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. 2018 Oct 23;2018:4794690. doi: 10.1155/2018/4794690

Table 2.

The substrate specificity of the purified recombinant Bgl3Ba.

Substrate Glycosyl linkage Specific activity (U/mg) Relative activity (%)a
Aryl-glycosides
pNPG (2 mM) β-Glucose 222.8 ± 6.7 100.0
Genistin (1%) β-Glucose 69.7 ± 0.2 31.3
Daidzin (1%) β-Glucose 50.9 ± 0.2 22.8
Amygdalin (1%) - 146.9 ± 0.1 65.9
Oligosaccharides
Cellobiose (4 mM) β-1,4-Glucose 189.5 ± 1.8 100.0
Cellotriose (1%) β-1,4-Glucose 185.0 ± 4.1 97.6
Cellotetraose (1%) β-1,4-Glucose 94.1 ± 2.1 49.7
Cellopentaose (1%) β-1,4-Glucose 85.8 ± 1.5 45.3
Laminaritetraose (5 mM) [β-d-Glc-1,3)]3-d-Glc 173.0 ± 4.1 91.3
Polysaccharides
Laminarin (1%) β-1,3-Glucan 25.7 ± 0.9 100.0
Lichenan (0.5%) 1,3:(1,4)2-β-d-Glucan 25.6 ± 0.6 99.8
Barley β-d-glucan (1%) 1,3:1,4-β-d-Glucan 7.2 ± 0.2 28.1
Avicel (1%) β-1,4-Glucose 6.6 ± 0.2 25.5
Xylan (1%) β-1,4-Xylose 4.1 ± 0.5 16.1
CMC-Na (1%) β-1,4-Glucose 5.9 ± 0.4 23.0

aThe 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.