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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Bacillus subtilis and UniProt Accession P18429
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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: Bacillus subtilis
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
endo-1,4-beta-xylanase
-
-
-
-
endoxylanase
-
-
-
-
xylanase
-
-
-
-
additional information
the enzyme belongs to glycosyl hydrolase family 11, GH11
additional information
the enzyme belongs to the glycosyl hydrolase family 11, GH11
additional information
-
the enzyme belongs to glycosyl hydrolase family 11, GH11
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
beechwood xylan + H2O
?
low affinity of the enzyme towards this substrate
-
-
?
sucrose + H2O
D-fructose + D-glucose
strong transxylosylation activity
-
-
?
xylan + H2O
xylobiose + xylotriose + xylotetraose
the hydrolysis products are mainly xylobiose (57.5% with immobilized enzyme, 36.1% with soluble enzyme) and xylotriose (38.4% with immobilized enzyme, 48.7% with soluble enzyme)
-
-
?
arabinoxylan + H2O
xylo-oligosaccharide + ?
-
product analysis, overview
-
?
arabinoxylan + H2O
xylo-oligosaccharide + ?
higher activity with water-unextractable, than-extractable arabinoxylans, overview
product analysis, overview
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharide + ?
-
product analysis, overview
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharide + ?
from birchwood xylan and wheat bran
product analysis, overview
-
?
arabinoxylan + H2O
?
-
the GHF 11 endoxylanase has a higher substrate specificity as compared to GHF 10 endoxylanases
-
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
-
the predominant products resulting from xylan and xylooligosaccharide hydrolysis are xylobiose and xylotriose. The enzyme can hydrolyze xylooligosaccharides larger than xylotriose
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
from birchwood
major products with equimolar ratio
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
from oat spelt or birchwood
the predominant products resulting from xylan and xylooligosaccharide hydrolysis are xylobiose and xylotriose. The enzyme can hydrolyze xylooligosaccharides larger than xylotriose
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
soluble larchwood xylan
-
-
?
additional information
?
-
-
digestion of a (1, 3),(1, 4)-beta-D-linkage sequence xylan from Rhodymenia into 4-linked xylobiose and xylotriose and 3,4-mixed linked oligosaccharides having a degree of polymerization of four or more
-
-
?
additional information
?
-
displays no transxylosylation activity toward xylitol, cellulose, chitin, chitosan, pectin, sorbitol, ribose, phenol, guaiacol, o-nitorphenol, vanilin and alcoholic compounds (methanol, ethanol, ethylene grecol and grecerol)
-
-
?
additional information
?
-
-
AMX-4 xylanase is not active toward other polysaccharides including carboxymethylcellulose, locust bean gum, lichenan, laminarin, and Avicel or toward synthetic substrate derivatives such as 4-nitrophenyl-beta-xylopyranoside, 4-nitrophenyl-beta-mannoside, and 4-nitrophenyl-beta-cellobioside, it can hydrolyze only beta-1,4-xylosidic linkages and has no beta-xylosidase activity
-
-
?
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
arabinoxylan + H2O
xylo-oligosaccharide + ?
-
product analysis, overview
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharide + ?
-
product analysis, overview
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
-
the predominant products resulting from xylan and xylooligosaccharide hydrolysis are xylobiose and xylotriose. The enzyme can hydrolyze xylooligosaccharides larger than xylotriose
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
other metalions than Fe2+ have an insignificant effect on transxylosylation activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
hydrolytic activity almost entirely inhibits at acidic pH
-
Triticum aestivum xylanase inhibitor
inhibits only microbial endoxylanases
-
Triticum aestivum xylanase inhibitor
inhibits only microbial endoxylanases. Microbial enzymes present in wheat flour are hardly active due to rapid inhibition by enzyme inhibitors present in wheat flour
-
Triticum aestivum xylanase inhibitor
TAXI, 44-50% inhibition of the wild-type enzyme, nearly no inhibition of enzyme mutant D11F/R122D
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
trehalose
-
activates both isozymes and stabilizes them at higher temperatures
additional information
endoxylanase activity is positively correlated with ash and negatively correlated with starch content
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
beechwood xylan
Km value for wild-type 5.84 mg/ml, for chimera carrying a carbohydrate-binding module 4.04 mg/ml, respectively, pH 6.0, 50°C
-
additional information
beechwood xylan
-
Km value for wild-type 5.84 mg/ml, for chimera carrying a carbohydrate-binding module 4.04 mg/ml, respectively, pH 6.0, 50°C
-
additional information
1,4-beta-D-xylan
-
Km for chimeric enzyme CorA-XynA at pH 6.5, 65°C: 6.3 mg/ml, KM for chimeric enzyme CorA-XynAG3 at pH 7.5, 75°C: 5.3 mg/ml, Km for xylanase XynA at pH 6.5, 55°C: 5.5 mg/ml, Km for thermostabel xylanase variant XynAG3 at pH 7.5, 70°C: 5.1 mg/ml
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
268
beechwood xylan
chimera carrying a carbohydrate-binding module, pH 6.0, 50°C
-
61
1,4-beta-D-xylan
-
pH 7.5, 70°C, thermostable xylanase variant XynAG3, calculated as D-xylose liberated from 1,4-beta-D-xylan per second
65
1,4-beta-D-xylan
-
pH 7.5, 70°C, chimeric enzyme CorA-XynAG3, calculated as D-xylose liberated from 1,4-beta-D-xylan per second
75
1,4-beta-D-xylan
-
pH 6.5, 65°C, chimeric enzyme CorA-XynA, calculated as D-xylose liberated from 1,4-beta-D-xylan per second
82
1,4-beta-D-xylan
-
pH 6.5, 55°C, xylanase XynA, calculated as D-xylose liberated from 1,4-beta-D-xylan per second
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
beechwood xylan
kcat/Km value for wild-type 40.6 ml/mg/s, for chimera carrying a carbohydrate-binding module 66.4 ml/mg/s, respectively, pH 6.0, 50°C
-
additional information
beechwood xylan
-
kcat/Km value for wild-type 40.6 ml/mg/s, for chimera carrying a carbohydrate-binding module 66.4 ml/mg/s, respectively, pH 6.0, 50°C
-
additional information
1,4-beta-D-xylan
-
kcat/Km for chimeric enzyme CorA-XynA at pH 6.5, 65°C: 12 ml/mg*ml, kcat/KM for chimeric enzyme CorA-XynAG3 at pH 7.5, 75°C: 12 ml/mg*ml, kcat/Km for xylanase XynA at pH 6.5, 55°C: 14.9 ml/mg*ml, kcat/Km for thermostabel xylanase variant XynAG3 at pH 7.5, 70°C: 11.9 ml/mg*ml
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.87
substrate rye arabinoxylan xylan, fusion protein with XylZ CBM domain, pH 6.0, 50°C
0.88
substrate oat spelt xylan, fusion protein with XylZ CBM domain, pH 6.0, 50°C
3.03
substrate beechwood xylan, fusion protein with XylZ CBM domain, pH 6.0, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
activity range, pH dependency of recombinant His-tagged wild-type and mutant enzymes, overview
5.5 - 8.5
more than 50% activity retained, enzyme activity decreases sharply below pH 5.5 and above pH 9.0, negligible amount of activity at pH below 5.0 and above 10.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
activity range, inactive at 60°C, temperature profile of recombinant His-tagged wild-type and mutant enzymes, overview
30 - 70
30°C: immobilized enzyme shows about 50% of maximal activity, soluble enzyme shows about 40% of maximal activity. 70°C: immobilized enzyme shows about 65% of maximal activity, soluble enzyme shows about 50% of maximal activity
40 - 60
transxylosylation and hydrolysis activities are optimal at temperatures of 60°C and 40°C, respectively
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
wheat kernel associated endoxylanases consist of a majority of microbial endoxylanases. Higher microbial endoxylanase activity in Legat than in Astuce wheat flour
additional information
wheat-kernel, most wheat-kernel-associated endoxylanases are from microbial origin
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
expression in a leaky outer membrane mutant of Gluconobacter oxydans created by deleting the TolB encoding gene gox1687. More than 70% of the total XynA activity (0.91 mmol per h and l culture) is detected in the culture supernatant of the TolB mutant and only 10% of endoxylanase activity is observed in the supernatant of wild-type Gluconobacter oxydans expressing XynA
additional information
additional information
a one-step method to immobilize xylanase onto cellulosic material by fusion of expansin from Bacillus subtilis to xylanase LC9 without the requirement of prior purification of enzyme is developed. Fusion enzyme EXLXR2-XYN is specifically adsorbed onto corncob residue with high loading capacity due to bio-affinity adsorption of expansin onto cellulose. The immobilization yield is close to 100%, with a recovered activity of 82.4%
additional information
-
a one-step method to immobilize xylanase onto cellulosic material by fusion of expansin from Bacillus subtilis to xylanase LC9 without the requirement of prior purification of enzyme is developed. Fusion enzyme EXLXR2-XYN is specifically adsorbed onto corncob residue with high loading capacity due to bio-affinity adsorption of expansin onto cellulose. The immobilization yield is close to 100%, with a recovered activity of 82.4%
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
structure homology modelling of wild-type and mutant enzymes, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
the extracellular endoxylanase expressed in yeast shows an enhanced thermal stability due to the N-linked glycosylation, the native enzyme in Bacillus subtilis is not glycosylated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D11F/R122D
the mutant shows highly decreased sensitivity to inhibitor Triticum aestivum xylanase inhibitor compared to wild-type enzyme
G23R
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
Q175K
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
T10H
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
W9H
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
F48C
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
T44C
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
T44Y
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
T87D
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
Y94C
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
additional information
additional information
generation of a bifunctional enzyme consisting of a GH11 endo-1,4-beta-xylanase fused to a GH43 beta-xylosidase, both from Bacillus subtilis. The substrate cleavage rate is altered by the molecular fusion improving at least 3fold the xylose production using specific substrates as beechwood xylan and hemicelluloses from pretreated biomass. The chimeric enzyme shows higher thermotolerance with a positive shift of the optimum temperature from 35°C to 50°C for xylosidase activity
additional information
fusion of enzyme with a carbohydrate-binding module from Clostridium thermocellum which exhibits high affinity to xylan. The molecular fusion does not alter the pH and temperature dependence, but leads to an increase of 65% in the catalytic efficiency. As supplement in the commercial cocktail Accellerase1 1500, the chimeric enzyme improves the reducing sugar release by 17% from pretreated sugarcane bagasse
additional information
-
fusion of enzyme with a carbohydrate-binding module from Clostridium thermocellum which exhibits high affinity to xylan. The molecular fusion does not alter the pH and temperature dependence, but leads to an increase of 65% in the catalytic efficiency. As supplement in the commercial cocktail Accellerase1 1500, the chimeric enzyme improves the reducing sugar release by 17% from pretreated sugarcane bagasse
additional information
construction of a fusion protein with the carbohydrate-binding doamin of xylanase XynZ from Clostridium thermocellum. The fusion does not alter the pH and temperature dependence, but increases the catalytic activity by 65%
additional information
-
construction of a fusion protein with the carbohydrate-binding doamin of xylanase XynZ from Clostridium thermocellum. The fusion does not alter the pH and temperature dependence, but increases the catalytic activity by 65%
additional information
-
the fusion of the 1642-bp laccase (CorA) with either the 555-bp xylanase (XynA) or the thermostable variant (XynAG3) are performed by insertion of the xylanase into a surface loop of the laccase. The resulting chimeric constructs of 2197 bp contain a central region composed of the XynA or XynAG3 sequence flanked by the regions of the CorA encoding the N-terminal residues 1216 (forming the 5' region of the chimera) and the C-terminal region comprising residues 217513 of CorA. As a consequence, the final construct results in two linkage points between the laccase and xylanase domains
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3
30-70% remaining activity for the enzyme mutants, 23% for the wild-type
710466
4
75-95% remaining activity for the enzyme mutants, 57% for the wild-type
710466
additional information
additional information
molecular mechanisms governing the pH-dependent stability of GH11 proteins, overview
710466
additional information
-
molecular mechanisms governing the pH-dependent stability of GH11 proteins, overview
710466
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
the half-life of the recombinant protein at 50°C is 65 min whereas it is approximately 25 min at 60°C. The enzyme is not stable at 70°C and it loses almost all of its activity even 5 min after incubation
60
70
additional information
-
trehalose stabilizes both isozymes at 60°C and 70°C and increases the enzyme activity, thermal deactivation kinetics of enzyme forms XylI and XylII
60
-
50% final residual activity in presence of 0.5 M trehalose as well as 8fold increased half-life of XylII and 2.5fold of XylI, inactivation in absence of trehalose
60
-
the wild type enzyme completely loses activity after preincubation at 60°C
60
glycosylated recombinant enzyme, 30 h, 50% remaining activity. Unglycosylated native enzyme, 12 h, 50% activity remaining
70
-
35% final residual activity in presence of 0.5 M trehalose as well as 2fold increased half-lives of XylII and XylI, inactivation in absence of trehalose
70
-
the thermostable variant XynAG3 loses 90% of its activity after 10 min, and after 30 min no activity is observed. The chimeric CotA-XynAG3 retains 60% activity after 10 min and about 20% activity after 120 min. The half-lives of the chimeric enzymes XynAG3 and CotA-XynAG3 are 2.2 and 21 min
70
3 h, immobilized enzyme retains 45.3% of its activity, soluble enzyme retains 16.3% of its activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the immobilized enzyme retains more than 70% of its initial capability for xylooligosaccharide production after five reaction cycles
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
by ammonium sulfate fractionation, centrifugation and gel filtration, 7.7fold
by ammonium sulfate precipitation, anion-exchange and hydrophobic interaction column chromatographies, 17.5fold purified
the chimeric enzymes, CorA-XynA and CorA-XynAG3, the parental enzyme XynA, and the thermostable variant XynAG3 are produced in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene xynA, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expressed from vector pT-xyl in Escherichia coli strain BL21(DE3)CodonPlus-RIL
gene xylA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
gene xynB, expression in Saccharomyces cerevisiae strain SEY2102, the recombinant enzyme is secreted, and the extracellular endoxylanase expressed in yeast shows an enhanced thermal stability due to the N-linked glycosylation
the chimeric enzymes, CorA-XynA and CorA-XynAG3, the parental enzyme XynA, and the thermostable variant XynAG3 are produced in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
when a fusion protein with the carbohydrate-binding domain of xylanase XynZ from Clostridium thermocellum supplements the commercial cocktail Accellerase1 1500, reducing sugar release is improved by 17% from pretreated sugarcane bagasse
food industry
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
food industry
-
application of the extremely thermo- and alkali-stable enzyme for preparation of prebiotic xylooligosaccharides
industry
the broad temperature profile of the enzyme makes it a potential candidate for its use in the pulp and paper industry
additional information
the Bacillus sp. KT12 xylanolytic enzyme is a suitable enzyme for the synthesis of polyphenyl beta-oligoxylosides
food industry
contribution of microbial endoxylanases to changes in arabinoxylan during the breadmaking process are very low. Microbial endoxylanases end up in flour as contaminant and affect its functional properties
food industry
high levels of endoxylanase activity in wheat flour should be avoided as they can cause uncontrolled degradation of arabinoxylan during bread dough processing, glutenstarch separation, or refrigerated dough storage
food industry
improvement of cereal-based industrial processing by endoxylanase enzymes insensitive towards inhibitors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kato, Y.; Nevins, D.J.
Enzymic dissociation of Zea shoot cell wall polysaccharides. III. Purification and partial characterization of an endo-(1->4)-beta-D-xylanase
Plant Physiol.
75
753-758
1984
Bacillus subtilis
Bernier, R.; Desrochers, M.; Jurasek, L.; Paice, M.G.
Isolation and characterization of a xylanase from Bacillus subtilis
Appl. Environ. Microbiol.
46
511-514
1983
Bacillus subtilis, Bacillus subtilis PAP115
Sa-Pereira, P.; Carvalho, A.S.L.; Costa-Ferreira, M.; Aires-Barros, M.R.
Thermostabilization of Bacillus subtilis CCMI 966 xylanases with trehalose. Study of deactivation kinetics
Enzyme Microb. Technol.
34
278-282
2004
Bacillus subtilis, Bacillus subtilis CCMI 966
-
Belien, T.; Verjans, P.; Courtin, C.M.; Delcour, J.A.
Phage display based identification of novel stabilizing mutations in glycosyl hydrolase family 11 B. subtilis endoxylanase XynA
Biochem. Biophys. Res. Commun.
368
74-80
2008
Bacillus subtilis
Dornez, E.; Gebruers, K.; Wiame, S.; Delcour, J.A.; Courtin, C.M.
Insight into the distribution of arabinoxylans, endoxylanases, and endoxylanase inhibitors in industrial wheat roller mill streams
J. Agric. Food Chem.
54
8521-8529
2006
Triticum aestivum, Bacillus subtilis (P18429), Talaromyces purpureogenus (Q9P8J1)
Verwimp, T.; Van Craeyveld, V.; Courtin, C.M.; Delcour, J.A.
Variability in the structure of rye flour alkali-extractable arabinoxylans
J. Agric. Food Chem.
55
1985-1992
2007
Aspergillus aculeatus, Bacillus subtilis
Dornez, E.; Cuyvers, S.; Gebruers, K.; Delcour, J.A.; Courtin, C.M.
Contribution of wheat endogenous and wheat kernel associated microbial endoxylanases to changes in the arabinoxylan population during breadmaking
J. Agric. Food Chem.
56
2246-2253
2008
Triticum aestivum, Bacillus subtilis (P18429), Talaromyces purpureogenus (Q9P8J1)
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
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
Jalal, A.; Rashid, N.; Rasool, N.; Akhtar, M.
Gene cloning and characterization of a xylanase from a newly isolated Bacillus subtilis strain R5
J. Biosci. Bioeng.
107
360-365
2009
Bacillus subtilis (B9ZZN9), Bacillus subtilis R5 (B9ZZN9)
Lee, J.; Heo, S.; Lee, J.; Yoon, K.; Kim, Y.; Nam, S.
Thermostability and xylan-hydrolyzing property of endoxylanase expressed in yeast Saccharomyces cerevisiae
Biotechnol. Bioprocess Eng.
14
639-644
2009
Bacillus subtilis (Q45VU2)
-
Rasmussen, L.E.; Soerensen, J.F.; Meyer, A.S.
Kinetics and substrate selectivity of a Triticum aestivum xylanase inhibitor (TAXI) resistant D11F/R122D variant of Bacillus subtilis XynA xylanase
J. Biotechnol.
146
207-214
2010
Bacillus subtilis (P18429)
Yoon, K.H.
Cloning of a Bacillus subtilis AMX-4 xylanase gene and characterization of the gene product
J. Microbiol. Biotechnol.
19
1514-1519
2009
Bacillus subtilis, Bacillus subtilis AMX-4
Belien, T.; Joye, I.J.; Delcour, J.A.; Courtin, C.M.
Computational design-based molecular engineering of the glycosyl hydrolase family 11 B. subtilis XynA endoxylanase improves its acid stability
Protein Eng. Des. Sel.
22
587-596
2009
Bacillus subtilis (P18429), Bacillus subtilis
Ribeiro, L.F.; Furtado, G.P.; Lourenzoni, M.R.; Costa-Filho, A.J.; Santos, C.R.; Nogueira, S.C.; Betini, J.A., Polizeli, Mde L.; Murakami, M.T.; Ward, R.J.
Engineering bifunctional laccase-xylanase chimeras for improved catalytic performance
J. Biol. Chem.
286
43026-4338
2011
Bacillus subtilis
Diogo, J.A.; Hoffmam, Z.B.; Zanphorlin, L.M.; Cota, J.; Machado, C.B.; Wolf, L.D.; Squina, F.; Damasio, A.R.; Murakami, M.T.; Ruller, R.
Development of a chimeric hemicellulase to enhance the xylose production and thermotolerance
Enzyme Microb. Technol.
69
31-37
2015
Bacillus subtilis (P18429), Bacillus subtilis 168 (P18429)
Kosciow, K.; Domin, C.; Schweiger, P.; Deppenmeier, U.
Extracellular targeting of an active endoxylanase by a TolB negative mutant of Gluconobacter oxydans
J. Ind. Microbiol. Biotechnol.
43
989-999
2016
Bacillus subtilis (P18429), Bacillus subtilis, Bacillus subtilis 168 (P18429)
Hoffmam, Z.; Zanphorlin, L.; Cota, J.; Diogo, J.; Almeida, G.; Damasio, A.; Squina, F.; Murakami, M.; Ruller, R.
Xylan-specific carbohydrate-binding module belonging to family 6 enhances the catalytic performance of a GH11 endo-xylanase
New Biotechnol.
33
467-472
2016
Bacillus subtilis (P18429), Bacillus subtilis, Bacillus subtilis 168 (P18429)
Gagoski, D.; Shi, Z.; Nielsen, L.K.; Vickers, C.E.; Mahler, S.; Speight, R.; Johnston, W.A.; Alexandrov, K.
Cell-free pipeline for discovery of thermotolerant xylanases and endo-1,4-beta-glucanases
J. Biotechnol.
259
191-198
2017
Thermothielavioides terrestris, Bacillus subtilis, Humicola insolens
Wu, B.; Yu, Q.; Chang, S.; Pedroso, M.M.; Gao, Z.; He, B.; Schenk, G.
Expansin assisted bio-affinity immobilization of endoxylanase from Bacillus subtilis onto corncob residue Characterization and efficient production of xylooligosaccharides
Food Chem.
282
101-108
2019
Bacillus subtilis (A0A172MAU1), Bacillus subtilis
de Almeida, M.; Guimaraes, V.; Falkoski, D.; de Camargo, B.; Fontes-Santana, G.; Maitan-Alfenas, G.; de Rezende, S.
Purification and characterization of an invertase and a transfructosylase from Aspergillus terreus
J. Food Biochem.
42
e12551
2018
Bacillus subtilis, Bacillus subtilis DFR40
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