Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
CtXynGH30 is a family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase
evolution
enzyme Xyn10B belongs to the glycoside hydrolase family 10, GH10
evolution
enzyme XynD belongs to the glycoside hydrolase family 10, GH10
evolution
the enzyme belongs to the CBM2 superfamily, glycoside hydrolase family 10, GH10
evolution
the enzyme belongs to the CBM2 superfamily, glycoside hydrolase family 11, GH11
evolution
the enzyme belongs to the glycoside hydrolase family 10, GH10
evolution
the enzyme belongs to the glycoside hydrolase family 10, GH10
evolution
the enzyme belongs to the glycoside hydrolase family 8, GH8
evolution
the enzyme belongs to the glycosyl hydrolase family 11, GH11
evolution
-
enzyme Xyn10B belongs to the glycoside hydrolase family 10, GH10
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 11, GH11
-
evolution
-
enzyme XynD belongs to the glycoside hydrolase family 10, GH10
-
evolution
-
the enzyme belongs to the CBM2 superfamily, glycoside hydrolase family 11, GH11
-
evolution
-
the enzyme belongs to the CBM2 superfamily, glycoside hydrolase family 10, GH10
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 10, GH10
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 10, GH10
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 11, GH11
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 8, GH8
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 10, GH10
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 10, GH10
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 11, GH11
-
evolution
-
enzyme Xyn10B belongs to the glycoside hydrolase family 10, GH10
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 10, GH10
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 8, GH8
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 10, GH10
-
metabolism
-
key enzyme in beta-1,4-xylan degradation, which involves several hydrolases, overview
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
metabolism
-
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
the gene xyl1 is important for the nematode to complete its life cycle
physiological function
-
the N-terminal domain A2 is responsible for both the thermostability and substrate-binding capacity of XynA
physiological function
-
two roles of Xyn5, localized on the cell surface, in water-insoluble xylan utilization: generation of the xylo-oligosaccharide inducers of all the xyn genes from water-insoluble xylan and attachment of the cells to the substrate so that the generated inducers can be immediately taken up by cells to activate expression of the xyn system, overview. Cell surface-bound Xyn5 is crucial for growth of strain W-61 in the water-insoluble xylan medium
physiological function
-
endo-beta-1,4-xylanase is one of the key enzymes of ethanol productivity during the consolidated bioprocessing of lignocellulosics
physiological function
-
endoxylanase is the key enzyme for xylan depolymerization, which attacks the main chain of xylan
physiological function
constitutive expression of enzyme gene in tall fescue in the vacuole, apoplast, and Golgi, results in only a small number of plants with low enzyme activities and in reduced plant growth in apoplast, and golgi targeted plants. Constitutive expression in the apoplast also results in increased levels of cell wall bound hydroxycinnamic acid monomers and dimers, but no significant effect on cell wall xylose or arabinose content. In situ constitutive xylanase expression in the Golgi also results in increased ferulate dimers. Senescence-induced xylanase expression in the apoplast is considerably higher and does not affect plant growth or the level of monomeric hydroxycinnamic acids or lignin in the cell walls. These plants also show increased levels of ferulate dimers, and decreased levels of xylose with increased levels of arabinose in their cell walls
physiological function
deletion of the gene encoding xylanase 11A reduces the growth rate of the mutant on minimal medium with xylan to 0.09 per h compared to 0.10 per h of the wild-type. The deletion mutant reaches a final OD600 of 6.78 compared to 8.18 in the wild-type culture. The drop of the pH value from initially 5.7 to 3.4 is approximately 3 h delayed in comparison to wild-type. Also the maximal concentration of reducing sugars in the medium is lower, and occurs 9 h later than in the wildtype culture. Heterologous expression of xylanase 11A on the cell surface of a xylanase-negative strain of Saccharomyces cerevisiae enables the strain to almost completely degrade xylan to xylotriose
physiological function
-
coexpression of vacuole- or apoplast-targeted ferulic acid esterase from Aspergillus niger and senescence-induced and apoplast-targeted beta-1,4 endo-xylanase from Trichoderma reesei in Festuca arundinacea. Xylanase activity in senescent leaves increases and ferulic acid esterase activity decreases after tillering. Plants coexpressing both enzymes in the apoplast, with the lowest levels of ferulate monomers and dimers and the lowest levels of cell wall arabinoxylans, release ten times more cell wall hydroxycinnamic acids and five times more arabinoxylan from the cell wall on autodigestion compared to expression of ferulic acid esterase or xylanase alone. These plants also show a 31% increase in cellulase-mediated release of reducing sugars, a 5% point increase in in vitro dry matter digestibility and a 23% increase in acetyl bromide-soluble lignin
physiological function
-
enzyme consists of a family 22 carbohydrate-binding module, a glycoside hydrolase family 10 catalytic domain, two fibronectin type III (Fn3) domains, and a family 3 carbohydrate-binding module at the C-terminus. The family 22 carbohydrate-binding module has an important role not only in binding to xylan and beta-glucan but also in feeding both polysaccharides into the neighboring GH10 catalytic domain
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
physiological function
-
highest xylanase production (208 IU/ml) in 96 h occurs using 1% rice bran as the only carbon source
physiological function
-
growth on oat spelt xylan is the most effective for xylanase production followed by beech wood or birch wood xylan
physiological function
-
highest titer of xylanase (5.5 IU/ml) is obtained b y growth on oat spelt xylan
physiological function
-
in solid state fermentation using lignocellulosic materials as substrates, Myceliophthora thermophila JCP 1-4 is the best producer of endoglucanase (357,51 U/g), beta-glucosidase (45.42 U/g), xylanase (93,11 U/g) and avicelase (3.58 U/g) among the strain tested
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 grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
physiological function
Thermothelomyces fergusii
-
strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
physiological function
-
strain produces 1044 U/g of carboxymethylcellulase in medium composed of a sugarcane bagasse and wheat bran mixture in 192 h of fermentation
physiological function
-
strain produces 7238 U/g of carboxymethylcellulase in medium composed of a sugarcane bagasse and wheat bran mixture in 192 h of fermentation
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
physiological function
endo-1,4-beta-xylanase is the most important arabinoxylan (AX) degrading enzyme, which cleaves the beta-xylosidic bond between two D-xylopyranosyl residues linked in beta-(1,4). Arabinoxylan (AX) is the main non-starch polysaccharide in wheat. Wheat malts are traditional raw materials for beer brewing. AX is divided into water-soluble arabinoxylan (WEAX) and water-insoluble arabinoxylan (WUAX). In the mashing stage of beer production, WUAX in malt is degraded by arabinoxylanase to WEAX, which is further degraded to smaller molecules and retained in the final beer
physiological function
endo-xylanase and beta-xylosidase are the major enzymes for hemicellulose hydrolysis, which play a significant role in biomass conversion
physiological function
high levels of expression and catalytic activity for XYN10Ks_480 during hydrolysis of xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides
physiological function
primary role in the degradation of marine polysaccharides
physiological function
-
the enzymatic hydrolysis of beechwood xylan and preprocessed agrowaste corncob leads to high release of xylotriose and xylobiose oligosaccharide (XOS). Xylobiose and xylotriose exhibit higher binding affinities with the BIAXP transporter protein of probiotic bacteria explaining their easy uptake by the cells. MIxed xylooligosaccharides are cytotoxic to HeLa cells. Bacillus licheniformis strain DM5 is attributed for the production of prebiotic and anti-inflammatory XOS from agrowaste
physiological function
the enzyme plays a primary role in the degradation of marine polysaccharides, potential of Teredinibacter turnerae for effective and diverse biomass degradation
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
-
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
-
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
-
high levels of expression and catalytic activity for XYN10Ks_480 during hydrolysis of xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides
-
physiological function
-
endo-beta-1,4-xylanase is one of the key enzymes of ethanol productivity during the consolidated bioprocessing of lignocellulosics
-
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
-
physiological function
-
strain produces 7238 U/g of carboxymethylcellulase in medium composed of a sugarcane bagasse and wheat bran mixture in 192 h of fermentation
-
physiological function
-
in solid state fermentation using lignocellulosic materials as substrates, Myceliophthora thermophila JCP 1-4 is the best producer of endoglucanase (357,51 U/g), beta-glucosidase (45.42 U/g), xylanase (93,11 U/g) and avicelase (3.58 U/g) among the strain tested
-
physiological function
-
deletion of the gene encoding xylanase 11A reduces the growth rate of the mutant on minimal medium with xylan to 0.09 per h compared to 0.10 per h of the wild-type. The deletion mutant reaches a final OD600 of 6.78 compared to 8.18 in the wild-type culture. The drop of the pH value from initially 5.7 to 3.4 is approximately 3 h delayed in comparison to wild-type. Also the maximal concentration of reducing sugars in the medium is lower, and occurs 9 h later than in the wildtype culture. Heterologous expression of xylanase 11A on the cell surface of a xylanase-negative strain of Saccharomyces cerevisiae enables the strain to almost completely degrade xylan to xylotriose
-
physiological function
-
primary role in the degradation of marine polysaccharides
-
physiological function
-
the enzyme plays a primary role in the degradation of marine polysaccharides, potential of Teredinibacter turnerae for effective and diverse biomass degradation
-
physiological function
-
endo-xylanase and beta-xylosidase are the major enzymes for hemicellulose hydrolysis, which play a significant role in biomass conversion
-
physiological function
-
enzyme consists of a family 22 carbohydrate-binding module, a glycoside hydrolase family 10 catalytic domain, two fibronectin type III (Fn3) domains, and a family 3 carbohydrate-binding module at the C-terminus. The family 22 carbohydrate-binding module has an important role not only in binding to xylan and beta-glucan but also in feeding both polysaccharides into the neighboring GH10 catalytic domain
-
physiological function
-
the enzymatic hydrolysis of beechwood xylan and preprocessed agrowaste corncob leads to high release of xylotriose and xylobiose oligosaccharide (XOS). Xylobiose and xylotriose exhibit higher binding affinities with the BIAXP transporter protein of probiotic bacteria explaining their easy uptake by the cells. MIxed xylooligosaccharides are cytotoxic to HeLa cells. Bacillus licheniformis strain DM5 is attributed for the production of prebiotic and anti-inflammatory XOS from agrowaste
-
physiological function
-
strain produces 1044 U/g of carboxymethylcellulase in medium composed of a sugarcane bagasse and wheat bran mixture in 192 h of fermentation
-
physiological function
-
strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
-
physiological function
Thermothelomyces fergusii MTCC 9293
-
strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
-
physiological function
-
endoxylanase is the key enzyme for xylan depolymerization, which attacks the main chain of xylan
-
physiological function
-
primary role in the degradation of marine polysaccharides
-
physiological function
-
the enzyme plays a primary role in the degradation of marine polysaccharides, potential of Teredinibacter turnerae for effective and diverse biomass degradation
-
physiological function
-
highest xylanase production (208 IU/ml) in 96 h occurs using 1% rice bran as the only carbon source
-
additional information
several sequence and structure modifications appears to be responsible for the acidophilic characteristic of XYL1p 1. The presence of an aspartic acid H bonded to the acid/base catalyst 2. the nature of specifically conserved residues in the active site 3. the negative potential at the surface 4. the decreased number of salt bridges and H bonds in comparison with highly alkaline enzymes
additional information
-
specific activity of purified recombinant XynS14, expressed in Pichia pastoris, is 2.4fold higher than recombinant XynS14, expressed in Escherichia coli
additional information
-
the enzyme shows a high salt tolerance
additional information
the N-terminal domain of the enzyme is required for catalytic activity
additional information
-
the N-terminal domain of the enzyme is required for catalytic activity
additional information
XynD possesses four catalytic subsites with a high energy of interaction with the substrate and a fifth subsite with a small energy of interaction
additional information
-
XynD possesses four catalytic subsites with a high energy of interaction with the substrate and a fifth subsite with a small energy of interaction
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%
additional information
multiple template-based enzyme structure homology modeling
additional information
multiple template-based enzyme structure homology modeling
additional information
Thermochaetoides thermophila
the enzyme belongs to the glycosyl hydrolase family 7, GH7. Residue Glu197 acts as the active-site nucleophile and Glu202 is the acid-base catalyst, and this is consistent with a catalytic mechanism leading to a net retention of configuration at the anomeric carbon in the deep substrate binding cleft
additional information
the enzyme has six catalytically relevant subsites, structural analysis of substrate-binding sites and the distortions of xylose within the catalytic centre, overview. Enzymatic glycoside hydrolysis involves the distortion of the reactive, -1 subsite, sugar into a variety of skew-boat and boat conformations, reflecting the requirements of inline attack and the stereoelectronic requirements of an oxocarbenium-ion-like transition state
additional information
-
the enzyme has six catalytically relevant subsites, structural analysis of substrate-binding sites and the distortions of xylose within the catalytic centre, overview. Enzymatic glycoside hydrolysis involves the distortion of the reactive, -1 subsite, sugar into a variety of skew-boat and boat conformations, reflecting the requirements of inline attack and the stereoelectronic requirements of an oxocarbenium-ion-like transition state
additional information
-
the enzyme is immobilized and stabilized on glyoxyl-agarose beads by multipoint covalent attachment using a novel strategy based on surface coating with a multilayer of polymers. The optimal modification consists of surface coating with a bilayer formed by a layer of derived dextran polymers and a layer of polyethylenimine
additional information
the enzyme is immobilized and stabilized on glyoxyl-agarose beads by multipoint covalent attachment using a novel strategy based on surface coating with a multilayer of polymers. The optimal modification consists of surface coating with a bilayer formed by a layer of derived dextran polymers and a layer of polyethylenimine
additional information
XYN10Ks_480 is an endo-1,4-beta-xylanase with a ricin-type beta-trefoil type of domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
additional information
XYN10Ks_480 is an endo-1,4-beta-xylanase with a ricin-type beta-trefoil type of domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
additional information
-
XYN10Ks_480 is an endo-1,4-beta-xylanase with a ricin-type beta-trefoil type of domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
additional information
XYN11Ks_480 is an endo-1,4-beta-xylanase with an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (psoition 165) catalyst and the other acts as a nucleophile (position 273)
additional information
XYN11Ks_480 is an endo-1,4-beta-xylanase with an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (psoition 165) catalyst and the other acts as a nucleophile (position 273)
additional information
-
XYN11Ks_480 is an endo-1,4-beta-xylanase with an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (psoition 165) catalyst and the other acts as a nucleophile (position 273)
additional information
Thermochaetoides thermophila IMI 039719
-
the enzyme belongs to the glycosyl hydrolase family 7, GH7. Residue Glu197 acts as the active-site nucleophile and Glu202 is the acid-base catalyst, and this is consistent with a catalytic mechanism leading to a net retention of configuration at the anomeric carbon in the deep substrate binding cleft
-
additional information
-
multiple template-based enzyme structure homology modeling
-
additional information
-
XYN11Ks_480 is an endo-1,4-beta-xylanase with an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (psoition 165) catalyst and the other acts as a nucleophile (position 273)
-
additional information
-
XYN10Ks_480 is an endo-1,4-beta-xylanase with a ricin-type beta-trefoil type of domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
-
additional information
Thermochaetoides thermophila DSM 1495
-
the enzyme belongs to the glycosyl hydrolase family 7, GH7. Residue Glu197 acts as the active-site nucleophile and Glu202 is the acid-base catalyst, and this is consistent with a catalytic mechanism leading to a net retention of configuration at the anomeric carbon in the deep substrate binding cleft
-
additional information
-
the enzyme shows a high salt tolerance
-
additional information
-
the enzyme is immobilized and stabilized on glyoxyl-agarose beads by multipoint covalent attachment using a novel strategy based on surface coating with a multilayer of polymers. The optimal modification consists of surface coating with a bilayer formed by a layer of derived dextran polymers and a layer of polyethylenimine
-
additional information
Thermochaetoides thermophila CBS 144.50
-
the enzyme belongs to the glycosyl hydrolase family 7, GH7. Residue Glu197 acts as the active-site nucleophile and Glu202 is the acid-base catalyst, and this is consistent with a catalytic mechanism leading to a net retention of configuration at the anomeric carbon in the deep substrate binding cleft
-
additional information
-
multiple template-based enzyme structure homology modeling
-
additional information
-
the enzyme has six catalytically relevant subsites, structural analysis of substrate-binding sites and the distortions of xylose within the catalytic centre, overview. Enzymatic glycoside hydrolysis involves the distortion of the reactive, -1 subsite, sugar into a variety of skew-boat and boat conformations, reflecting the requirements of inline attack and the stereoelectronic requirements of an oxocarbenium-ion-like transition state
-
additional information
-
specific activity of purified recombinant XynS14, expressed in Pichia pastoris, is 2.4fold higher than recombinant XynS14, expressed in Escherichia coli
-
additional information
-
multiple template-based enzyme structure homology modeling
-
additional information
-
the enzyme has six catalytically relevant subsites, structural analysis of substrate-binding sites and the distortions of xylose within the catalytic centre, overview. Enzymatic glycoside hydrolysis involves the distortion of the reactive, -1 subsite, sugar into a variety of skew-boat and boat conformations, reflecting the requirements of inline attack and the stereoelectronic requirements of an oxocarbenium-ion-like transition state
-