Information on EC 3.2.1.32 - endo-1,3-beta-xylanase

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

EC NUMBER
COMMENTARY
3.2.1.32
-
RECOMMENDED NAME
GeneOntology No.
endo-1,3-beta-xylanase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
random endohydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
(1,3)-beta-D-xylan degradation
-
SYSTEMATIC NAME
IUBMB Comments
3-beta-D-xylan xylanohydrolase
This enzyme is found mostly in marine bacteria, which break down the beta(1,3)-xylan found in the cell wall of some green and red algae. The enzyme produces mainly xylobiose, xylotriose and xylotetraose.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1,3-beta-xylanase
-
-
-
-
1,3-xylanase
-
-
-
-
beta-1,3-xylanase
-
-
-
-
beta-1,3-xylanase
-
-
beta-1,3-xylanase
D5MP61
-
beta-1,3-xylanase
Vibrio sp. AX4
-
-
-
endo-1,3-beta-xylanase
-
-
-
-
endo-1,3-xylanase
-
-
-
-
TxyA
Q8RS40
-
TxyA
Q8RS40
-
-
TxyA
Q9LCB9
-
TxyA
Q9LCB9
-
-
XYL4
-
-
XYL4
D5MP61
-
xylanase
-
-
-
-
xylanase, endo-1,3-
-
-
-
-
endo-beta-1,3-xylanase
-
-
-
-
additional information
D5MP61
XYL4 is a modular enzyme composed of an N-terminal catalytic module belonging to glycoside hydrolase family 26 and two putative carbohydrate-binding modules belonging to family 31 in the C-terminal region
CAS REGISTRY NUMBER
COMMENTARY
9025-55-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain XY-234
-
-
Manually annotated by BRENDA team
strain XY-234, enzyme TxyA, family 26 of glycosyl hydrolases
SwissProt
Manually annotated by BRENDA team
XY-234
-
-
Manually annotated by BRENDA team
strain XY-234
-
-
Manually annotated by BRENDA team
strain XY-234, enzyme TxyA, family 26 of glycosyl hydrolases
SwissProt
Manually annotated by BRENDA team
Aspergillus terreus A-07
A-07
-
-
Manually annotated by BRENDA team
No. C-59-2
-
-
Manually annotated by BRENDA team
Bacillus sp. No. C-59-2
No. C-59-2
-
-
Manually annotated by BRENDA team
CCMI 966, enzyme Xyl II
-
-
Manually annotated by BRENDA team
CCMI 966, enzymes alkaline Xyl I, neutral Xyl II
-
-
Manually annotated by BRENDA team
Pseudomonas sp. PT-5
PT-5
-
-
Manually annotated by BRENDA team
strain AX-4
-
-
Manually annotated by BRENDA team
strain AX4
-
-
Manually annotated by BRENDA team
gene xyl4
UniProt
Manually annotated by BRENDA team
Vibrio sp. AX4
strain AX4
-
-
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
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
action pattern of type I occurs in the hydrolysis by enzyme form EF-1, EF-2 and EF-5: beta-1,3-xylobiose, beta-1,3-xylotriose, beta-1,3-xylotetraose and an unknown disaccharide are liberated. The action pattern of type II occurs during hydrolysis by enzyme form EF-4 and EF-6. In the initial stage the enzyme produces mainly beta-1,2-xylobiose, beta-1,3-xylotriose and beta-1,3-xylotetraose. As hydrolysis proceeds an isomeric xylotriose is detectable as well as xylose, beta-1,3-xylobiose, beta-1,3-xylotriose and beta-1,3-xylotetraose
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
Vibrio sp. AX4
-
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
Pseudomonas sp. PT-5
-
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
Bacillus sp. No. C-59-2
-
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
Aspergillus terreus A-07
-
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
Aspergillus terreus A-07
-
action pattern of type I occurs in the hydrolysis by enzyme form EF-1, EF-2 and EF-5: beta-1,3-xylobiose, beta-1,3-xylotriose, beta-1,3-xylotetraose and an unknown disaccharide are liberated. The action pattern of type II occurs during hydrolysis by enzyme form EF-4 and EF-6. In the initial stage the enzyme produces mainly beta-1,2-xylobiose, beta-1,3-xylotriose and beta-1,3-xylotetraose. As hydrolysis proceeds an isomeric xylotriose is detectable as well as xylose, beta-1,3-xylobiose, beta-1,3-xylotriose and beta-1,3-xylotetraose
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
-
-
-
-
?
beta-1,3-xylan + H2O
?
show the reaction diagram
D5MP61
-
-
-
?
beta-1,3-xylan + H2O
?
show the reaction diagram
-
enzyme production is induced by beta-1,3-xylan
-
-
-
beta-1,3-xylan + H2O
?
show the reaction diagram
-, Q8RS40
hydrolysis and specific binding to
-
-
?
beta-1,3-xylan + H2O
?
show the reaction diagram
Q8RS40
hydrolysis and specific binding to
-
-
?
beta-1,3-xylan + H2O
disaccharides + trisaccharides + tetrasaccharides
show the reaction diagram
-
-
disaccharides, trisaccharides and tetrasaccharides are the major products, whereas the monosaccharides, pentasaccharides and oligosaccharides with more than five xylose units are produces at small quantities
-
?
beta-1,3-xylan + H2O
beta-1,3-D-xylobiose
show the reaction diagram
Q9LCB9
-
main product, with D-xylose and beta-1,3-D-xylotriose as minor products
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
-
?
glycol-beta-1,3-xylan + H2O
xylose + ?
show the reaction diagram
-
-
-
-
?
rhodymenan + H2O
beta-1,4-xylotriose + beta-1,4-linked xylooligosaccharides
show the reaction diagram
Aspergillus terreus, Aspergillus terreus A-07
-
-
beta-1,4-xylotriose and trace amounts of other beta-1,4-linked xylooligosaccharides
?
xylan (birchwood) + H2O
xylotetraose + ?
show the reaction diagram
-
-
xylotetraose is main product of xylan degradation
-
?
xylan (larchwood) + H2O
xylotetraose + ?
show the reaction diagram
-
-
xylotetraose is main product of xylan degradation
-
?
xylan (oat spelts) + H2O
xylotetraose + ?
show the reaction diagram
-
-
xylotetraose is main product of xylan degradation
-
?
xylopentaose + H2O
xylose + xylotetraose + xylobiose + xylotriose
show the reaction diagram
-
-
-
?
xylopentaose + H2O
xylose + xylotetraose + xylobiose + xylotriose
show the reaction diagram
-
-
small amounts of xylobiose and xylotriose
?
xylopentaose + H2O
xylose + xylotetraose + xylobiose + xylotriose
show the reaction diagram
-
-
-
?
xylopentaose + H2O
xylose + ?
show the reaction diagram
-
-
-
-
?
xylotetraose + H2O
xylose + xylotriose + xylobiose
show the reaction diagram
-
-
-
?
xylotetraose + H2O
xylose + xylotriose + xylobiose
show the reaction diagram
-
-
small amount of xylobiose
?
xylotetraose + H2O
xylose + xylotriose + xylobiose
show the reaction diagram
-
-
-
?
xylotetraose + H2O
xylose + ?
show the reaction diagram
-
-
-
-
?
xylotriose + H2O
xylose + xylobiose
show the reaction diagram
-
-
-
?
xylotriose + H2O
xylose + xylobiose
show the reaction diagram
-
-
-
?
xylotriose + H2O
xylose + xylobiose
show the reaction diagram
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no hydrolysis of xylobiose and p-nitrophenyl-beta-D-xyloside
-
-
-
additional information
?
-
-
does not act on xylobiose
-
-
-
additional information
?
-
-, Q8RS40
no substrate: beta-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan, beta-1,4-mannan
-
-
-
additional information
?
-
D5MP61
XYL4, an endo-type enzyme, contains two putative carbohydrate-binding modules, CBMs, belonging to family 31 in the C-terminal region. Repeating CBMs bind specifically to insoluble beta-1,3-xylan, but not to beta-1,4-xylan, Avicel, beta-1,4-mannan, curdlan, chitin or soluble glycol-beta-1,3-xylan, through hydrophobic interaction. Binding specificities of XYL4 and its mutants, overview
-
-
-
additional information
?
-
-
no hydrolysis of xylobiose and p-nitrophenyl-beta-D-xyloside
-
-
-
additional information
?
-
Q8RS40
no substrate: beta-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan, beta-1,4-mannan
-
-
-
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
beta-1,3-xylan + H2O
?
show the reaction diagram
D5MP61
-
-
-
?
beta-1,3-xylan + H2O
?
show the reaction diagram
-
enzyme production is induced by beta-1,3-xylan
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
activates
Mg2+
-
activates
NaCl
D5MP61
both the enzyme and the binding activities for insoluble beta-1,3-xylan but not soluble glycol-beta-1,3-xylan, are enhanced by NaCl
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ag+
-
1 mM, over 90% inhibition
Al3+
-
1 mM AlCl3, strong
Cu2+
-
1 mM CuCl2, strong
Cu2+
-
1 mM, complete inhibition
Cu2+
-
1 mM
dithiothreitol
-
-
Fe3+
-
1 mM, complete inhibition
-
Fe3+
-
1 mM FeCl3, strong
-
Fe3+
-
-
-
Hg2+
-
1 mM, strong inhibition
Hg2+
-
1 mM, strong
Hg2+
-
1 mM, complete inhibition
Mn2+
-
1 mM, strong inhibition
Mn2+
-
1 mM
N-bromosuccinimide
-
1 mM, strong inhibition
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
1 mM, complete inhibition
Pb(CH3COO)2
-
1 mM, strong
Pb2+
-
1 mM, over 90% inhibition
Pb2+
-
1 mM
Zn2+
-
1 mM, over 90% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
activates
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.75
-
xylopentaose
-
pH 7.5, 37C
0.74
-
xylotetraose
-
pH 7.5, 37C
additional information
-
additional information
-
-
-
additional information
-
additional information
D5MP61
binding specificities and dissociation constants of XYL4 and its mutants with different polysaccharides and glycol-beta-1,3-xylan and beta-1,3-xylan, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
14000
-
xylopentaose
-
pH 7.5, 37C
350
-
xylotetraose
-
pH 7.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.7
-
-
-
6.4
-
-
enzyme form EF-3 and EF-5
8.5
-
-
enzyme form EF-4
9.3
-
-
enzyme form EF-2
9.9
-
-
-
13.3
-
-
enzyme form EF-6
13.6
-
-
-
15.2
-
-
enzyme form EF-1
17.5
-
-
-
35
-
-
-
207
-
-
xylan (oat spelts), pH 6.0, 30C
225
-
-
xylan (birchwood), pH 6.0, 30C
226
-
-
laminarin, pH 6.0, 30C
253
-
-
xylan (larchwood), pH 6.0, 30C
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
enzyme form EF-4
4.5
-
-
enzyme forms EF-5 and EF-6
5
-
-
enzyme forms EF-1 and EF-3
5.5
-
-
enzyme form EF-2
6
6.5
-
-
6
7.5
-
-
7
7.5
-
-
7
-
-
-
7.5
-
D5MP61
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
10
-
about 50% of maximal activity at pH 4.0 and at pH 10.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
D5MP61
assay at
40
-
-
enzyme form EF-4 and EF-5
45
-
-
enzyme form EF-2
50
-
-
enzyme form EF-3 and EF-6
55
-
-
enzyme form EF-1
60
-
-
-
60
-
-
activity increases with temperature, denaturation above
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
70
-
about 20% of maximal activity at 30C and at 70C
37
60
-
37C: optimum, 60C: does not hydrolyze beta-1,3-xylan above 60C at pH 7.5
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.6
4.7
-
or higher, enzyme Xyl I
7.5
-
-
enzyme Xyl II
7.5
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Aspergillus terreus A-07, Bacillus subtilis CCMI 966
-
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
36000
-
-
gel filtration
53000
-
-
gel filtration
340000
-
-
PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 59000, SDS-PAGE
?
-
x * 52000, SDS-PAGE
?
Q9LCB9
x * 49264, calculated
?
-
x * 59000, SDS-PAGE
-
?
-
x * 49264, calculated; x * 52000, SDS-PAGE
-
monomer
-
1 * 35000, SDS-PAGE
multimer
-
x * 20000, SDS-PAGE, x * 20000-24000, gel filtration
monomer
Pseudomonas sp. PT-5
-
1 * 35000, SDS-PAGE
-
additional information
Q8RS40
contains a novel carbohydrate-binding module
additional information
-
enzyme shows no xylan-binding domain
additional information
D5MP61
XYL4 is a modular enzyme composed of an N-terminal catalytic module belonging to glycoside hydrolase family 26 and two putative carbohydrate-binding modules belonging to family 31 in the C-terminal region, sequence determination, overview
additional information
-
contains a novel carbohydrate-binding module
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
Q8RS40
contains a signal peptide of 22 amino acids
proteolytic modification
-
contains a signal peptide of 22 amino acids
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
structure of recombinant carbohydrate-binding module of beta-1,3-xylanase is determined at a resolution of 1.25 A
-
to 1.8 A resolution, space group P21
-
sitting-drop and hanging-drop vapour-diffusion method, crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 51.6 A, b = 75.8 A, c = 82.0 A. X-ray diffraction data are collected to 1.44 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
6
-
30C, 1 h, stable
4
-
-
4C, 24 h, 35% loss of activity
4.5
10
-
4C, 20 h, stable
5
8
-
4C, 20 h, stable
5
9
-
50C, 10 min, stable
5.5
8
-
4C, 20 h, stable
6
10
-
4C, 24 h, enzyme retains 90-100% of activity
7
7.5
-
60C, 10 min, stable
8
-
-
30C, 1 h, almost all activity is lost
12
-
-
4C, 24 h, retains 70% of its activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
stable below
40
-
-
pH 6.0, 15 min, stable below
40
-
-
pH 7.5, 10 min, stable below
40
-
-
180 min, stable
50
-
-
pH 4.5, 1 h, enzyme forms EF-5 and EF-6, stable up to
50
-
-
pH 7.5, 10 min, 70% loss of activity
50
-
-
92 min, 50% loss of activity
55
-
-
pH 6.0, 15 min, complete loss of activity
60
-
-
pH 4.5, 1 h, enzyme forms EF-1, EF-2, EF-3 and EF-4 are stable, enzyme form EF-5 and EF-6 rapidly lose activity
60
-
-
pH 7.5, 10 min, 99% loss of activity
60
-
-
Xyl I, 3 h, 20% of initial activity; Xyl I, 3 h, presence of 0.5 M trehalose, 50% of initial activity; Xyl II, 3 h, complete inactivation; Xyl II, 3 h, presence of 0.5 M trehalose, 50% of initial activity
60
-
-
20 min, 50% loss of activity
70
-
-
pH 4.5, 1 h, rapid decrease of activity of enzyme forms EF-1, EF-2, EF-3 and EF-4
70
-
-
Xyl I, 3 h, no activity; Xyl I, 3 h, presence of 0.5 M trehalose, 36% of initial activity; Xyl II, 3 h, presence of 0.5 M trehalose, 50% of initial activity
70
-
-
8 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ca2+ stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, stable for more than 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
6 different enzyme forms: EF-1, EF-2, EF-3, EF-4, EF-5 and EF-6
-
recombinant
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL2(DE3) by nickel affinity and beta-1,3-xylan affinity chromatography and gel filtration
D5MP61
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expressed in Escherichia coli BL21(DELTADE3)pLysS cells
-
expression in Escherichia coli
Q9LCB9
expression in Escherichia coli DH5alpha
-
wild-type and mutant enzymes are expressed in Escherichia coli
-
gene xyl4, DNA and amino acid sequence determination and comparison, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
D5MP61
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E138D
-
activity is extremely low
E138Q
-
inactive mutant
E234D
-
activity is extremely low
additional information
Q8RS40
analysis of truncated enzyme lacking N- or C-terminus, locates the carbohydrate-bindung module between residues 376 and 469
additional information
-
analysis of truncated enzyme lacking N- or C-terminus, locates the carbohydrate-bindung module between residues 376 and 469
-
E234Q
-
inactive mutant
additional information
D5MP61
construction of five different XYL4 deletion mutants, CBM-1, CBM-2, CBM-1-2, CM-CBM-1, and CM, possessing a catalytic module
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
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the enzyme may be an essential component for the preparation of protoplasts from some groups of seaweed
synthesis
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preparation of a large number of protoplasts are isolated from Porphyra yezoensis, Phorphyra tenera, and Bangia atropurpurea
synthesis
Q9LCB9
production of D-ylulose from beta-1,3-xylan, of the killer alga Caulerpa taxifolia. The synergistic action of beta-1,3-xylanase TxyA and beta-1,3-xylosidase XloA from Vibrio sp. strain XY-214 enables efficient saccharification of beta-1,3-xylan to D-xylose. D-Xylose is then converted to D-xylulose by using XylA
synthesis
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preparation of a large number of protoplasts are isolated from Porphyra yezoensis, Phorphyra tenera, and Bangia atropurpurea; production of D-ylulose from beta-1,3-xylan, of the killer alga Caulerpa taxifolia. The synergistic action of beta-1,3-xylanase TxyA and beta-1,3-xylosidase XloA from Vibrio sp. strain XY-214 enables efficient saccharification of beta-1,3-xylan to D-xylose. D-Xylose is then converted to D-xylulose by using XylA
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