BaAra43A (exo-α-arabinofuranosidase,AXH-d3)

BaAra43A (AXH-d3)

Exo-Gal0153

(EC. 3.2.1.55) exo-α-L-arabinofuranosidase

CAZy Family: GH43

 

PROPERTIES

1. ELECTROPHORETIC PURITY

-Single band on SDS-gel electrophoresis (MW ~59 kDa)

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Figure 1. Electrophoresis analysis of BaAra43A. M, molecular weight marker (PageRuler Prestained Protein Ladder, Thermo Scientific); lane 1, culture lysate before IPTG induction; lane 2, culture lysate after IPTG induction; lane 3, BaAra43A  purified from Ni sepharose fastflow column.

 

2. SPECIFIC ACTIVITY

No activity on pNPαAra. Only C3-linked arabinose residues from double-substituted xylose residues.

 

3. RELATIVE RATES OF HYDROLYSIS OF SUBSTRATES

 

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Figure 2.  A–C High-performance anion-exchange analysis of the reaction products obtained after incubation of the oligosaccharide 6.1 with arabinofuranohydrolase. A Untreated oligosaccharide 6.1; B oligosaccharide 6.1 treated with arabinofuranohydrolase; C standard oligosaccharide 5.4.

 

4. PHYSICOCHEMICAL PROPERTIES

 pH Optima: suggested use 6.0

Temperature Optima: suggested use 30°C

 

5. STORAGE CONDITIONS

The enzyme should be stored at -20°C. For assay, this enzyme should be diluted in phosphate buffer (20 mM) pH 7.0. Swirl to mix the enzyme immediately prior to use.

 

6.  REFERENCES

[1] Van Laere KM, Beldman G, Voragen AG. A new arabinofuranohydrolase from Bifidobacterium adolescentis able to remove arabinosyl residues from double-substituted xylose units in arabinoxylan. Appl Microbiol Biotechnol. 1997 Mar;47(3):231-5.

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BaAra43A (exo-α-arabinofuranosidase,AXH-d3)

BaAra43A (AXH-d3)

Exo-Gal0153

(EC. 3.2.1.55) exo-α-L-arabinofuranosidase

CAZy Family: GH43

 

PROPERTIES

1. ELECTROPHORETIC PURITY

-Single band on SDS-gel electrophoresis (MW ~59 kDa)

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Figure 1. Electrophoresis analysis of BaAra43A. M, molecular weight marker (PageRuler Prestained Protein Ladder, Thermo Scientific); lane 1, culture lysate before IPTG induction; lane 2, culture lysate after IPTG induction; lane 3, BaAra43A  purified from Ni sepharose fastflow column.

 

2. SPECIFIC ACTIVITY

No activity on pNPαAra. Only C3-linked arabinose residues from double-substituted xylose residues.

 

3. RELATIVE RATES OF HYDROLYSIS OF SUBSTRATES

 

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Figure 2.  A–C High-performance anion-exchange analysis of the reaction products obtained after incubation of the oligosaccharide 6.1 with arabinofuranohydrolase. A Untreated oligosaccharide 6.1; B oligosaccharide 6.1 treated with arabinofuranohydrolase; C standard oligosaccharide 5.4.

 

4. PHYSICOCHEMICAL PROPERTIES

 pH Optima: suggested use 6.0

Temperature Optima: suggested use 30°C

 

5. STORAGE CONDITIONS

The enzyme should be stored at -20°C. For assay, this enzyme should be diluted in phosphate buffer (20 mM) pH 7.0. Swirl to mix the enzyme immediately prior to use.

 

6.  REFERENCES

[1] Van Laere KM, Beldman G, Voragen AG. A new arabinofuranohydrolase from Bifidobacterium adolescentis able to remove arabinosyl residues from double-substituted xylose units in arabinoxylan. Appl Microbiol Biotechnol. 1997 Mar;47(3):231-5.