or pMA5R17E were cultured in SR medium in flasks at 37 °C. The culture medium was concentrated, and twofold concentrate was obtained. 20 mL concentrate was reacted with the enterokinase. a SDS-PAGE analysis. Lane 1, the concentrate containing RDPE; Lane 2, the concentrate containing RDPE-E-AmyL; RDPE-E-AmyL contains the enterokinase cleavage site between RDPE and AmyL; Lane 3, the concentrate containing RDPE-E-AmyL following cleavage with the enterokinase; Lane 4, the concentrate containing RDPE-E-GFP; RDPE-E-GFP contains the enterokinase cleavage site between RDPE and GFP; Lane 5, the concentrate containing RDPE-E-GFP following cleavage with the enterokinase; Lane 6, the concentrate containing AmyL; Lane 7, the concentrate containing GFP. b The relative activity analysis. Column 1 is the control. Column 2 is served as 100 %. c The relative RFU (relative fluorescence units) analysis. Column 1 is the control. Column 2 is served as 100 %. The samples 1, 2, 3, 4 and 5 in b or c are same with that in a. Data represent the mean of three parallel experiments, and error bars represent standard error