Information on EC 3.2.1.99 - arabinan endo-1,5-alpha-L-arabinanase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.1.99
-
RECOMMENDED NAME
GeneOntology No.
arabinan endo-1,5-alpha-L-arabinanase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
-
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
-
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
-
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
also acts slowly on beet-arabinan
-
-
-
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
three catalytic carboxylates: Asp27, the general base, Glu201, the general acid, and Asp147, the pKa modulator, substrate binding structure and catalytic mechanism, overview
B3EYM8
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
Aspergillus niger N400, Aspergillus niger N400(CBS 120-49)
-
-
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
three catalytic carboxylates: Asp27, the general base, Glu201, the general acid, and Asp147, the pKa modulator, substrate binding structure and catalytic mechanism, overview
Geobacillus stearothermophilus T-6
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
5-alpha-L-arabinan 5-alpha-L-arabinanohydrolase
Acts best on linear 1,5-alpha-L-arabinan. Also acts on branched arabinan, but more slowly.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1,5-alpha-arabinanase A
-
exhibits endo- and exo-mode of action
ABN
B3FRL6
-
ABN
Geobacillus thermodenitrificans TS-3
-, AB063312
-
-
Abn1
Chrysosporium lucknowense C1
-
-
-
Abn2
Bacillus subtilis 168T+
B3FRL6
-
-
Abnc
Penicillium chrysogenum 31B
-
-
-
AbnS1
Penicillium chrysogenum 31B
Q5H7M8
-
-
alpha-L-arabinohydrolase
-
-
alpha-L-arabinohydrolase
Chrysosporium lucknowense C1
-
-
-
araban 5-alpha-L-arabinohydrolase
-
-
-
-
arabinanase A
-
exhibits endo- and exo-mode of action
arabinase, endo-1,5-alpha-L-
-
-
-
-
Arb43A
B3FRL6
isoform, formally named AbnA
Arb43B
B3FRL6
isoform, formally named Abn2
arbA
-
exhibits endo- and exo-mode of action
cold-adapted endo-arabinanase
-
-
cold-adapted endo-arabinanase
Penicillium chrysogenum 31B
-
-
-
endo-(1->5)-alpha-L-arabinanase
-
-
-
-
endo-1,5-alpha-arabinanase
-
-
-
-
endo-1,5-alpha-arabinanase
B3FRL6
-
endo-1,5-alpha-L-arabinanase
-
-
-
-
endo-1,5-alpha-L-arabinanase
-
-
endo-1,5-alpha-L-arabinanase
B3FRL6
-
endo-1,5-alpha-L-arabinanase
-
-
endo-1,5-alpha-L-arabinanase
A4XJR7
-
endo-1,5-alpha-L-arabinanase
-
-
endo-1,5-alpha-L-arabinanase
Geobacillus thermodenitrificans TS-3
-
;
-
endo-1,5-alpha-L-arabinanase
-
-
endo-1,5-alpha-L-arabinanase
A5IKD4
-
endo-1,5-alpha-L-arabinase
-
-
-
-
endo-1,5-alpha-L-arabinase A
-
-
endo-alpha-(1->5)-L-arabinanase
-
-
-
-
endo-alpha-1,5-arabanase
-
-
-
-
endo-alpha-1,5-L-arabinanase
B3FRL6
-
endo-alpha-1,5-L-arabinanase
Bacillus subtilis 168T+
B3FRL6
-
-
endo-alpha-arabinanase
-
-
endo-ara
-
-
endo-arabanase
-
-
-
-
endo-arabinanase
-
-
-
-
endo-arabinase
-
-
-
-
endo-arabinase
-
-
endo-arabinase
Q5H7M8
-
endo-arabinase
Penicillium chrysogenum 31B
Q5H7M8
-
-
endo-L-arabinanase
-
-
-
-
endoarabinanase
-
-
endoarabinanase
Chrysosporium lucknowense C1
-
-
-
endoarabinase
-
-
-
-
GH43 arabinanase
B3FRL6
-
PPase-C
-
IFO 3134
protopectinase C
-
IFO 3134
protopectinase-C
-
IFO 3134
GH43 arabinanase
Bacillus subtilis 168T+
B3FRL6
-
-
additional information
B3EYM8
the enzyme belongs to the glycoside hydrolase family 43, GH43
additional information
Geobacillus stearothermophilus T-6
B3EYM8
the enzyme belongs to the glycoside hydrolase family 43, GH43
-
additional information
-
the enzyme belongs to the glycoside hydrolase family 43, GH43
CAS REGISTRY NUMBER
COMMENTARY
75432-96-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
creA mutant, mutant relieved of carbon repression
-
-
Manually annotated by BRENDA team
wild-type N400 and mutant N572, lacks xylulose kinase activity
-
-
Manually annotated by BRENDA team
wild-type N402 and mutant N572, xylulose kinase negative mutant
-
-
Manually annotated by BRENDA team
Aspergillus niger N400
N400
-
-
Manually annotated by BRENDA team
-
B3FRL6
UniProt
Manually annotated by BRENDA team
F-11; IFO 3022
-
-
Manually annotated by BRENDA team
IFO 3022
-
-
Manually annotated by BRENDA team
IFO 3022; IFO 3134
-
-
Manually annotated by BRENDA team
IFO 3134
-
-
Manually annotated by BRENDA team
strain 168T+
B3FRL6
UniProt
Manually annotated by BRENDA team
Bacillus subtilis 168T+
strain 168T+
B3FRL6
UniProt
Manually annotated by BRENDA team
Bacillus subtilis F-11
F-11
-
-
Manually annotated by BRENDA team
Chrysosporium lucknowense C1
-
-
-
Manually annotated by BRENDA team
Clostridium felsineum var. sikokianum
-
-
-
Manually annotated by BRENDA team
wild-type WG096
-
-
Manually annotated by BRENDA team
wild-type WG096 and cre mutant, carbon catabolite derepressed mutant
-
-
Manually annotated by BRENDA team
strain T-6, gene abnB
UniProt
Manually annotated by BRENDA team
Geobacillus stearothermophilus T-6
strain T-6, gene abnB
UniProt
Manually annotated by BRENDA team
strain TS-3
AB063312
GenBank
Manually annotated by BRENDA team
Geobacillus thermodenitrificans TS-3
strain TS-3
AB063312
GenBank
Manually annotated by BRENDA team
Geobacillus thermodenitrificans TS-3
strain TS-3
-
-
Manually annotated by BRENDA team
Penicillium chrysogenum 31B
-
-
-
Manually annotated by BRENDA team
Penicillium chrysogenum 31B
-
UniProt
Manually annotated by BRENDA team
arabinanase A, exhibits endo- and exo-mode of action; subspecies cellulosa
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1->5)-L-alphaarabinan + H2O
(1->5)-L-arabinooligosaccharides
show the reaction diagram
A5IKD4, -
-
-
-
?
1,5-alpha-arabinan + H2O
?
show the reaction diagram
Chrysosporium lucknowense, Chrysosporium lucknowense C1
-
-
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
-
-
-
-
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
-
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
-
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
-
product formation, overview: oligoarabinosides with degree of polymerization between 2 and 5 are the major products, but only trace amounts of free arabinose
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
-
major final end-products, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
-
action patterns of initial hydrolysis products
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
best substrate, endo mechanism
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
best substrate, endo mechanism
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
best substrate, endo mechanism
major final end-products, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
best substrate, endo mechanism
action patterns of initial hydrolysis products
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
best substrate, endo mechanism
product formation, overview
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
best substrate: linear 1,5-alpha-L-haze arabinan
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
i.e. debranched arabinan
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
AB063312, -
i.e. debranched arabinan
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
Geobacillus thermodenitrificans TS-3
AB063312
i.e. debranched arabinan
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
-
-
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
-
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
-
F-11 and IFO 3022: best substrate, endo mechanism
end-product
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
-
F-11 best substrate
end-product, F-11: releases arabinose, arabinobiose, arabinotriose and higher oligosaccharides during hydrolysis, end-product are arabinose and arabinobiose
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
-
IFO 3134, linear 1,5-alpha-L-arabinan
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
Bacillus subtilis F-11
-
-
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
Bacillus subtilis F-11
-
F-11 and IFO 3022: best substrate, endo mechanism
end-product
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
Bacillus subtilis F-11
-
F-11 best substrate
end-product, F-11: releases arabinose, arabinobiose, arabinotriose and higher oligosaccharides during hydrolysis, end-product are arabinose and arabinobiose
?
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
F-11 and IFO 3022: best substrate, endo mechanism
-
-
?
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
F-11 best substrate
-
-
?
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
IFO 3022, best substrate
IFO 3022
?
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
Bacillus subtilis F-11
-
F-11 and IFO 3022: best substrate, endo mechanism
-
-
?
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
Bacillus subtilis F-11
-
F-11 best substrate
-
-
?
1,5-alpha-L-arabinan + H2O
L-arabinan oligomers
show the reaction diagram
-
-
-
-
-
1,5-alpha-L-arabinan + H2O
L-arabinan oligomers
show the reaction diagram
-
-
-
ir
1,5-alpha-L-arabinan + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
linear arabinan
main product
?
1,5-alpha-L-arabinan + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
linear arabinan
main product
?
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
-
-
-
-
-
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
B3FRL6
Abn2, together with previously characterized AbnA, is responsible for the majority of the extracellular arabinan activity in Bacillus subtilis. Abn2 is monocistronic, and its expression is driven from two different promoters
-
-
?
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
A4XJR7
debranched arabinan, best substrate
-
-
?
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
Bacillus subtilis 168T+
B3FRL6
Abn2, together with previously characterized AbnA, is responsible for the majority of the extracellular arabinan activity in Bacillus subtilis. Abn2 is monocistronic, and its expression is driven from two different promoters
-
-
?
1,5-arabinan + H2O
L-arabinose + ?
show the reaction diagram
Geobacillus thermodenitrificans, Geobacillus thermodenitrificans TS-3
-
-
-
-
?
1,5-L-alpha-arabinoheptaose + H2O
1,5-L-alpha-arabinotriose + 1,5-L-alpha-arabinotetraose
show the reaction diagram
Chrysosporium lucknowense, Chrysosporium lucknowense C1
-
-
-
-
?
1,5-L-alpha-arabinopentaose + H2O
1,5-L-alpha-arabinotriose + 1,5-L-alpha-arabinobiose
show the reaction diagram
Chrysosporium lucknowense, Chrysosporium lucknowense C1
-
-
-
-
?
1,5-L-alpha-arabinotetraose + H2O
1,5-L-alpha-arabinobiose + 1,5-L-alpha-arabinobiose
show the reaction diagram
Chrysosporium lucknowense, Chrysosporium lucknowense C1
-
-
-
-
?
1,5-L-alpha-arabinotriose + H2O
L-arabinose + 1,5-L-alpha-arabinobiose
show the reaction diagram
Chrysosporium lucknowense, Chrysosporium lucknowense C1
-
-
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
very poor substrate
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
poor substrate
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
poor substrate
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
mild hydrolysis: no significant degradation, exhaustive enzymatic hydrolysis: extremely low degradation, DP3
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
poor substrate
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
DP4
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, product formation, intermediate enzymatic hydrolysis: L-arabinobiose and much less L-arabinose + L-arabinotriose, end-products after exhaustive enzymatic degradation
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranose
show the reaction diagram
-
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
-
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
DP5
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, product formation, end-products after exhaustive enzymatic degradation, intermediate enzymatic hydrolysis: L-arabinobiose + L-arabinotriose
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
DP6
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, product formation, end-products after exhaustive enzymatic degradation, intermediate enzymatic hydrolysis: L-arabinobiose + L-arabinotetraose and L-arabinotriose
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
DP7
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, product formation, end-products after exhaustive enzymatic degradation, intermediate enzymatic hydrolysis: L-arabinotriose + L-arabinotetraose
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
-
-
-
-
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
show the reaction diagram
-
DP8
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, product formation, end-products after exhaustive enzymatic degradation, intermediate enzymatic hydrolysis: L-arabinotriose + L-arabinopentaose and L-arabinobiose + L-arabinohexaose and L-arabinotetraose
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
-
-
?
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + H2O
L-arabinose
show the reaction diagram
-
not a substrate
-
-
-
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + H2O
L-arabinose
show the reaction diagram
-
at very low rate, with high enzyme concentration
-
?
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + H2O
L-arabinose
show the reaction diagram
-
no or extremely low degradation, DP2
-
-
?
apple pectin + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis 168T+
B3FRL6
-
-
-
?
arabinan + H2O
?
show the reaction diagram
AB063312, -
-
-
-
-
arabinan + H2O
?
show the reaction diagram
Geobacillus thermodenitrificans TS-3
AB063312
-
-
-
-
arabinogalactan + H2O
?
show the reaction diagram
-
-
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
very poor substrate
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
for optimal breakdown of potato arabinogalactan combined action of endo-arabinase and endo-galactanase is required
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
onion arabinogalactan: not a substrate
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
potato arabinogalactan
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
potato arabinogalactan
-
-
?
carboxymethylarabinan + H2O
?
show the reaction diagram
-
-
-
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
-
-
-
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
-
F-11, primary cell wall polysaccharides
-
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
-
F-11, sycamore
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
-
F-11, sycamore
-
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
Bacillus subtilis F-11
-
F-11, primary cell wall polysaccharides, F-11, sycamore
-
-
?
cell wall polysaccharide + H2O
arabinose + galactose + rhamnose + fucose
show the reaction diagram
-
F-11, apple
F-11, 34.3% arabinose + 10% galactose + 2.6% rhamnose/fucose
?
CM-cellulose + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
debranched (1->5)-L-arabinan + H2O
L-arabinose
show the reaction diagram
-
under the optimum conditions, 16 g/l L-arabinose is obtained from 20 g/l debranched arabinan with a hydrolysis yield of 80%
-
-
?
feruloylated oligosaccharide + H2O
ferulic acid + ?
show the reaction diagram
-
from sugar beet pulp, SBP
efficient releasing free ferulic acid from sugar beet pulp requires strong synergy involving three enzymes: endo-arabinanase, alpha-L-arabinofuranosidase and cinnamoyl esterase, free and esterified ferulic acid
?
feruloylated oligosaccharide + H2O
ferulic acid + ?
show the reaction diagram
-
endo-arabinanase alone: very poor substrate, endo-arabinanase and alpha-L-arabinofuranosidase together: good substrate, best: combination endo-arabinanase, alpha-L-arabinofuranosidase and cinnamoyl esterase
efficient releasing free ferulic acid from sugar beet pulp requires strong synergy involving three enzymes: endo-arabinanase, alpha-L-arabinofuranosidase and cinnamoyl esterase, free and esterified ferulic acid
?
galactan + H2O
?
show the reaction diagram
-
very poor substrate
-
-
?
galactan + H2O
?
show the reaction diagram
-
not a substrate
-
-
-
galactan + H2O
?
show the reaction diagram
-
potato galactan: poor substrate, citrus galactan: very poor substrate
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
-
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
-
main product: L-arabinotriose
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
linear arabinan
main product: L-arabinotriose
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
apple juice ultrafiltration retentate arabinan, branched sugar-beet arabinan, linear apple arabinan
end-product: low molecular weight oligomeric products
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
beet and apple juice ultrafiltration retentate, UFR, arabinan
end-product: L-arabinose disaccharide + L-arabinose trisaccharide, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
apple and sugar beet pulp
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
branched and partially debranched arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
end-product: L-arabinose disaccharide + L-arabinose trisaccharide, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
branched sugar beet arabinan containing alpha-1,3-arabinose side chains: not a substrate
main product: L-arabinotriose
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar-beet arabinan in commercial apple juice concentrate, beet arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
beet arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
debranched and branched sugar beet arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
linear and branched arabinan
end-product: low molecular weight oligomeric products
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
random hydrolysis of L-arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
random hydrolysis of L-arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
random hydrolysis of L-arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Clostridium felsineum var. sikokianum
-
random hydrolysis of L-arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
random hydrolysis of L-arabinan
end-product: L-arabinose disaccharide + L-arabinose trisaccharide, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
debranched arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Aspergillus niger N400
-
sugar beet pulp
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Bacillus subtilis F-11
-
sugar-beet arabinan in commercial apple juice concentrate, beet arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Bacillus subtilis F-11
-
beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Bacillus subtilis F-11
-
beet arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Bacillus subtilis F-11
-
branched and partially debranched arabinan, beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Aspergillus niger N400(CBS 120-49)
-
sugar beet pulp
-
-
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
-
-
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
-
main product: L-arabinotriose
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
-
product formation
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
-
small oligomeric products
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
degree of polymerization 2-8, DP2-8
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, L-arabinose + L-arabinobiose: end-products after exhaustive enzymatic degradation, product formation
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
linear 1,5-alpha-L-arabino-oligosaccharide
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, L-arabinose + L-arabinobiose: end-products after exhaustive enzymatic degradation, product formation
?
linear 1,5-alpha-L-arabinan + H2O
L-arabinose + ?
show the reaction diagram
-
-
-
-
?
protopectin + H2O
pectin
show the reaction diagram
-
IFO 3134, protopectin of sugar beet pulp and various citrus fruit peels, but much less on that from lemon peel
IFO 3134, highly polymerized pectin
?
protopectin + H2O
pectin
show the reaction diagram
-
IFO 3134, protopectin of sugar-beet and apple pulp
IFO 3134, soluble pectin
?
red debranched arabinan + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis 168T+
B3FRL6
-
-
-
?
reduced arabinohexaose + H2O
arabinotriose + reduced arabinotriose
show the reaction diagram
-
the enzyme hydrolyzes a branched arabinohexaose with a double substituted arabinose at subsite-2
-
-
?
sugar beet arabinan + H2O
L-arabinose + ?
show the reaction diagram
-
-
-
-
?
sugar beet arabinan + H2O
?
show the reaction diagram
B3FRL6
-
-
-
?
sugar beet arabinan + H2O
?
show the reaction diagram
A4XJR7
the substrate is composed of 1,2-alpha- and 1,3-alpha-L-arabinofuranosyl side chains linked to a 1,5-alpha-L-arabinofuranosyl backbone
-
-
?
sugar beet arabinan + H2O
?
show the reaction diagram
Bacillus subtilis 168T+
B3FRL6
-
-
-
?
linear arabinan + H2O
?
show the reaction diagram
Geobacillus stearothermophilus, Geobacillus stearothermophilus T-6
B3EYM8
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
-
substrate binding site, action pattern, subsite mapping
-
-
-
additional information
?
-
-
no bi-substrate reactions such as condensation or transglycosylation
-
-
-
additional information
?
-
-
IFO 3022: potato disc macerating activity, able to loosen potato tissue
-
-
-
additional information
?
-
-
inactive on p-nitrophenyl-alpha-L-arabinofuranoside
-
-
-
additional information
?
-
-
inactive on p-nitrophenylarabinofuranoside, onion arabinogalactan, stractan, wheat arabinoxylan, oat spelts arabinoxylan, avicel, polygalacturonic acid
-
-
-
additional information
?
-
-
IFO 3022: inactive on p-nitrophenyl alpha-L-arabinofuranoside, p-nitrophenyl alpha-D-galactopyranoside, p-nitrophenyl beta-D-galactopyranoside, arabinogalactan, carboxymethyl cellulose, filter paper, pectin and polygalacturonic acid
-
-
-
additional information
?
-
-
F-11: inactive on phenyl alpha-L-arabinofuranoside, p-nitrophenyl alpha-D-galactopyranoside, p-nitrophenyl beta-D-galactopyranoside, arabinoxylan, arabinogalactan and gum arabic
-
-
-
additional information
?
-
-
product specificity, overview
-
-
-
additional information
?
-
-
product specificity, overview
-
-
-
additional information
?
-
-
inactive on arabinobiitol
-
-
-
additional information
?
-
-
IFO 3134, inactive on polygalacturonic acid and soluble pectin
-
-
-
additional information
?
-
-
F-11, substrate specificity
-
-
-
additional information
?
-
-
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times
-
-
-
additional information
?
-
-
inactive towards synthetic arabinosides, p-nitrophenyl-alpha-L-arabinoside, arabinose disaccharide, arabinogalactan, stractan and xylan from oat spelts
-
-
-
additional information
?
-
-
inactive towards phenyl and p-nitrophenyl alpha-L-arabinofuranoside, arabinoxylan, arabinogalactan, and gum arabic
-
-
-
additional information
?
-
-
F-11, inactive on potato galactan
-
-
-
additional information
?
-
-
inactive on cellulose, avicel, amorphous cellulose, carboxymethylcellulose, xylan, galactan, mannan, 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl alpha-L-arabinopyranoside, 4-nitrophenyl beta-xyloside and 2,4-dinitrophenyl beta-xylobioside
-
-
-
additional information
?
-
-
plays a role in degradation of plant tissues, macerating enzyme
-
-
-
additional information
?
-
AB063312, -
no substrates: carboxymethyl cellulose, xylan, polygalacturonate, pectin, galactan, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside,4-nitrophenyl-alpha-D-xylopyranoside and 4-nitrophenyl-beta-D-cellobioside
-
-
-
additional information
?
-
-
alkali extract of cell walls of Gossypium hirsutum is sequentially digested by endo-polygalacturonase, arabinofuranosidase, endo-arabinase, and rhamnogalacturonan hydrolase AN9314.2
-
-
-
additional information
?
-
B3FRL6
shows no activity toward larchwood arabinogalactan, wheat arabinoxylan, and p-nitrophenyl-alpha-L-arabinofuranoside
-
-
-
additional information
?
-
-
the enzyme shows the ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides
-
-
-
additional information
?
-
A4XJR7
no activity for arabinoxylan, 1,4-beta-D-xylose units with side chains of 1,3-alpha-L-arabinose, xylan, starch, or 4-nitrophenyl-alpha-L-arabinofuranoside, a typical substrate for the arabinofuranosidase. Synergistic hydroysis of arabinan by endo-1,5-alpha-L-arabinanase and alpha-L-arabinofuranosidase
-
-
-
additional information
?
-
A5IKD4, -
the enzyme acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan
-
-
-
additional information
?
-
Bacillus subtilis 168T+
B3FRL6
shows no activity toward larchwood arabinogalactan, wheat arabinoxylan, and p-nitrophenyl-alpha-L-arabinofuranoside
-
-
-
additional information
?
-
Geobacillus thermodenitrificans TS-3
AB063312
no substrates: carboxymethyl cellulose, xylan, polygalacturonate, pectin, galactan, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside,4-nitrophenyl-alpha-D-xylopyranoside and 4-nitrophenyl-beta-D-cellobioside
-
-
-
additional information
?
-
Bacillus subtilis F-11
-
F-11, inactive on potato galactan
-
-
-
additional information
?
-
Bacillus subtilis F-11
-
IFO 3022: potato disc macerating activity, able to loosen potato tissue, inactive towards phenyl and p-nitrophenyl alpha-L-arabinofuranoside, arabinoxylan, arabinogalactan, and gum arabic
-
-
-
additional information
?
-
Bacillus subtilis F-11
-
F-11: inactive on phenyl alpha-L-arabinofuranoside, p-nitrophenyl alpha-D-galactopyranoside, p-nitrophenyl beta-D-galactopyranoside, arabinoxylan, arabinogalactan and gum arabic
-
-
-
additional information
?
-
Bacillus subtilis F-11
-
F-11, substrate specificity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
plays a role in degradation of plant tissues, macerating enzyme
-
-
-
additional information
?
-
-
the enzyme shows the ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(NH4)2HPO4
-
IFO 3134, stimulation of enzyme production and activity
(NH4)H2PO4
-
IFO 3134, stimulation of enzyme production and activity
BaCl2
-
IFO 3134, slight activation
Ca2+
-
isoform Arb43B possesses a cluster containing a calcium ion in the catalytic domain
CaCl2
-
IFO 3134, slight activation
CoCl2
-
IFO 3134, very slight activation
Hg2Cl2
-
IFO 3134, slight activation
K2HPO4
-
IFO 3134, stimulation of enzyme production and activity
KH2PO4
-
IFO 3134, stimulation of enzyme production and activity
Na2HPO4
-
IFO 3134, stimulation of enzyme production and activity
NaH2PO4
-
IFO 3134, stimulation of enzyme production and activity
MgCl2
-
IFO 3134, activation
additional information
-
F-11, no divalent cation requirement
additional information
-
IFO 3134, stimulation of enzyme production by several phosphates, but not by chloride, acetate or sulfate
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
IFO 3134, slight inhibition
Ag2+
AB063312, -
complete inhibition at 1 mM
AgNO3
-
IFO 3134
branched arabinofuranosides
-
-
-
CdCl2
-
IFO 3134
CH3COO- NH4+
-
IFO 3134, complete inhibition of enzyme production
CH3COONa
-
IFO 3134, inhibition of enzyme production
EGTA
-
isoform Arb43B shows a drastic decrease in the activity of the enzyme in the presence of 1 mm EGTA
Fe2(SO4)3
-
IFO 3134
Fe2+
-
IFO 3022
-
Fe3+
-
IFO 3022
-
Hg2+
-
IFO 3022, completely
Hg2+
-
completely
Hg2+
-
IFO 3134, completely
Hg2+
AB063312, -
complete inhibition at 1 mM
HgCl2
-
completely
HgCl2
-
IFO 3134, completely
iodoacetamide
-
very slight inhibition
MgSO4
-
very slight inhibition
Mn2+
-
IFO 3134, completely
NaN3
-
IFO 3134, slight inhibition
NaNO2
-
IFO 3134, strong inhibition
o-phenanthroline
-
IFO 3134, slight inhibition
p-chloromercuribenzoate
-
IFO 3134, slight inhibition
PbCl2
-
IFO 3134
Sn2+
-
IFO 3134, strong inhibition
SnCl2
-
IFO 3134, strong inhibition
MnCl2
-
IFO 3134, completely
additional information
-
IFO 3022: no inhibition by L-arabonic-gamma-lactone, D- and L-galactonic-gamma-lactones
-
additional information
-
no inhibition by CaCl2, EDTA, L-arabono-gamma-lactone, L-arabinose, D-arabitol
-
additional information
-
IFO 3134, inhibition of enzyme production
-
additional information
-
-
-
additional information
AB063312, -
no inhibition by Ba2+, Mn2+ and Mg2+
-
additional information
B3FRL6
expression of abn2 is repressed by glucose. Glucose causes a 17- and 44fold repression of the abn2'-lacZ fusion expression during the exponential growth phase and the early postexponential phase, respectively
-
additional information
-
Abn1 is not inhibited by arabinobiose in the degradation of linear arabinan even when 50 mg/ml arabinobiose are added
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
apple pulp
-
induction of endo-arabinase and activation
-
L-arabinose
-
induction of endo-arabinase, addition of D-glucose prevents this induction
L-arabinose
-
induction of endo-arabinase, addition of D-glucose prevents this induction
L-Arabitol
-
induction of endo-arabinase, addition of D-glucose prevents this induction
L-Arabitol
-
induction of endo-arabinase, addition of D-glucose prevents this induction
sugar beet pulp
-
induction of endo-arabinase and activation
-
sugar beet pulp
-
induction of endo-arabinase and activation
-
additional information
B3FRL6
expression of abn2 is stimulated by arabinan and pectin, arabinose is not the natural inducer. EDTA does not affect the activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.052
-
1,5-Alpha-L-arabinan
-
CM-linear 1,5-alpha-L-arabinan
0.336
-
1,5-Alpha-L-arabinan
-
CM-linear 1,5-alpha-L-arabinan
4.2
-
1,5-Alpha-L-arabinan
-
-
0.388
-
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
-
-
0.592
-
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
-
-
9.3
-
L-arabinan
-
apple juice ultrafiltration retentate, UFR, arabinan, linearised
-
26
-
L-arabinan
-
apple juice ultrafiltration retentate, UFR, arabinan
-
0.076
-
linear 1,5-alpha-L-arabinan
-
mutant H318A of isoform Arb43B, pH and temperature not specified in the publication
0.111
-
linear 1,5-alpha-L-arabinan
-
wild type isoform Arb43B, pH and temperature not specified in the publication
5.92
-
linear 1,5-alpha-L-arabinan
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic data and mechanism
-
additional information
-
additional information
-
kinetic data
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic data
-
additional information
-
additional information
-
kinetic data
-
additional information
-
additional information
AB063312, -
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
50
-
1,5-Alpha-L-arabinan
A4XJR7
recombinant enzyme, pH 6.5, 75C
3.1
-
linear 1,5-alpha-L-arabinan
-
mutant H318A of isoform Arb43B, pH and temperature not specified in the publication
191.6
-
linear 1,5-alpha-L-arabinan
-
wild type isoform Arb43B, pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4e-05
-
linear 1,5-alpha-L-arabinan
-
mutant H318A of isoform Arb43B, pH and temperature not specified in the publication
227797
0.00172
-
linear 1,5-alpha-L-arabinan
-
wild type isoform Arb43B, pH and temperature not specified in the publication
227797
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.36
-
-
apple juice ultrafiltration retentate, UFR, arabinan
1.2
-
-
best substrate: 1,5-alpha-L-arabinan
2.6
-
A4XJR7
purified recombinant enzyme, substrate is sugar beet arabinan
5.8
-
-
IFO 3134
7.78
-
-
IFO 3022
12
-
A4XJR7
purified recombinant enzyme, substrate 1,5-alpha-L-arabinan
14
-
-
substrate: branched sugar beet arabinan
26
-
-
using linear arabinan as substrate, pH and temperature not specified in the publication
46.5
-
-
F-11
48.8
-
-
F-11
81.1
-
-
substrate: debranched sugar beet arabinan
90.2
-
-
best substrate: linear 1,5-alpha-L-arabinan
116
-
-
sugar beet arabinan, at 37C, pH 6.6
152.1
-
A5IKD4, -
purified protein, using L-arabinan as substrate, at pH 6.0 and 70C
366
-
-
linear 1,5-alpha-L-arabinan, at 37C, pH 6.6
429
-
-
F-11
additional information
-
-
-
additional information
-
-
no detectable activity against larch wood arabinoxylan, wheat arabinoxylan or p-nitrophenyl-alpha-L-arabinofuranoside
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.6
-
-
maximum, pH optimum is quite broad
4.8
-
-
maximum
6
-
-
F-11; IFO 3022
6
-
-
IFO 3022
6
-
-
IFO 3134
6
-
-
IFO 3134, at 37C
6
-
-
at 37C
6
-
-
mutant enzyme DELTAV2-W17
6
-
A5IKD4, -
-
6
-
-
using sugar beet arabinan as substrate
6.5
-
-
using debranched arabinan as substrate
7
-
B3FRL6
-
8
-
-
IFO 3134, at 60C
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
9
-
IFO 3022
4
10
-
IFO 3134
4
7
A5IKD4, -
the enzyme retains more than 75% activity over a pH range from 4.0 to 7.0
5
8
-, Q5H7M8
arabinanase activity drops to about 55% and 70% of the highest activity at pH 5.0 and 8.0, respectively
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
B3EYM8
assay at
50
-
B3FRL6
-
60
-
-
IFO 3134
60
-
-
at pH 6.6
70
-
-
mutant enzyme DELTAV2-W17
73
-
A5IKD4, -
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
80
-
IFO 3134, activity between
62
80
A5IKD4, -
the enzyme shows relative activity ranging from 77% to 78% at temperatures of 62C and 80C, respectively
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
AB063312, -
isoelectric focusing, pH gradient 3-10
4.9
-
-
calculated from amino acid sequence
7.37
-
B3FRL6
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Aspergillus niger N400, Aspergillus niger N400(CBS 120-49)
-
-
-
Manually annotated by BRENDA team
Bacillus subtilis F-11
-
F-11; F-11
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Aspergillus niger N400, Aspergillus niger N400(CBS 120-49)
-
-
-
-
Manually annotated by BRENDA team
Bacillus subtilis F-11
-
F-11
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27000
-
-
3134, gel filtration on Toyopearl HW-55S
27000
-
-, Q5H7M8
gel filtration
30000
-
-
IFO 3134, SDS-PAGE
31000
-
-
SDS-PAGE
32000
-
-
F-11, SDS-PAGE
32500
-
-
calculated from nucleotide sequence
33000
-
-
IFO 3022, SDS-PAGE
33900
-
-
MALDI-TOF-MS
34000
-
-
SDS-PAGE
35000
-
-
SDS-PAGE
35000
-
AB063312, -
SDS-PAGE
35280
-
-
calculated from amino acid sequence
35710
-
-
IFO 3134, calculated from nucleotide sequence
36000
-
-
F-11, gel filtration
39440
-
-
calculated from nucleotide sequence
40000
-
-
SDS-PAGE
41000
-
-
gel filtration
42500
-
-
SDS-PAGE
43000
-
-
SDS-PAGE
52380
-
B3FRL6
sequence analysis
112000
-
A4XJR7
recombinant His-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 33000, mutant enzyme DELTAV2-W17, SDS-PAGE
?
Geobacillus thermodenitrificans TS-3
-
x * 33000, mutant enzyme DELTAV2-W17, SDS-PAGE
-
dimer
A4XJR7
2 * 56000, recombinant His-tagged enzyme, SDS-PAGE, 2 x 56268, sequence calculation
monomer
-
F-11, 1 * 32000, SDS-PAGE
monomer
-
IFO 3134, 1 * 30000, SDS-PAGE
monomer
-, Q5H7M8
1 * 31000, SDS-PAGE
monomer
A5IKD4, -
1 * 49000, small angle X-ray scattering
monomer
Bacillus subtilis F-11
-
F-11, 1 * 32000, SDS-PAGE
-
monomer
Penicillium chrysogenum 31B
-
1 * 31000, SDS-PAGE
-
additional information
A4XJR7
structure modelling and analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
-
O-linked glycosylation: approximately 10000 Da
additional information
-, Q5H7M8
no glycoprotein
additional information
Penicillium chrysogenum 31B
-
no glycoprotein
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native and seleno-methionine-labelled derivative, by sitting-drop vapour-diffusion method, to 1.9 and 2.7 A resolution, respectively. Native protein crystals appear in two different space groups, P1, with unit-cell parameters a=51.9, b=57.6, c=86.2 A, alpha=82.3, beta=87.9, gamma=63.6, and P212121, with unit-cell parameters a=57.9, b=163.3, c=202.0 A. The selenol-methionine-labelled derivative of Abn2 only crystallizes in one crystal form, which is similar to the form of space group P212121 of the wild-type protein, with unit-cell parameters a=57.84, b=163.22, c=201.85 A, which can accommodate four molecules (each containing 13 selenomethionine residues) in the asymmetric unit
-
sitting drop vapor diffusion method, using 65% (w/v) 2-methyl-2,4-pentadiol and 100 mM Tris, pH 8.5
-
purified recombinant wild-type enzyme, and mutant enzyme E201A in complex with arabinotriose, hanging drop vapour diffusion, 0.0025-0.003 ml of protein solution with 6.5-13 mg/ml protein is mixed with an equal volume of precipitant solution containing 1.7 M lithium sulfate, 0.1 M Tris buffer, pH 7.5, and 15% v/v glycerol for the wild-type enzyme, and 1.9 M lithium sulfate, 0.1 M Tris buffer, pH 8.5, and 4% w/v PEG 400 for the mutant enzyme, X-ray diffraction structure determination and analysis, molecular replacement
B3EYM8
hanging drop vapour-diffusion
-
hanging-drop vapor-diffusion method using 1.0 mM sodium citrate as a precipitant at pH 6.0. Structure determined at 1.9 A to an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule has a five-bladed beta-propeller fold. Crystals belong to orthorhombic space group P2(1)2(1)2(1) with unit cell parameters of a = 40.3, b = 77.8 and c = 89.7 A
-
preliminary x-ray analysis; resolution limit of 3.5 A
-
purified recombinant His-tagged enzyme, 0.0005 ml of protein solution containing 30 mg/ml in 25 mM Tris-HCl buffer, pH 7, 5, is mixed with 0.0005 ml of reservoir solution containing 0.1 M MES buffer, pH 6.5, 0.8 M ammonium sulfate, 0.1 M EDTA, 0.1 M L-proline and 5% v/v dioxane, X-ray diffraction structure determination and analysis at 2.86 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
8
-
85% activity retained between, 67 h at 25C
5
9
-
IFO 3134, stable between at 50C: 30 min
5.5
6.3
-
stable between
6
11
AB063312, -
quite stable at 37C for 16 h
7
10
-
F-11, stable between
9
-
-
F-11, most stable at
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
long incubation times, 26.5 h, at 40C: 90% activity retained
45
-
-
up to 45C: more than 95% activity retained for 3 h
50
60
-, Q5H7M8
the enzyme maintains 100% of the initial activity by treatment it at 50C for 1 h, while approximately 70% of the activity is lost at 60C
50
-
-
up to, full retention of activity, sharp drop in activity beyond 50C
50
-
B3FRL6
remains fully active after 30 min of preincubation at 50C. After preincubation at 60C, the residual activity is only 15%
60
-
-
IFO 3134, up to, retains more than 80% of activity after 10 min
60
-
-
mutant enzyme DELTAV2-W17 loses 65% of its activity after 4 h, half-life: 2.5 h
65
-
-
mutant enzyme DELTAV2-W17, 70% loss of activity after 5 min
65
-
A4XJR7
purified recombinant His-tagged enzyme, half-life is 2440 h
70
-
-
stable for 30 min
70
-
-
wild-type enzyme retains more than 80% of its activity after 4 h, complete loss of activity of mutant enzyme DELTAV2-W17 after 5 min
70
-
A4XJR7
purified recombinant His-tagged enzyme, half-life is 254 h
75
-
AB063312, -
half-life: 4 h
75
-
-
half-life of wild-type enzyme: 4 h
75
-
A4XJR7
purified recombinant His-tagged enzyme, half-life is 93 h
90
95
A5IKD4, -
the enzyme is fully heat-stable (up to 10 h) and retains activity at temperatures up to 90C. The enzyme loses its activity only after 90 min when incubated at 95C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
IFO 3134, EDTA stabilizes during purification
-
IFO 3134, enzyme stable against protease secreted by the microorganism even during 2 days cultivation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 10 mM sodium acetate or piperazine buffer, pH 5.0 dispensed in small tubes
-
-80C, 20 mM Na-phosphate buffer, pH 7.4, 50 mM NaCl, 10% glycerol
B3FRL6
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by fast protein liquid chromatography, FPLC
-
wild-type N400
-
by gel filtration, more than 95% pure
B3FRL6
F-11; IFO 3022
-
His-Trap column chromatography
-
Ni-NTA agarose affinity chromatography
-
wild-type and selenol-methionine-labelled protein purified on nickel column, more than 95% pure
-
His-Trap column chromatography, gel filtration
-
recombinant His-tagged enzyme 39fold from Escherichia coli by nickel affinity chromatography
A4XJR7
recombinant wild-type and mutant enzymes
B3EYM8
hydrophobic chromatography, anion-exchange chromatography, gel filtration chromatography
-
CM-Toyopearl 650 M column chromatography, Ni Sepharose 6 column chromatography, butyl-Toyopearl column chromatography, and Superdex 75 gel filtration; CM-Toyopearl 650 M column chromatography, Ni Sepharose 6 column chromatography, butyl-Toyopearl column chromatography, and Superdex 75 gel filtration
-, Q5H7M8
recombinant arabinanase
-
Ni2+-chelating affinity column chromatography and Superdex 75 gel filtration
A5IKD4, -
recombinant His-tagged enzyme from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cDNA clone, overexpression in Aspergillus niger and Aspergillus nidulans
-
Abn2 overexpressed in Escherichia coli BL21(DE3) pLysS harboring pZI39
B3FRL6
expressed in Escherichia coli BL21(DE3) pLysS cells
-
wild-type ligated into vector pET30a(+) and overexpressed in Escherichia coli BL21 (DE3) pLysS harbouring pZI39. Selenol-methionine-labelled protein overexpressed in an auxotrophic Escherichia coli strain B834 (DE3) harbouring pZI39
-
expressed in Escherichia coli ER2566 cells
-
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli
A4XJR7
gene abnB, expression of wild-type and mutant enzymes
B3EYM8
expressed in Bacillus subtilis
-
expressed in Bacillus subtilis strain MI112
-
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
-, Q5H7M8
expressed in Escherichia coli; hyperexpression in Escherichia coli
-
expressed in Escherichia coli BL21 cells
A5IKD4, -
overexpression of His-tagged enzyme in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of the gene encoding cold-adapted endo-arabinase Abnc is strongly induced by arabinose, arabinitol, and arabinan
-, Q5H7M8
expression of the gene encoding cold-adapted endo-arabinase Abnc is strongly induced by arabinose, arabinitol, and arabinan
Penicillium chrysogenum 31B
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D171A
-
the mutant of isoform Arb43B displays no measurable activity
D38A
-
the mutant of isoform Arb43B displays no measurable activity
E224A
-
the mutant of isoform Arb43B displays no measurable activity
H318A
-
the mutant of isoform Arb43B displays a drastic decrease in enzymatic activity
D147A
B3EYM8
site-directed mutagenesis, structure comparison with the wild-type enzyme
E201A
B3EYM8
site-directed mutagenesis, structure comparison with the wild-type enzyme
D147A
Geobacillus stearothermophilus T-6
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
E201A
Geobacillus stearothermophilus T-6
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
DELTAV2-W17
-
deletion of the N-terminal amino acids causes thermal instability
DELTAV2-W17
Geobacillus thermodenitrificans TS-3
-
deletion of the N-terminal amino acids causes thermal instability
-
H318Q
-
enzymatic activity is completely lost in this mutant
additional information
B3FRL6
mutant strains IQB413 (DELTAabnA), IQB485 (DELTAabn2), and IQB486 (DELTAabnA DELTAabn2). Almost complete loss of activity in the DELTAabn2 DELTAabnA double mutant
additional information
Bacillus subtilis 168T+
-
mutant strains IQB413 (DELTAabnA), IQB485 (DELTAabn2), and IQB486 (DELTAabnA DELTAabn2). Almost complete loss of activity in the DELTAabn2 DELTAabnA double mutant
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nutrition
-
commercial applications in fruit and vegetable processing, particularly in apple juice manufacture where their use prevents haze formation in pectinase-treated apple pulp by depolymerizing debranched arabinan, linear alpha-1,5-arabinan, formed by the action of alpha-L-arabinofuranosidases during this process
analysis
-
structural analysis of plant cell pectic polysaccharides and arabinans
nutrition
-
commercial applications in fruit and vegetable processing, particularly in apple juice manufacture where their use prevents haze formation in pectinase-treated apple pulp by depolymerizing debranched arabinan, linear alpha-1,5-arabinan, formed by the action of alpha-L-arabinofuranosidases during this process
nutrition
-
-
analysis
-
useful in structural analysis of primary cell wall polysaccharides
analysis
-
useful for studies on structure of protopectin
nutrition
-
role in juice clarification
nutrition
-
useful for pectin extraction from citrus peel from fruit-juice industries and sugar-beet pulp from sugar factories
nutrition
-
useful for pectin production from sugar beet pulp
synthesis
-
applied to the refinement of cotton fiber, enzyme is able to release the cotton fiber coating, yielding product of high quality but with lower amounts of wastes
analysis
Bacillus subtilis F-11
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useful in structural analysis of primary cell wall polysaccharides
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nutrition
Bacillus subtilis F-11
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role in juice clarification
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nutrition
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production of L-arabinose from plant arabinan at high temperatures
nutrition
Geobacillus thermodenitrificans TS-3
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production of L-arabinose from plant arabinan at high temperatures
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industry
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endo-1,5-alpha-L-arabinanases belonging to glycoside hydrolase family 43 are of great industrial interest for use in food technology, organic synthesis and biofuel production owing to their ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides