Figure 2: BlCel5B enzymatic activity characterization. | Scientific Reports

Figure 2: BlCel5B enzymatic activity characterization.

From: Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism

Figure 2

(a) MALDI/TOF-MS spectra of the products released after incubation of BlCel5B and its two deletion constructs (ΔCBM46 and ΔIg-CBM46) with the substrate cellopentaose (C5). The first three spectra show the substrate, enzyme and buffer controls. The forth spectrum reveals that full length BlCel5B is capable of enzymatic hydrolysis of C5 into smaller oligosaccharides such as C4, C3 and C2. The last two spectra show that the C-terminal deletions eliminate the enzyme activity. BlCel5B activities on CMC as functions of pH and temperature are shown in (b) and (c), respectively. The enzyme exhibits optimal pH of 4.0 and optimal temperature of 55 °C, retaining about 50% of its activity at 80 °C. (d) Michaelis-Menten curve using CMC as a substrate.

Back to article page