Soluble Production, Characterization, and Structural Aesthetics of an Industrially Important Thermostable <i>β</i>-Glucosidase from <i>Clostridium thermocellum</i> in <i>Escherichia coli</i>

<div>Solubility analysis and purification of BglA by 12% SDS-PAGE. Lane M: protein standard marker; Lane 1: control (pET28a, without gene of interest); Lane 2: pET28a-bglA, total cellular protein (TCP) of <i>E. coli</i> BL21-CodonPlus (DE3)-RIPL cells showing expression of BglA at ∼53 kDa; Lane 3: insoluble fraction of TCP; Lane 4: soluble fraction of TCP showing expression of BglA at ∼53 kDa; Lane 5: pelleted proteins after heat inactivation of soluble fraction; Lane 6: supernatant proteins after heat inactivation of soluble fraction; Lane 7: purified His-tagged BglA protein through Ni<sup>2+</sup>-NTA chromatography.</div>

BioMed Research International

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Figure 3

Figure 3: Soluble Production, Characterization, and Structural Aesthetics of an Industrially Important Thermostable <i>β</i>-Glucosidase from <i>Clostridium thermocellum</i> in <i>Escherichia coli</i> 

Figure 3 | Soluble Production, Characterization, and Structural Aesthetics of an Industrially Important Thermostable β-Glucosidase from Clostridium thermocellum in Escherichia coli 