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Information on EC 3.2.1.37 - xylan 1,4-beta-xylosidase
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3.2.1.37 xylan 1,4-beta-xylosidaseIUBMB Comments
Also hydrolyses xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver.
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Word Map
- 3.2.1.37
- xylans
- xylose
- arabinose
- arabinoxylans
- xylobiose
- xylooligosaccharides
- niger
- trichoderma
- p-nitrophenyl
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xylanolytic
- cellulase
- xylanases
-
hemicellulases
- endoxylanase
- arabinans
- reesei
- spelt
- beta-d-xylopyranoside
- endoglucanase
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saccharification
- cellobiohydrolase
- p-nitrophenyl-beta-d-xylopyranoside
- pumilus
- beta-d-galactosidase
-
xylan-degrading
- beta-xylanase
-
arabinosidase
- alpha-fucosidase
- avicel
-
birchwood
- beta-d-fucosidase
- cmcases
-
thermoanaerobacterium
- alpha-glucuronidase
- thermomonospora
-
xylopyranosyl
- saccharolyticum
- ruminantium
- xylotetraose
-
hemicellulolytic
-
feruloyl
- alpha-d-mannosidase
- fibrisolvens
- endo-1,4-beta-xylanase
-
selenomonas
- glucuronoxylans
-
hemicellulosic
- nutrition
- degradation
- synthesis
- food industry
- analysis
- biotechnology
-
xylanohydrolase
- biofuel production
- agriculture
- alpha-d-galactosidase
- industry
- l-arabitol
- pharmacology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
beta-xylosidase, alpha-l-arabinofuranosidase, xylosidase, beta-d-xylosidase, xyl i, xynb2, xyl3a, xln-dt, xynb3, axh-d3, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-D-xylan xylohydrolase
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beta-D-xylopyranosidase
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beta-xylosidase
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exo-1,4-beta-D-xylosidase
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exo-1,4-beta-xylosidase
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Exo-beta-(1,4)-xylanase
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Xylan 1,4-beta-xylosidase
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xylobiase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-xylan xylohydrolase
Also hydrolyses xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver.
CAS REGISTRY NUMBER
COMMENTARY
9025-53-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7.5
pH 5.5: about 60% of maximal activity, pH 7.5: about 50% of maximal activity, enzyme entrapped in calcium alginate beads
6 - 7.5
less than 10% of maximal activity at pH 5.5, pH 6.0: maximal activity, pH 7.5: about 60% of maximal activity, soluble enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 100
65°C: about 60% of maximal activity, 100°C: about 85% of maximal activity, enzyme entrapment in calcium alginate beads
70 - 90
70°C: about 50% of maximal activity, 90°C: about 25% of maximal activity, soluble enzyme
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q97UI4_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
754
0
83619
TrEMBL
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
24 h, soluble enzyme and enzyme immobilized by entrapment into alginate are completely stable
90
half life of enzyme immobilized by entrapment into alginate: 21 h. Half-life of soluble enzyme: 10 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized enzyme shows good operational stability retaining 84% of its initial activity and yielding 63% xylose after four cycles of reusing
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, soluble enzyme, retains 50% of the activity after 2 months
4°C, the enzyme immobilized by entrapment into alginate retains 38% activity after 1 year
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the enzyme immobilized by entrapment into alginate can be used for a continuous production of xylose from xylooligosaccharides at high temperature
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morana, A.; Mangione, A.; Maurelli, L.; Fiume, I.; Paris, O.; Cannio, R.; Rossi, M.
Immobilization and characterization of a thermostable beta-xylosidase to generate a reusable biocatalyst
Enzyme Microb. Technol.
39
1205-1213
2006
Saccharolobus solfataricus (Q97UI4), Saccharolobus solfataricus P2 (Q97UI4)
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