BioMed Research International / 2018 / Article / Tab 2

Research Article

A Novel Thermostable GH3 β-Glucosidase from Talaromyce leycettanus with Broad Substrate Specificity and Significant Soybean Isoflavone Glycosides-Hydrolyzing Capability

Table 2

The substrate specificity of the purified recombinant Bgl3B.

SubstrateGlycosyl linkageSpecific activity (U/mg)Relative activity (%)

Aryl-glycosides
pNPG (2 mM)β-Glucose222.8 ± 6.7100.0
Genistin (1%)β-Glucose69.7 ± 0.231.3
Daidzin (1%)β-Glucose50.9 ± 0.222.8
Amygdalin (1%)-146.9 ± 0.165.9
Oligosaccharides
Cellobiose (4 mM)β-1,4-Glucose189.5 ± 1.8100.0
Cellotriose (1%)β-1,4-Glucose185.0 ± 4.197.6
Cellotetraose (1%)β-1,4-Glucose94.1 ± 2.149.7
Cellopentaose (1%)β-1,4-Glucose85.8 ± 1.545.3
Laminaritetraose (5 mM)[β-D-Glc-1,3)]3-D-Glc173.0 ± 4.191.3
Polysaccharides
Laminarin (1%)β-1,3-Glucan25.7 ± 0.9100.0
Lichenan (0.5%)1,3:(1,4)2-β-D-Glucan25.6 ± 0.699.8
Barley β-D-glucan (1%)1,3:1,4-β-D-Glucan7.2 ± 0.228.1
Avicel (1%)β-1,4-Glucose6.6 ± 0.225.5
Xylan (1%)β-1,4-Xylose4.1 ± 0.516.1
CMC-Na (1%)β-1,4-Glucose5.9 ± 0.423.0

The data are shown as mean ± SD (n = 3). The specific activities of Bgl3B towards pNPG, cellobiose, and laminarin are defined as 100% for the aryl-glycosides, oligosaccharides, and polysaccharides, respectively.

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