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

<div>Enzymatic activity of BglA. (a) Lineweaver–Burk plot having substrate (salicin) concentration in mM on X-axis and enzyme (BglA) activity in μM·min−1 on Y-axis; (b) reciprocated substrate concentration and enzyme activity values from which Michaelis–Menten constant was derived through nonlinear regression.</div>

BioMed Research International

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Figure 4

Figure 4: Soluble Production, Characterization, and Structural Aesthetics of an Industrially Important Thermostable β-Glucosidase from Clostridium thermocellum in Escherichia coli

Figure 4 | Soluble Production, Characterization, and Structural Aesthetics of an Industrially Important Thermostable β-Glucosidase from Clostridium thermocellum in Escherichia coli 