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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Thermomyces lanuginosus and UniProt Accession O43097
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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: Thermomyces lanuginosus
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 family 11 of glycosyl hydrolases
endoxylanase
-
-
-
-
xylanase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
histidine, tryptophan residues and carboxylic groups are involved in substrate binding or catalysis
-
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
avicel + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
barley glucan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
beechwood xylan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
birchwood xylan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
carboxymethyl cellulose + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
oat spelt xylan + H2O
xylose + ?
-
no release of xylo-oligosaccharides detected
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
no hydrolysis
-
-
?
beechwood 4-O-methyl-D-glucuronoxylan + H2O
xylose + xylobiose + ?
-
-
-
-
?
jute dust + H2O
?
-
pretreated with boiling sodium hydroxide solution for 1 h, followed by washing. Xylanase from Thermomyces lanuginosus produces a softer and mechanically stronger final product than that from Thermomyces aurantiacus when applied to low-quality jute fiber
-
-
?
O-acetyl-4-O-methyl-D-glucuronoxylan + H2O
xylose + xylobiose + ?
-
-
-
-
?
wheat arabinoxylan + H2O
?
-
incomplete utilization of wheat arabinoxylan, which leads to the accumulation of a complex mixture of branched oligosaccharides accounting more than 90% of the starting polysaccharide
-
-
?
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
-
?
beechwood xylan + H2O
?
-
77% of the activtiy with oat spelt xylan
-
-
?
birchwood xylan + H2O
?
-
84% of the activtiy with oat spelt xylan
-
-
?
xylan + H2O
?
-
commercial substrate and from oat spelts and larch sawdust, the latter being the best substrate for wild-type and mutant enzyme
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylooligosaccharides are observed at the beginning and after prolonged incubation, xylotriose and xylobiose are predominant, with a small amount of xylose
?
additional information
?
-
-
no activity with mannan, araban, galactomannan, inulin, Avicel, soluble starch, sodium carboxymethylcellulose, 2- or 4-nitrophenyl-gluco-, xylo-, manno-, galacto-pyranosides, and arabinofuranoside
-
-
?
additional information
?
-
-
facilitating hemicellulose degradation
-
-
?
additional information
?
-
-
releases chromophoric material from bagasse pulp. Amounts of reducing sugars released by the enzyme from bagasse pulp are significantly greater than that released from wheat and rice straw pulps. It decreases the kappa number of pulps, improves pulp brightness and reduces the chlorine dioxide consumption on pulp
-
-
?
additional information
?
-
-
enzyme displays no other enzyme activity such as cellulase, beta-glucosidase, beta-mannosidase, alpha-arabinofuranosidase, or beta-xylosidase
-
-
?
additional information
?
-
-
no substrates: 4-nitrophenyl beta-D--xyloside, 4-nitrophenyl beta-cellobioside
-
-
?
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
additional information
?
-
-
facilitating hemicellulose degradation
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 1.1fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Co2+
5 mM, 3.3fold activation of activity with carboxymethyl cellulose, 1.4fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Cu2+
5 mM, 1.6fold activation of activity with carboxymethyl cellulose, 16.4% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Fe2+
5 mM, 2.9fold activation of activity with carboxymethyl cellulose, 6.7% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Fe3+
5 mM, 1.1fold activation of activity with carboxymethyl cellulose, 9.1% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
K+
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 13% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Mg2+
5 mM, 2.3fold activation of activity with carboxymethyl cellulose, 6.5% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Mn2+
5 mM, 6.6fold activation of activity with carboxymethyl cellulose, 1.6fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Na+
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 6% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Zn2+
5 mM, 1.7fold activation of activity with carboxymethyl cellulose, no effect on xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
5 mM, 90.6% inhibition of activity with carboxymethyl cellulose, 1.1fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
ethanol
5%, 16% inhibition of activity with carboxymethyl cellulose, 24% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Fe3+
5 mM, 1.1fold activation of activity with carboxymethyl cellulose, 9.1% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Isopropanol
5%, 21.6% inhibition of activity with carboxymethyl cellulose, 53% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
K+
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 13% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
methanol
5%, 26.5% inhibition of activity with carboxymethyl cellulose, 13.5% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Mg2+
5 mM, 2.3fold activation of activity with carboxymethyl cellulose, 6.5% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Na+
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 6% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
NaN3
0.1%, 45.2% inhibition of activity with carboxymethyl cellulose, 12.25% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
N-bromosuccinamide
-
oxidation of one or two tryptophan residues by N-bromosuccinamide per enzyme molecule is sufficient to inhibit the enzyme activity completely
additional information
-
native XynA loses 80% activity after 90 min at 80°C and 70% activity at pH 10
-
Cu2+
5 mM, 1.6fold activation of activity with carboxymethyl cellulose, 16.4% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Fe2+
5 mM, 2.9fold activation of activity with carboxymethyl cellulose, 6.7% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Hg2+
-
6 mM, complete inhibition. Addition of 40 mM EDTA does not recover any lost activity
Pb2+
-
8 mM, 74% residual activity. Addition of 40 mM EDTA does not recover any lost activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetone
5%, 4.3fold activation of activity with carboxymethyl cellulose, slight activation of xylanase activity (to 104.6% of control), fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
butanol
5%, 1.1fold activation of activity with carboxymethyl cellulose, 73% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
EDTA
5 mM, 90.6% inhibition of activity with carboxymethyl cellulose, 1.1fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
glycerol
5%, 8.2fold activation of activity with carboxymethyl cellulose, 10% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
SDS
1%, 5.7fold activation of activity with carboxymethyl cellulose, 4.5fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
bagasse pulp
-
Thermomyces lanuginosus SSBP produces high level of cellulase-free xylanase during growth on a cheap bagasse pulp carbon source after 120 h
-
additional information
-
higher level of xylanase activity is obtained in solid-state cultures than in submerged cultures after 120 h with 10% inoculum
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
beechwood xylan
Km value is 17.7 mg/ml, pH 6.0, 60°C
-
additional information
beechwood xylan
Km-value: 60.6 mg/ml, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, pH 5.0, 70°C
-
additional information
carboxymethyl cellulose
Km-value: 6.8 mg/ml, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, pH 5.0, 70°C
-
additional information
oat spelt xylan
Km value is 10.9 mg/ml, pH 6.0, 60°C
-
additional information
birchwood xylan
-
Km value 3.26 mg/ml, pH 6.5, 50°C
-
additional information
oat spelt xylan
-
Km value of wild-type 0.112 mg/ml, of mutant M7 0.098 mg/ml, respectively, pH 6.0, 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
oat spelt xylan
-
kcat/Km value of wild-type 53279 ml/mg/s, of mutant M7 73048 ml/mg/s, respectively, pH 6.0, 50°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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 at a water activity between 0.91 and 0.83, 0.1 M sodium phosphate, pH 6.0, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
carboxymethyl cellulase activity of the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus and of the parental endoglucanase
7
xylanase activity of the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
carboxymethyl cellulase activity of the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus and of the parental endoglucanase
65
70
xylanase activity of the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
75
60
65
70
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
KU366607
optimization of xylanase production using agro-industrial substrates up to 132 U/ml. Pretreated rice straw yields 126.9 mg/g maximum fermentable sugars
physiological function
physiological function
-
maximum peaks of xylanase production and specific activity occurr after 96 hours of cultivation in liquid medium using 3% (w/v) corncob as substrate
physiological function
-
strain produces beta-xylanase activity of 59600 nkat/ml when cultivated on a medium containing corn cobs as substrate and yeast extract as nitrogen source, at pH 6.5 and 50°C. Lower beta-xylanase activities are produced after growth on other xylan substrates, sugars and soluble starch
physiological function
-
strain produces considerable amounts of extracellular hydrolytic enzymes on lignocellulosic substrates at 55°C incubated for 8 days in 150 ml shake flask experiments. The maximum enzyme activities on wheat straw and guayule bagasse are: xylanase 130.1 U/mg, inulinase 34.1 U/mg, carboxymethylcellulase 4.8 U/mg, filter paper assay (FPase) 5.5 FPU/g and pectinase 3.2 U/mg, respectively
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_THELA
225
0
24356
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75500
gel filtration, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
23600
24000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
x * 21900 or x * 22100 or x * 22300, mass spectrometry of recombinant protein with variability in the amino terminus, x * 26900, SDS-PAGE
monomer
-
1 * 22000, wild-type enzyme, SDS-PAGE, 1 * 24000, mutant enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
0.74% carbohydrate content of the wild-type enzyme, 11.8% of the mutant enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.55 A resolution. The central three sugar rings of the substrate are tightly bound, whereas the peripheral ones can assume different orientations and conformations. The thermostability is due to the presence of an extra disulfide bridge, as well as to an increase in the density of charged residues throughout the protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q1C/Q24C
introduction of disulfide bridge, leading to increase in temperature optimum at pH 6.5 by about 10 degrees to 75°C, increased resistance to thermal inactivation and increased melting temperature. At pH 8 and 70°C, the disulfide bridge increases the enzyme half-life 20fold in the presence of substrate
A54T
-
when exposed to 80°C for 90 min the mutant displays a low stability and retains only 10% of its activity. It is extremely alkali tolerant. After 90 min at pH 10 it retains 93% of its activity. It has catalytic activity almost comparable to the wild-type
K30E/W40R/T57A/K80R
-
thermostable mutant, when exposed to 80°C for 90 min it displays 75% retention of its total activity. The mutant loses nearly 60% of its activity under extremely alkaline conditions (after 90 min at pH 10). It has a much lower activity as compared to the wild-type
additional information
additional information
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
additional information
-
random mutagenesis leads to mutant M7 with improved kinetic and thermodynamic properties
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 12
8.3
-
wild-type and mutant enzymes, stable up to 24 h at 50°C, 60% remaining activity
655088
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
70
80
90
50
55
60
70
50
t1/2: 173 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
50
t1/2: 693 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
60
t1/2: 16 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
60
t1/2: 347 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
70
80 min, 60% remaining activity, native and recombinant enzyme
70
wild-type at pH 8.0, half-life 11 min in presence of substrate, 33 min in absence of substrate, respectively. Mutant Q1C/Q24C at pH 8.0, half-life 229 min in presence of substrate, 315 min in absence of substrate, respectively. Mutant Q1C/Q24C at pH 9.0, half-life 112 min in presence of substrate, 169 min in absence of substrate, respectively
70
t1/2: 15 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
70
t1/2: 231 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
80
40 min, 60% remaining activity, native and recombinant enzyme
80
t1/2: 12 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
80
t1/2: 63 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
90
t1/2: 12 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
90
t1/2: 20 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 2 month, enzyme becomes inactivated when stored in the dry state
-
-20°C, crude culture, 30 days, 15-20% loss of activity, maintaining stable thereafter for 5 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
recombinant enzyme from Pichia pastoris, and native enzyme, by gel filtration
native wild-type, 17fold, and mutant enzymes, to homogeneity by anion exchange chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus in Yarrowia lipolytica
gene XynA, overexpression in Pichia pastoris, method optimization, functional expression under control of the AOX1 promotor
xynA cloned from a genomic library into pBluescript. Extraneous fungal DNA upstream and downstream of xynA and the lacZ fusion partner removed by PCR. After PCR, cleavage and recloning, and the plasmid transformed into Escherichia coli XL1 Blue MRF'
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
rice bran supports the maximum production of endo-xylanase followed by wheat straw, canola meal and sunflower meal. Highest yields are 842, 840, 610 and 608 IU per g substrate consumed, respectively.
-
Thermomyces lanuginosus A72 shows xylanase activity (411 U/ml) on cane bagasse (1.0%) as carbon source, while Thermomyces lanuginosus YMN72 produces highest xylanase activity (428 U/ml) when grown on corn cobs (1.5%) as carbon source. Both strains reach a maximum value of xylanase activity at pH 6.6. Sodium nitrate (0.3 % w/v) is the best nitrogen source for Thermomyces lanuginosus A72, where xylanase activity reaches 563U/mg., ammonium nitrate (0.1% w/v) is the best nitrogen source for Thermomyces lanuginosus YMN72 giving 946U/ml. Gamma radiation increases xylanase production
-
using final optimized medium of 2% xylan, 0.6% meat peptone, 0.12% (NH4)2SO4 and 1.5% KH2PO4 in tap water, a catalytic activity of 9168-9502 nkat/ml medium can be obtained
-
xylanase production is induced by growth on wheat bran and xylan. Strain performs best at 80% initial moisture
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone
degradation
enzyme is able to degrade pulp and release substantial chromophoric materials and lignin derived compounds indicating its effective utility in pulp bleaching
industry
the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone
synthesis
optimization of recombinant enzyme production in 1-liter flasks. Initial cell density is the most important parameter. Under optimized conditions, 1498 mg xylanase per liter can be achieved
biofuel production
-
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently
degradation
industry
paper production
synthesis
-
alkali-pretreated roots of Taraxacum kok-saghyz (rubber dandelion), incubated with crude enzyme extracts from Thermomyces lanuginosus STm yield more natural rubber (90 mg/g dry root) than the protocols, Eskew process (24 mg/g) and commercial-enzyme-combination process (45 mg/g). The crude enzyme treatment at 91.6% rubber purity approaches the purity of the commercial-enzyme-combination process at 94.1% purity
additional information
-
simultaneous production of endoxylanase and oligosaccharides
degradation
-
degradation of alpha-amylase-treated wheat bran by xylanase solubilises about 20% of the fibre residue, i.e. 10% of the original bran. Amylase, protease and xylanase treatments alter the composition of the original bran, removing starch (100%), a portion of the non-starch glucan (39%), xylan (57%), arabinan (61%), ash (62%) and other components including protein (52%). Pre-extraction of enzymatically-hydrolysable starch and xylan reduces the release of furfural. Steam explosion of the lignocellulosic residue followed by cellulase treatment and conversion to ethanol at a high substrate concentration (19%) gives an ethanol titre ofabout 25 g/l or a yield of 93% of the theoretical maximum
degradation
-
maximum saccharification is obtained from treatment of cane bagasse by partially purified xylanase from Thermomyces lanuginosus A72 and Thermomyces lanuginosus YMN72 after 24 hrs of incubation. The maximum production of ethanol and xylitol is obtained after 48 and 24 h fermentation giving 22.48 g/l and 13.54 g/l, respectively, in enzyme broth of Thermomyces lanuginosus YMN72 using Candida tropicalis EMCC2
degradation
KU366607
optimization of xylanase production using agro-industrial substrates. Pretreated rice straw yields 126.9 mg/g maximum fermentable sugars
degradation
-
treatment of Eucalyptus kraft pulp with culture supernatant at 10 IU per gram pulp to enhance bleaching of kraft pulp results in a 10.5% reduction in Kappa number (indicating the amount of chemicals needed for bleaching pulps) and has a positive effect on the brightness of the resulting handsheets
industry
-
Thermomyces lanuginosus SSBP has potential applications due to its high productivity of xylanase and its efficiency in pulp bleaching
industry
-
variants with improved thermal and alkaline stability are ideal candidates for DNA shuffling experiments to produce a robust xylanase for industrial application
industry
-
xylanase has potential in bleach boosting and reducing the consumption elemental chlorine-free bleaching sequence. Effects produced are dependent on the enzyme and pulp type used. No correlation between the xylanase-induced brightness gains and possible savings of chlorine dioxide. Use of xylanases for pulp bleaching can boost pulp brightness or alternatively decrease the amounts of bleaching chemicals consumed, which in turn may result in respective reductions of the absorbable organic halogens and chloride levels of the bleach wastewaters and alleviate the environmental impact of the industry
REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kitpreechavanich, V.; Hayashi, M.; Nagai, S.
Purification and properties of endo-1,4-beta-xylanase from Humicola lanuginosa
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62
415-420
1984
Thermomyces lanuginosus
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Lin, J.; Ndlovu, L.M.; Singh, S.; Pillay, B.
Purification and biochemical characteristics of beta-D-xylanase from a thermophilic fungus, Thermomyces lanuginosus - SSBP
Biotechnol. Appl. Biochem.
30
73-79
1999
Thermomyces lanuginosus, Thermomyces lanuginosus SSBP
Damaso, M.C.T.; Almeida, M.S.; Kurtenbach, E.; Martins, O.B.; Pereira, N.Jr.; Andrade, C.M.M.C.; Albano, R.M.
Optimized expression of a thermostable xylanase from Thermomyces lanuginosus in Pichia pastoris
Appl. Environ. Microbiol.
69
6064-6072
2003
Thermomyces lanuginosus (O43097), Thermomyces lanuginosus, Thermomyces lanuginosus IOC-4145 (O43097), Thermomyces lanuginosus IOC-4145
Bakalova, N.G.; Petrova, S.D.; Atev, A.P.; Bhat, M.K.; Kolev, D.N.
Biochemical and catalytic properties of endo-1,4-beta-xylanases from Thermomyces lanuginosus (wild and mutant strains)
Biotechnol. Lett.
24
1167-1172
2002
Thermomyces lanuginosus
Stephens, D.E.; Rumbold, K.; Permaul, K.; Prior, B.A.; Singh, S.
Directed evolution of the thermostable xylanase from Thermomyces lanuginosus
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127
348-354
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Thermomyces lanuginosus
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
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2009
Aspergillus niger, Thermomyces lanuginosus, Trichoderma longibrachiatum
Manimaran, A.; Kumar, K.S.; Permaul, K.; Singh, S.
Hyper production of cellulase-free xylanase by Thermomyces lanuginosus SSBP on bagasse pulp and its application in biobleaching
Appl. Microbiol. Biotechnol.
81
887-893
2009
Thermomyces lanuginosus
Ziaie-Shirkolaee, Y.; Talebizadeh, A.; Soltanali, S.
Comparative study on application of T. lanuginosus SSBP xylanase and commercial xylanase on biobleaching of non wood pulps
Biores. Technol.
99
7433-7437
2008
Thermomyces lanuginosus, synthetic construct
Stephens, D.E.; Singh, S.; Permaul, K.
Error-prone PCR of a fungal xylanase for improvement of its alkaline and thermal stability
FEMS Microbiol. Lett.
293
42-47
2009
Thermomyces lanuginosus
Hernandez, A.; Lopez, J.C.; Santamaria, R.; Diaz, M.; Fernandez-Abalos, J.M.; Copa-Patino, J.L.; Soliveri, J.
Xylan-binding xylanase Xyl30 from Streptomyces avermitilis: cloning, characterization, and overproduction in solid-state fermentation
Int. Microbiol.
11
133-141
2008
Thermomyces lanuginosus, Streptomyces lividans, Streptomyces avermitilis (Q9X584), Streptomyces avermitilis, Streptomyces avermitilis CECT 3339 (Q9X584), Streptomyces avermitilis CECT 3339, Streptomyces lividans 66
Puchart, V.; Biely, P.
Simultaneous production of endo-beta-1,4-xylanase and branched xylooligosaccharides by Thermomyces lanuginosus
J. Biotechnol.
137
34-43
2008
Dickeya chrysanthemi, Thermomyces lanuginosus
Shrivastava, S.; Shukla, P.; Deepalakshmi, P.D.; Mukhopadhyay, K.
Characterization, cloning and functional expression of novel xylanase from Thermomyces lanuginosus SS-8 isolated from self-heating plant wreckage material
World J. Microbiol. Biotechnol.
29
2407-2415
2013
Thermomyces lanuginosus (O43097), Thermomyces lanuginosus SS-8 (O43097)
Anand, L.; Krishnamurthy, S.; Vithayathil, P.J.
Purification and properties of xylanase from the thermophilic fungus, Humicola lanuginosa (Griffon and Maublanc) Bunce
Arch. Biochem. Biophys.
276
546-553
1990
Thermomyces lanuginosus, Thermomyces lanuginosus Bunce
Damaso, M.C.; Almeida, M.S.; Kurtenbach, E.; Martins, O.B.; Pereira, N.; Andrade, C.M.; Albano, R.M.
Optimized expression of a thermostable xylanase from Thermomyces lanuginosus in Pichia pastoris
Appl. Environ. Microbiol.
69
6064-6072
2003
Thermomyces lanuginosus (O43097), Thermomyces lanuginosus
Gruber, K.; Klintschar, G.; Hayn, M.; Schlacher, A.; Steiner, W.; Kratky, C.
Thermophilic xylanase from Thermomyces lanuginosus high-resolution X-ray structure and modeling studies
Biochemistry
37
13475-13485
1998
Thermomyces lanuginosus (O43097), Thermomyces lanuginosus
Wang, Y.; Fu, Z.; Huang, H.; Zhang, H.; Yao, B.; Xiong, H.; Turunen, O.
Improved thermal performance of Thermomyces lanuginosus GH11 xylanase by engineering of an N-terminal disulfide bridge
Biores. Technol.
112
275-279
2012
Thermomyces lanuginosus (O43097), Thermomyces lanuginosus, Thermomyces lanuginosus DSM 10635 (O43097)
Kumar, V.; Chhabra, D.; Shukla, P.
Xylanase production from Thermomyces lanuginosus VAPS-24 using low cost agro-industrial residues via hybrid optimization tools and its potential use for saccharification
Biores. Technol.
243
1009-1019
2017
Thermomyces lanuginosus (KU366607), Thermomyces lanuginosus VAPS-24 (KU366607)
Lin, J.; Ndlovu, L.M.; Singh, S.; Pillay, B.
Purification and biochemical characteristics of beta-D-xylanase from a thermophilic fungus, Thermomyces lanuginosus-SSBP
Biotechnol. Appl. Biochem.
30
73-79
1999
Thermomyces lanuginosus, Thermomyces lanuginosus SSBP
Haarhoff, J.; Moes, C.; Cerff, C.; Van Wyk, W.; Gerischer, G.; Janse, B.
Characterization and biobleaching effect of hemicellulases produced by thermophilic fungi
Biotechnol. Lett.
21
415-420
1999
Thermomyces lanuginosus
-
Triches Damaso, M.; Carvalho Andrade, C.; Pereira Jr., N.
Production and properties of the cellulase-free xylanase from Thermomyces lanuginosus IOC-4145
Braz. J. Microbiol.
33
333-338
2002
Thermomyces lanuginosus, Thermomyces lanuginosus IOC-4145
-
Bennett, N.A.; Ryan, J.; Biely, P.; Vrsanska, M.; Kremnicky, L.; Macris, B.J.; Kekos, D.; Christakopoulos, P.; Katapodis, P.; Claeyssens, M.; Nerinckx, W.; Ntauma, P.; Bhat, M.K.
Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Thermomyces lanuginosus ATCC 46882
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306
445-455
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Thermomyces lanuginosus, Thermomyces lanuginosus ATCC 46882
Alam, M.; Gomes, I.; Mohiuddin, G.; Hoq, M.
Production and characterization of thermostable xylanases by Thermomyces lanuginosus and Thermoascus aurantiacus grown on lignocelluloses
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16
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1994
Thermomyces lanuginosus, Termitomyces aurantiacus
-
Wood, I.; Cook, N.; Wilson, D.; Ryden, P.; Robertson, J.; Waldron, K.
Ethanol from a biorefinery waste stream Saccharification of amylase, protease and xylanase treated wheat bran
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198
125-131
2016
Thermomyces lanuginosus
Sikandar, S.; Ujor, V.; Ezeji, T.; Rossington, J.; Michel, F.J.; McMahan, C.; Ali, N.; Cornish, K.
Thermomyces lanuginosus STm A source of thermostable hydrolytic enzymes for novel application in extraction of high-quality natural rubber from Taraxacum kok-saghyz (Rubber dandelion)
Ind. Crops Prod.
103
161-168
2017
Thermomyces lanuginosus, Thermomyces lanuginosus STm
-
Singh, S.; Pillay, B.; Dilsook, V.; Prior, B.A.
Production and properties of hemicellulases by a Thermomyces lanuginosus strain
J. Appl. Microbiol.
88
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2000
Thermomyces lanuginosus, Thermomyces lanuginosus SSBP
Gomes, J.; Gomes, I.; Kreiner, W.; Esterbauer, H.; Sinner, M.; Steiner, W.
Production of high level of cellulase-free and thermostable xylanase by a wild strain of Thermomyces lanuginosus using beechwood xylan
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30
283-297
1993
Thermomyces lanuginosus
-
Ali, U.; Ibrahim, Z.; Isaac, G.
Ethanol and xylitol production from xylanase broth of Thermomyces lanuginosus grown on some lignocellulosic wastes using Candida tropicalis EMCC2
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10
968-978
2013
Thermomyces lanuginosus
-
Rajoka, M.; Huma, T.; Khalid, A.; Latif, F.
Kinetics of enhanced substrate consumption and endo-beta-xylanase production by a mutant derivative of Humicola lanuginosa in solid-state fermentation
World J. Microbiol. Biotechnol.
21
869-876
2005
Thermomyces lanuginosus
-
Bokhari, S.; Latif, F.; Rajoka, M.
Purification and characterization of xylanases from Thermomyces lanuginosus and its mutant derivative possessing novel kinetic and thermodynamic properties
World J. Microbiol. Biotechnol.
25
493-502
2009
Thermomyces lanuginosus
-
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