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Table 4 Hydrolytic specific activities of two purified β-glucosidases (nBgl3 and rBgl3) on various substrates.

From: Characterization of a thermostable β-glucosidase from Aspergillus fumigatus Z5, and its functional expression in Pichia pastoris X33

Substrate

Specific activity (U mg-1)

Relative activityb (%)

Linkage of glycosyl group

 

nBgl3

rBgl3

nBgl3

rBgl3

 

4-Nitrophenyl-β-D-glucopyranoside (1 mM)

103.5 ± 7.1a

101.7 ± 5.2

100

100

βGlc

4-Nitrophenyl-α-D-glucopyranoside (1 mM)

< 0.01

< 0.01

0

0

αGlc

Cellobiose (5 mM)

64.1 ± 3.8

59.4 ± 2.1

61.9

58.4

β (1,4) Glc

Cellotriose (5 mM)

41.4 ± 3.2

39.3 ± 1.2

40.0

38.6

β (1,4) Glc

Cellotetraose (5 mM)

35.5 ± 1.6

32.7 ± 2.3

34.3

32.2

β (1,4) Glc

Cellopentaose (5 mM)

29.5 ± 2.0

23.7 ± 1.3

28.5

23.3

β (1,4) Glc

Carboxymethyl cellulose (1%, w/v)

< 0.01

< 0.01

0

0

β (1,4) Glc

Lactose (1%, w/v)

< 0.01

< 0.01

0

0

α (1,4) Glc

Xylan (1%, w/v)

< 0.01

< 0.01

0

0

β (1,4) Xyl

Lichenan (1%, w/v)

13.2 ± 0.1

9.7 ± 0.2

12.8

9.5

β (1,3-1,4) Glc

Laminarin (1%, w/v)

18.4 ± 1.3

17.5 ± 0.6

17.8

17.2

β (1,3) Glc

Gentiobiose (1%, w/v)

34.3 ± 2.4

29.4 ± 1.6

33.1

28.9

β (1,6) Glc

Salicin (1%, w/v)

38.1 ± 1.5

31.8 ± 2.7

36.8

31.3

βGlc

Avicel (1%, w/v)

2.1 ± 0.1

1.7 ± 0.08

2.0

1.7

β (1,4) Glc

  1. The purified enzyme was assayed in the standard assay condition with various compounds. Results are the mean of three replicates and varies from the mean by not more than 10%
  2. aStandard deviations of specific activity; bThe activity for pNPG was defined as 100%; nBgl3: the native Bgl3; rBgl3: the recombinant Bgl3