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EC Tree
IUBMB Comments The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Some beta-galactosidases (EC 3.2.1.23) and beta-D-fucosidases (EC 3.2.1.38) also hydrolyse alpha-L-arabinosides. cf. EC 3.2.1.185, non-reducing end beta-L-arabinofuranosidase.
The taxonomic range for the selected organisms is: Bifidobacterium longum The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
arabinofuranosidase, arabinosidase, alpha-l-araf, alpha-arabinosidase, alpha-l-arabinosidase, afase, alpha-l-arabinofuranosidase b, arabinoxylan arabinofuranohydrolase, alpha-araf, alpha-arabinofuranosidase,
more
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alpha-L-arabinofuranosidase
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alpha-arabinofuranosidase
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alpha-arabinosidase
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alpha-L-arabinanase
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alpha-L-arabinofuranosidase
alpha-L-arabinofuranoside arabinofuranohydrolase
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alpha-L-arabinofuranoside hydrolase
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alpha-L-arabinosidase
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polysaccharide alpha-L-arabinofuranosidase
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additional information
enzyme belongs to the family 51 of glycosidases
alpha-L-arabinofuranosidase
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alpha-L-arabinofuranosidase
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hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
exo-acting enzyme
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hydrolysis of O-glycosyl bond
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alpha-L-arabinofuranoside non-reducing end alpha-L-arabinofuranosidase
The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Some beta-galactosidases (EC 3.2.1.23) and beta-D-fucosidases (EC 3.2.1.38) also hydrolyse alpha-L-arabinosides. cf. EC 3.2.1.185, non-reducing end beta-L-arabinofuranosidase.
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4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
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?
alpha-(1->5)-L-arabinofuranotriose + H2O
alpha-L-arabinofuranose
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?
alpha-L-arabinofuranobiose + H2O
alpha-L-arabinofuranose
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alpha-L-arabinofuranopentaose + H2O
alpha-L-arabinofuranose
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?
alpha-L-arabinofuranoptetraose + H2O
alpha-L-arabinofuranose
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?
arabinan + H2O
alpha-L-arabinose + ?
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arabinoxylan + H2O
alpha-L-arabinose + ?
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4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
100% activity
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arabinan + H2O
L-arabinose + ?
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arabinoxylan + H2O
L-arabinose + ?
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ginsenoside Rc + H2O
ginsenoside Rd + L-arabinofuranose
10.5% activity compared to 4-nitrophenyl alpha-L-arabinofuranoside
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additional information
?
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additional information
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enzyme might have a role in the degradation of L-arabinose-containing polysaccharides together with other glycosidases
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additional information
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substrate specificity, no endoarabinanase activity
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additional information
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activity is subjected to two-seven-fold induction by L-arabinose, D-xylose, L-arabitol and xylitol and to repression by glucose. Maximum activity is obtained at 48 h incubation except for D-xylose that is at 24 h. High concentrations (200 mM) of L-arabitol also caused repression of the arabinofuranosidase
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additional information
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the enzyme does not hydrolyse 4-nitrophenyl alpha-L-arabinopyranoside, 4-nitrophenyl beta-L-arabinopyranoside, 4-nitrophenyl beta-L-arabinofuranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, and ginsenoside Rb2
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additional information
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additional information
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enzyme might have a role in the degradation of L-arabinose-containing polysaccharides together with other glycosidases
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additional information
?
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activity is subjected to two-seven-fold induction by L-arabinose, D-xylose, L-arabitol and xylitol and to repression by glucose. Maximum activity is obtained at 48 h incubation except for D-xylose that is at 24 h. High concentrations (200 mM) of L-arabitol also caused repression of the arabinofuranosidase
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Ca2+
109.4% relative activity at 1 mM
Na+
the enzyme activity is unaffected by NaCl concentration in the range of 0-1 mM
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Ba2+
68% residual activity at 1 mM
Co2+
54.4% residual activity at 1 mM
Cu2+
7% residual activity at 1 mM
Fe2+
81.3% residual activity at 1 mM
Mg2+
80.2% residual activity at 1 mM
Ni2+
85.1% residual activity at 1 mM
additional information
not affected by chelating or reducing agents
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0.295
4-nitrophenyl-alpha-L-arabinofuranoside
pH 6.0, 45°C
0.21
4-nitrophenyl alpha-L-arabinofuranoside
in 50 mM sodium acetate buffer (pH 5.5), at 37°C
1.73
ginsenoside Rc
in 50 mM sodium acetate buffer (pH 5.5), at 37°C
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2.64
crude extract, using 4-nitrophenyl alpha-L-arabinofuranoside as substrate, in 50 mM sodium acetate buffer (pH 5.5), at 37°C
71.36
after 26fold purification, using 4-nitrophenyl alpha-L-arabinofuranoside as substrate, in 50 mM sodium acetate buffer (pH 5.5), at 37°C
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57
when incubated for 15 min at pH 7.0
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SwissProt
brenda
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IABF_BIFLN
566
0
61548
Swiss-Prot
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260000
detagged enzyme, gel filtration
64000
4 * 64000, SDS-PAGE
61260
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mass spectrometry and gel filtration
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tetramer
4 * 64000, SDS-PAGE
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recombinant His-tagged enzyme from Lactococcus lactis by Ni2+-chelate affinity chromatography
Ni2+-charged HiTrap IMAC column chromatography
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DNA and amino acid sequence determination and analysis, overexpression of the C-terminally His-tagged enzyme in Lactococcus lactis NZ9000 under control of nisin-inducible nisA promotor
expressed in Escherichia coli BL21(DE3) cells
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biotechnology
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degradation of lignocellulose, hemicellulose and pectin
food industry
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clarification of fruit juices for wine industry
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Margolles, A.; de los Reyes-Gavillan, C.G.
Purification and functional characterization of a novel alpha-L-arabinofuranosidase from Bifidobacterium longum B667
Appl. Environ. Microbiol.
69
5096-5103
2003
Bifidobacterium longum (Q841V6), Bifidobacterium longum B667 (Q841V6)
brenda
Numan, M.T.; Bhosle, N.B.
alpha-L-Arabinofuranosidases: the potential applications in biotechnology
J. Ind. Microbiol. Biotechnol.
33
247-260
2006
Aspergillus luchuensis, Aspergillus oryzae, Aspergillus oryzae HL15, Bacillus pumilus, Bacillus pumilus PS213, Bifidobacterium longum, Bifidobacterium longum B667, Brevibacillus brevis, Brevibacillus brevis K-110, Cellvibrio japonicus, Clostridium cellulovorans, Fusarium oxysporum f. sp. dianthi, Penicillium chrysogenum, Rhizomucor pusillus, Rhizomucor pusillus HHT1, Streptomyces chartreusis, Streptomyces chartreusis GS901, Streptomyces thermoviolaceus, Streptomyces thermoviolaceus OP-520, Talaromyces purpureogenus, Thermoanaerobacter ethanolicus, Thermoanaerobacter ethanolicus JW 200, Thermobacillus xylanilyticus, Thermobacillus xylanilyticus D3, Thermobifida fusca, Thermomicrobia bacterium PRI-1686, Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
brenda
Gueimonde, M.; Noriega, L.; Margolles, A.; de los Reyes-Gavilan, C.G.
Induction of alpha-L-arabinofuranosidase activity by monomeric carbohydrates in Bifidobacterium longum and ubiquity of encoding genes
Arch. Microbiol.
187
145-153
2007
Bifidobacterium longum, Bifidobacterium longum NIZO B667
brenda
Lee, J.H.; Hyun, Y.J.; Kim, D.H.
Cloning and characterization of alpha-L-arabinofuranosidase and bifunctional alpha-L-arabinopyranosidase/beta-D-galactopyranosidase from Bifidobacterium longum H-1
J. Appl. Microbiol.
111
1097-1107
2011
Bifidobacterium longum (E7CY70), Bifidobacterium longum H-1 (E7CY70)
brenda