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Figure 3 | Microbial Cell Factories

Figure 3

From: Molecular cloning and biochemical characterization of a novel erythrose reductase from Candida magnoliae JH110

Figure 3

SDS-PAGE analysis of CmER expressed in recombinant E. coli. (A) Expression of CmER in the transformant E. coli BL21(DE3) harboring pCmER10, (B) Expressed CmER fused to GST at its N-terminus under the control of the tac promoter in E. coli BL21, (C) CmER expressed from the GST-fusion approach in conjunction with co-expression of molecular chaperones; Plasmids encoding the molecular chaperone, pGro7, pKJE7, and pGKJE3, were used to express GroEL-GroES, DnaK-DnaJ-GrpE, and GroEL-GroES-DnaK-DnaJ-GrpE, respectively, (D) SDS-PAGE analysis of CmER expressed and purified from the GST-fusion approach in conjunction with co-expression of molecular chaperones, GroEL-GroES-DnaK-DnaJ-GrpE. Lane M, protein standards; lane T, IPTG-induced total fraction; lane S, soluble fraction; lane I, insoluble fraction. Lane 1, soluble fraction of GST-fused CmER-expressed cells; lane 2, purified GST-CmER fusion protein; lane 3, cleavage of GST from GST-CmER fusion protein by Factor Xa; lane 4, purified intact CmER.

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