BoXyl43A
Ex-Xyl0164
(EC.3.2.1.37)exo-β-1,4-Xylosidase
CAZy Family: GH43
PROPERTIES
1.ELECTROPHORETIC PURITY
-Single band on SDS-gel electrophoresis (MW ~37 kDa)
Figure 1. Electrophoresis analysis of BoXyl43A. M, molecular weight marker (PageRuler Prestained Protein Ladder, Thermo Scientific); lane 1, culture lysate of before IPTG induction; lane 2, culture lysate after IPTG induction; lane 3, BoXyl43A purified from Ni sepharose fastflow column.
2.SPECIFIC ACTIVITY
2.1 U/mg protein (on pNP-β-Xyl) at pH 7.0 and 37°C.
One Unit of pNP-β-Xylactivity is defined as the amount of enzyme required to release 1 μmol of p-nitrophenyl per minute from pNP-β-Xyl(5 mM) in phosphate buffer (20 mM) pH 7.0.
3.RELATIVE RATES OF HYDROLYSIS OF SUBSTRATES
Table 1. Relative activity ofBoXyl43A on different substratesa.
Substrateb |
Relative activity (%)c |
pNPβGlu |
_ |
pNPβGal |
_ |
pNPβMan |
_ |
pNPβXyl |
100±0.0 |
pNPαGlc |
_ |
pNPαGal |
_ |
pNPαMan |
_ |
pNPαAraf |
54±0.0 |
pNPαArap |
_ |
aReactions were performed with 5mM substrate, pH 7.0, at 37°C for 5 min.
bAbsorption caused by released p-nitrophenol was measured at 405nm. The relative activity on pNPαXyl was taken as 100%.
cThe data are reported as means±standard errors from the mean for three independent experiments.
4.PHYSICOCHEMICAL PROPERTIES
pH suggestion: 7.0
Temperaturesuggestion: 37°C
5.STORAGE CONDITIONS
The enzyme should be stored at -20 °C. For assay, this enzyme should be diluted inphosphate buffer (20 mM) pH 7.0. Swirl to mix the enzyme immediately prior to use.
6. REFERENCES
[1] Zhou AD, Hu YB, et al. Characterization of a recombinant β-xylosidase of GH43 family from Bacteroides ovatus strain ATCC 8483. Biocatalysis and Biotransformation, 2020, 38(1): 46-52.
BoXyl43A
Ex-Xyl0164
(EC.3.2.1.37)exo-β-1,4-Xylosidase
CAZy Family: GH43
PROPERTIES
1.ELECTROPHORETIC PURITY
-Single band on SDS-gel electrophoresis (MW ~37 kDa)
Figure 1. Electrophoresis analysis of BoXyl43A. M, molecular weight marker (PageRuler Prestained Protein Ladder, Thermo Scientific); lane 1, culture lysate of before IPTG induction; lane 2, culture lysate after IPTG induction; lane 3, BoXyl43A purified from Ni sepharose fastflow column.
2.SPECIFIC ACTIVITY
2.1 U/mg protein (on pNP-β-Xyl) at pH 7.0 and 37°C.
One Unit of pNP-β-Xylactivity is defined as the amount of enzyme required to release 1 μmol of p-nitrophenyl per minute from pNP-β-Xyl(5 mM) in phosphate buffer (20 mM) pH 7.0.
3.RELATIVE RATES OF HYDROLYSIS OF SUBSTRATES
Table 1. Relative activity ofBoXyl43A on different substratesa.
Substrateb |
Relative activity (%)c |
pNPβGlu |
_ |
pNPβGal |
_ |
pNPβMan |
_ |
pNPβXyl |
100±0.0 |
pNPαGlc |
_ |
pNPαGal |
_ |
pNPαMan |
_ |
pNPαAraf |
54±0.0 |
pNPαArap |
_ |
aReactions were performed with 5mM substrate, pH 7.0, at 37°C for 5 min.
bAbsorption caused by released p-nitrophenol was measured at 405nm. The relative activity on pNPαXyl was taken as 100%.
cThe data are reported as means±standard errors from the mean for three independent experiments.
4.PHYSICOCHEMICAL PROPERTIES
pH suggestion: 7.0
Temperaturesuggestion: 37°C
5.STORAGE CONDITIONS
The enzyme should be stored at -20 °C. For assay, this enzyme should be diluted inphosphate buffer (20 mM) pH 7.0. Swirl to mix the enzyme immediately prior to use.
6. REFERENCES
[1] Zhou AD, Hu YB, et al. Characterization of a recombinant β-xylosidase of GH43 family from Bacteroides ovatus strain ATCC 8483. Biocatalysis and Biotransformation, 2020, 38(1): 46-52.
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