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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Aspergillus niger and UniProt Accession P55329
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3.2.1.8 endo-1,4-beta-xylanaseSpecify your search results
Word Map
- 3.2.1.8
- xylans
- xylanases
- xylose
- arabinoxylans
- trichoderma
- xylooligosaccharides
- reesei
- xylotriose
-
xylanolytic
-
birchwood
- spelt
- cellulases
- straw
-
carbohydrate-binding
-
lignocellulosic
- beta-xylosidase
- xylotetraose
- bran
-
hemicellulases
- lanuginosus
- thermomyces
- corncob
- arabinofuranosidase
- bagasse
- cellobiohydrolase
- alpha-l-arabinofuranosidase
- cellulomonas
-
saccharification
-
cellulose-binding
- avicel
-
thermoascus
- degradation
- agriculture
- cellulosome
- paper production
- glucuronoxylans
-
lignocellulolytic
- endo-1,4-beta-glucanase
- halodurans
- arabinan
- industry
- xylosidase
- biofuel production
-
breadmaking
- analysis
-
hemicellulolytic
- nutrition
- cellulolyticus
- longibrachiatum
-
taxi
- food industry
- synthesis
-
kraft
- biotechnology
-
biobleaching
-
cellulase-free
- neocallimastix
-
water-extractable
- cellulosa
-
dockerin
The taxonomic range for the selected organisms is: Aspergillus niger
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
endoxylanase, xylanase a, endo-xylanase, xyn11a, xyn10a, beta-xylanase, endo-1,4-beta-xylanase, gh11 xylanase, xylanase b, xynii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1--> 4)-beta-xylan 4-xylanohydrolase
-
-
-
-
1,4-beta-D-xylan xylanohydrolase
-
-
-
-
1,4-beta-D-xylan xylanohydrolase 22
-
-
-
-
1,4-beta-xylan xylanohydrolase
-
-
-
-
34 kDa xylanase
-
-
-
-
beta-1,4-D-xylanase
-
-
-
-
beta-1,4-xylan xylanohydrolase
-
-
-
-
beta-1,4-xylanase
-
-
-
-
beta-D-xylanase
-
-
-
-
beta-xylanase
-
-
-
-
endo-(1--> 4)-beta-xylanase
-
-
-
-
endo-1,4-beta-D-xylanase
endo-1,4-beta-xylanase
-
-
-
-
endo-1,4-xylanase
-
-
-
-
endo-beta-1,4-xylanase
-
-
-
-
endoxylanase
FIA-xylanase
-
-
-
-
ORF4
-
-
-
-
TAXI
-
-
-
-
X34
-
-
-
-
XYLA
-
-
-
-
xylanase
Xylanase 22
-
-
-
-
xylanase, endo-1,4-
-
-
-
-
XYLD
-
-
-
-
XYLY
-
-
-
-
additional information
-
the enzyme belongs to the glycosyl hydrolase family 11, GH11
endo-1,4-beta-D-xylanase
-
-
-
-
endoxylanase
-
-
-
-
xylanase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-xylan xylanohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9025-57-4
-
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 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
84% of the activity with xyloheptaose
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
-
?
birchwood xylan + H2O
D-xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose
-
can be hydrolyzed by hybrid xylanase and its Aspergillus parent. Hydrolysis products by hybrid xylanase and its Aspergillus parent are D-xylose, xylobiose, xylotriose, xylotetraose and xylopentaose. Xylotriose is the main product released from birchwood xylan and wheat bran insoluble xylan by hybrid xylanase and its Aspergillus parent, respectively
-
-
?
wheat bran xylan + H2O
D-xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose
-
can be hydrolyzed by hybrid xylanase and its Aspergillus parent. Hydrolysis products by hybrid xylanase and its Aspergillus parent are D-xylose, xylobiose, xylotriose, xylotetraose, xylopentaose and xylohexaose. Xylotriose is the main product released from birchwood xylan and wheat bran insoluble xylan by hybrid xylanase and its Aspergillus parent, respectively
-
-
?
xylan + H2O
xylobiose + D-xylose + ?
substrate birchwood xylan
after 24 h of hydrolysis, more than 90% of the total hydrolysis products of xylan are xylobiose and D-xylose with almost no xylotetraose, -pentaose, or -hexaose
-
?
xylobiose + H2O
?
-
can be hydrolyzed by the Aspergillus parent, no activity with hybrid xylanase
-
-
?
xylohexaose + H2O
2 xylotriose
-
can be hydrolyzed by the Aspergillus parent and hybrid xylanase
-
-
?
xylopentaose + H2O
xylobiose + xylotriose + xylotetraose
-
can be hydrolyzed by the Aspergillus parent and hybrid xylanase
-
-
?
xylotriose + H2O
?
-
can be hydrolyzed by the Aspergillus parent, no activity with hybrid xylanase
-
-
?
arabinoxylan + H2O
?
-
39% arabinan, 62% xylan from wheat, substrate water activity (ratio of the equilibrium water vapor pressure over a material to that over pure water, roughly corresponding to the water content) range from 0.21-1.0, corresponding to 5-60% water content (dry basis)
oligosaccharides, xylobiose, xylotriose
-
?
xylotetraose + H2O
2 xylobiose
-
can be hydrolyzed by the Aspergillus parent and hybrid xylanase
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
soluble xylan and insoluble xylan only after arabinosyl-initiated branch points are removed
oligosaccharides of intermediate length especially xylotriose and xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
oligosaccharides of intermediate length especially xylotriose and xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
hydrolyzes soluble xylan more rapidly than insoluble branched xylan
-
-
?
additional information
?
-
-
endo mechanism of Xln-1 and substrate specificity, overview, no activity with carboxymethyl cellulose, starch, pectin, and 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
NATURAL SUBSTRATE
NATURAL 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
maximum endoxylanase activity at 72 h of cultivation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
beechwood xylan
-
Km value is 3.0 mg/ml, pH 5.0, 50°C
-
additional information
birchwood xylan
-
Km value is 2.95 mg/ml, pH 5.0, 50°C
-
additional information
additional information
-
Km for oat spelt xylan is 8.19 mg/ml, kinetics
-
additional information
oat spelt xylan
-
Km value is 6.6 mg/ml, pH 5.0, 50°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
beechwood xylan
-
kcat/Km value is 3401 ml per mg and s, pH 5.0, 50°C
-
additional information
birchwood xylan
-
kcat/Km value is 2632 ml per mg and s, pH 5.0, 50°C
-
additional information
oat spelt xylan
-
kcat/Km value is 2625 ml per mg and s, pH 5.0, 50°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activities of wild-type and mutant enzymes, overview
additional information
-
enzyme activity is proportional to water activity (ratio of the equilibrium water vapor pressure over a material to that over pure water, roughly corresponding to the water content), enzyme activity as low as at a water activity of 0.59, 0.1 M sodium acetate, pH 4.5, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.8 - 7.5
-
pH 2.8: about 30% of maximal activity, pH 7.5: about 40% of maximal activity
3 - 8
-
pH 3.0: about 90% of maximal activity, pH 8.0: about 25% of maximal activity, xylanase IB
3.5 - 6.5
-
pH 3.5: about 40% of maximal activity, pH 6.5: about 35% of maximal activity
3.5 - 8
-
pH 3.5: about 70% of maximal activity, pH 8.0: about 30% of maximal activity, xylanase IA
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
50
50 - 60
-
optimum temperature for hybrid xylanase and its Aspergillus parent is 60°C and 50°C, respectively
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 70
-
activity at 50°C is about 20% higher compared to activity at 70°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
endoxylanase production is optimized using agricultural bagasses and cost 20 times less than enzyme production using synthetic xylan
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
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). XYNA_ASPNG
211
0
22642
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
enzyme N-terminal structure analysis and homology modelling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q127E
-
specific activity is lower than 5% compared to the wild type enzyme
Q127L
-
specific activity is lower than 5% compared to the wild type enzyme
T11Y/N12H/N13D/F15Y/F16F
-
the mutation increases the enzyme's thermostability
T205C/A52C
the optimum temperature of the mutant enzyme is improved from 45°C to 60°C, and it retains greater than 90.0% activity (wild-type enzyme retains only 50.0% activity) after treatment at 50°C for 85 min. The optimum pH of mutant xylanase is similar to wild-type enzyme (pH 5.0). The pH stability span (5.0-7.0) of the wild-type enzyme is increased to 3.0-9.0 for the mutant enzyme
W9Y
-
mutant enzyme is insensitive for Triticum aestivum xylanase inhibitor-II
W9Y/N35D
-
increased sensitivity to Triticum aestivum xylanase inhibitor-I and insensitive for Triticum aestivum xylanase inhibitor-II
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
5 - 7
-
purified native enzyme, 50°C, 86% residual activity after 45 min, the crude enzyme retains only 6% of the initial activity
710686
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
50
55
1 h, mutant enzyme T205C/A52C retains more than 80% of its initial activity
80
50
-
purified native enzyme, pH 5.0-7.0, 86% residual activity after 45 min, the crude enzyme retains only 6% of the initial activity
80
-
15 min, xylanase IA and Ib are rapidly inactivated above, xylanase II is completly inactivated
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 4fold by consecutive ultrafiltration and anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant AnxBs in Escherichia coli strain BL21 (DE3)
-
the mutant gene xynZFTA is cloned into pPIC9K and expressed in Pichia pastoris
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme is denatured by 8 M urea and 100 mM DTT, renaturation to 93% recovered activity by three-phase partitioning method using an ammonium sulfate, water, and tert-butanol mixture obtaining organic phase, interfacial precipitate and aqueous phase, the latter bearing the partially purified enzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
enzyme coupled assay procedure, using substrate 4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] and release of 4-nitrophenol by beta-xylosidase
biofuel production
-
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently
synthesis
production of enzyme in Pichia pastoris with codon optimization. The activity of dual-copy enzyme is maximized at 15158 U/ml after 120 h of shaking
additional information
-
the hybrid xylanase, whose parents are Thermomonospora fusca xylanase A and Aspergillus niger xylanase A, inherits some hydrolytic properties from its parents, and it is an endo-acting xylanase. X4 may be the minimum oligomer hydrolyzed by it
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Frederick, M.M.; Kiang, C.H.; Frederick, J.R.; Reilly, P.J.
Purification and characterization of endo-xylanases from Aspergillus niger. I. Two isozymes active on xylan backbones near branch points
Biotechnol. Bioeng.
27
525-532
1985
Aspergillus niger
Shei, J.C.; Fratzke, A.R.; Frederick, M.M.; Frederick, J.R.; Reilly, P.J.
Purification and characterization of endo-xylanases from Aspergillus niger. II. An enzyme of pI 4.5
Biotechnol. Bioeng.
27
533-538
1985
Aspergillus niger
Fournier, R.; Frederick, M.M.; Frederick, J.R.; Reilly, P.J.
Purification and characterization of endo-xylanases from Aspergillus niger. III. An enzyme of pI 3.65
Biotechnol. Bioeng.
27
539-546
1985
Aspergillus niger
John, M.; Schmidt, B.; Schmidt, J.
Purification and some properties of five endo-1,4-beta-D-xylanases and a beta-D-xylosidase produced by a strain of Aspergillus niger
Can. J. Biochem.
57
125-134
1979
Aspergillus niger
Gorbacheva, I.V.; Rodionova, N.A.
Studies on xylan degrading enzymes. I. Purification and characterization of endo-1,4-beta-xylanase from Aspergillus niger str. 14
Biochim. Biophys. Acta
484
79-93
1977
Aspergillus niger, Aspergillus niger 14
Roy, I.; Sharma, A.; Gupta, M.N.
Three-phase partitioning for simultaneous renaturation and partial purification of Aspergillus niger xylanase
Biochim. Biophys. Acta
1698
107-110
2004
Aspergillus niger
Levasseur, A.; Asther, M.; Record, E.
Overproduction and characterization of xylanase B from Aspergillus niger
Can. J. Microbiol.
51
177-183
2005
Aspergillus niger
Berrin, J.G.; Juge, N.
Factors affecting xylanase functionality in the degradation of arabinoxylans
Biotechnol. Lett.
30
1139-150
2008
Bacillus sp. (in: Bacteria), Cellvibrio japonicus, Cellvibrio japonicus (Q59675), Acetivibrio thermocellus (O52780), Streptomyces lividans (P26514), Neocallimastix patriciarum (P29127), Paenibacillus polymyxa (P45796), Cellulomonas fimi (P54865), Aspergillus niger (P55329), Rhodothermus marinus (P96988), Aspergillus nidulans (Q00177), Thermotoga maritima (Q60037), Streptomyces olivaceoviridis (Q7SI98), Thermoclostridium stercorarium (Q8GJ44), Talaromyces funiculosus (Q9HFH0), Trichoderma viride (Q9UVF9)
Ruanglek, V.; Sriprang, R.; Ratanaphan, N.; Tirawongsaroj, P.; Chantasigh, D.; Tanapongpipat, S.; Pootanakit, K.; Eurwilaichitr, L.
Cloning, expression, characterization, and high cell-density production of recombinant endo-1,4-beta-xylanase from Aspergillus niger in Pichia pastoris
Enzyme Microb. Technol.
41
19-25
2007
Aspergillus niger, Aspergillus niger BCC14405
-
Bourgois, T.M.; Nguyen, D.V.; Sansen, S.; Rombouts, S.; Belien, T.; Fierens, K.; Raedschelders, G.; Rabijns, A.; Courtin, C.M.; Delcour, J.A.; Van Campenhout, S.; Volckaert, G.
Targeted molecular engineering of a family 11 endoxylanase to decrease its sensitivity towards Triticum aestivum endoxylanase inhibitor types
J. Biotechnol.
130
95-105
2007
Aspergillus niger, Bacillus subtilis (P18429), Bacillus subtilis
Sun, J.Y.; Liu, M.Q.; Weng, X.Y.
Hydrolytic properties of a hybrid xylanase and its parents
Appl. Biochem. Biotechnol.
152
428-439
2009
Aspergillus niger, Thermobifida fusca
Smith, W.A.; Thompson, D.N.; Thompson, V.S.; Radtke, C.W.; Carter, B.
Assessment of xylanase activity in dry storage as a potential method of reducing feedstock cost
Appl. Biochem. Biotechnol.
154
108-122
2009
Aspergillus niger, Thermomyces lanuginosus, Trichoderma longibrachiatum
Chiku, K.; Uzawa, J.; Seki, H.; Amachi, S.; Fujii, T.; Shinoyama, H.
Characterization of a novel polyphenol-specific oligoxyloside transfer reaction by a family 11 xylanase from Bacillus sp. KT12
Biosci. Biotechnol. Biochem.
72
2285-2293
2008
Aspergillus niger, Penicillium expansum, Trichoderma viride, Bacillus subtilis (Q45VU2), Bacillus subtilis KT12 (Q45VU2), Penicillium expansum IFO 8800, Aspergillus niger IFO 31628
Aachary, A.A.; Prapulla, S.G.
Corncob-induced endo-1,4-beta-D-xylanase of Aspergillus oryzae MTCC 5154: production and characterization of xylobiose from glucuronoxylan
J. Agric. Food Chem.
56
3981-3988
2008
Aspergillus flavus, Aspergillus niger, Aspergillus ochraceus, Aspergillus oryzae, Aureobasidium pullulans, Penicillium citrinum, Trichoderma harzianum, Trichoderma viride, Aspergillus oryzae MTCC 5154, Penicillium citrinum MTCC 2553, Trichoderma harzianum ATCC 42459, Aureobasidium pullulans CFR 77
Zhang, S.; Zhang, K.; Chen, X.; Chu, X.; Sun, F.; Dong, Z.
Five mutations in N-terminus confer thermostability on mesophilic xylanase
Biochem. Biophys. Res. Commun.
395
200-206
2010
Aspergillus niger, Streptomyces olivaceoviridis, Thermobifida fusca, Aspergillus niger UV-11
Dobrev, G.; Zhekova, B.; Delcheva, G.; Koleva, L.; Tziporkov, N.; Pishtiyski, I.
Purification and characterization of endoxylanase Xln-1 from Aspergillus niger B03
World J. Microbiol. Biotechnol.
25
2095-2102
2009
Aspergillus niger, Aspergillus niger B03
Gao, H.; Yan, P.; Zhang, B.; Shan, A.
Expression of Aspergillus niger IA-001 endo-beta-1,4-xylanase in Pichia pastoris and analysis of the enzymic characterization
Appl. Biochem. Biotechnol.
173
2028-2041
2014
Aspergillus niger (F5CI28), Aspergillus niger, Aspergillus niger IA-0010 (F5CI28)
Guo, N.; Zheng, J.; Tian, J.; Wu, L.; Zhou, H.
Characterization and constitutive expression of an acidic mesophilic endo-1,4-beta-D-xylanohydrolase with high thermotolerance and catalytic efficiency in Pichia pastoris
World J. Microbiol. Biotechnol.
29
2095-2103
2013
Aspergillus niger
van den Brink, J.; van Muiswinkel, G.C.; Theelen, B.; Hinz, S.W.; de Vries, R.P.
Efficient plant biomass degradation by thermophilic fungus Myceliophthora heterothallica
Appl. Environ. Microbiol.
79
1316-1324
2013
Aspergillus niger, Thermothelomyces heterothallicus, Trichoderma reesei, Thermothelomyces thermophilus, Thermothelomyces thermophilus ATCC 424674, Thermothelomyces heterothallicus CBS 202.75, Thermothelomyces heterothallicus CBS 663.74
Mangan, D.; Cornaggia, C.; Liadova, A.; McCormack, N.; Ivory, R.; McKie, V.A.; Ormerod, A.; McCleary, B.V.
Novel substrates for the automated and manual assay of endo-1,4-beta-xylanase
Carbohydr. Res.
445
14-22
2017
Cellvibrio mixtus (O68541), Neocallimastix patriciarum (P29127), Aspergillus niger (P55329)
Cai, L.; Zhang, M.; Shao, T.; He, Y.; Li, J.; Ren, B.; Zhou, C.
Effect of introducing disulfide bridges in C-terminal structure on the thermostability of xylanase XynZF-2 from Aspergillus niger
J. Gen. Appl. Microbiol.
65
240-245
2019
Aspergillus niger (I3QKR9), Aspergillus niger
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