3.2.1.37: xylan 1,4-beta-xylosidase
This is an abbreviated version!
For detailed information about xylan 1,4-beta-xylosidase, go to the full flat file.
Word Map on EC 3.2.1.37
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3.2.1.37
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xylans
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xylose
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arabinose
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arabinoxylans
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xylobiose
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xylooligosaccharides
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niger
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trichoderma
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p-nitrophenyl
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xylanolytic
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cellulase
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xylanases
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hemicellulases
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endoxylanase
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arabinans
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reesei
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spelt
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beta-d-xylopyranoside
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endoglucanase
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saccharification
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cellobiohydrolase
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p-nitrophenyl-beta-d-xylopyranoside
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pumilus
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beta-d-galactosidase
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xylan-degrading
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beta-xylanase
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arabinosidase
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alpha-fucosidase
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avicel
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birchwood
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beta-d-fucosidase
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cmcases
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thermoanaerobacterium
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alpha-glucuronidase
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thermomonospora
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xylopyranosyl
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saccharolyticum
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ruminantium
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xylotetraose
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hemicellulolytic
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feruloyl
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alpha-d-mannosidase
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fibrisolvens
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endo-1,4-beta-xylanase
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selenomonas
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glucuronoxylans
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hemicellulosic
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nutrition
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degradation
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synthesis
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food industry
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analysis
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biotechnology
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xylanohydrolase
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biofuel production
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agriculture
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alpha-d-galactosidase
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industry
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l-arabitol
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pharmacology
- 3.2.1.37
- xylans
- xylose
- arabinose
- arabinoxylans
- xylobiose
- xylooligosaccharides
- niger
- trichoderma
- p-nitrophenyl
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xylanolytic
- cellulase
- xylanases
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hemicellulases
- endoxylanase
- arabinans
- reesei
- spelt
- beta-d-xylopyranoside
- endoglucanase
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saccharification
- cellobiohydrolase
- p-nitrophenyl-beta-d-xylopyranoside
- pumilus
- beta-d-galactosidase
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xylan-degrading
- beta-xylanase
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arabinosidase
- alpha-fucosidase
- avicel
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birchwood
- beta-d-fucosidase
- cmcases
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thermoanaerobacterium
- alpha-glucuronidase
- thermomonospora
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xylopyranosyl
- saccharolyticum
- ruminantium
- xylotetraose
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hemicellulolytic
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feruloyl
- alpha-d-mannosidase
- fibrisolvens
- endo-1,4-beta-xylanase
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selenomonas
- glucuronoxylans
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hemicellulosic
- nutrition
- degradation
- synthesis
- food industry
- analysis
- biotechnology
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xylanohydrolase
- biofuel production
- agriculture
- alpha-d-galactosidase
- industry
- l-arabitol
- pharmacology
Reaction
Synonyms
1,4-beta-D-xylan xylohydrolase, 1,4-beta-D-xylosidase, 1.4-beta-D-xylanase, exo-type, ABF3, AbfA, AbfB, AbXyl, alpha-arabinofuranosidase/beta-xylosidase, alpha-L-arabinofuranosidase, alpha-L-arabinofuranosidase 3, alpha-L-arabinofuranoside arabinofuranohydrolase, arabinofuranosidase 3, AXH-d3, Axy43A, BcXyl, beta-1,4-xylosidase, beta-D-xylopyranosidase, beta-D-xylosidase, beta-D-xylosidase/alpha-L-arabinofuranosidase, beta-D-xyloside xylohydrolase, beta-glucosidase/xylosidase, beta-xylosidase, beta-xylosidase A, beta-xylosidase B, beta-xylosidase I, beta-xylosidase II, beta-xylosidase-1, beta-xylosidase-2, beta-xylosidase-3, beta-xylosidase-4, betaXTE, betaXTR, bifunctional beta-glucosidase/xylosidase, BlxA, Bxl1, BxTW1, Bxyl, ccxyl3a, EcXyl43 beta-xylosidase, exo-1,4-beta-D-xylosidase, exo-1,4-beta-xylosidase, Exo-beta-(1,4)-xylanase, GH43 beta-1,4-xylosidase, GH43 xylosidase, GH43B6, glycoside hydrolase family 3 beta-xylosidase, More, Pae1263, RrXyl43A, Rubg3A, Rubg3B, RuBGX1, RuXyn1, SSO3032, Sxa, Thxyl43A, Tpexyl3, X12345, Xln-DT, Xyl, Xyl I, XYL1, Xyl3A, XYL4, xyl43, xyl43A, Xyl43C, Xyl5, XYLA, Xylan 1,4-beta-xylosidase, xylanase, XylB, XylC, XylCD2, xylobiase, xylosidase, XynB, XynB2, XynB3
ECTree
3.2.1.37 xylan 1,4-beta-xylosidaseAdvanced search results
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Application on EC 3.2.1.37 - xylan 1,4-beta-xylosidase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
analysis
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comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major
biofuel production
biotechnology
degradation
food industry
industry
nutrition
pharmacology
synthesis
additional information
agriculture
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the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
agriculture
Weissella cibaria FB069
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the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
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biofuel production
a tailored enzymatic cocktail of alpha-glucuronidase (Agu115) from Schizophyllum commune with alpha-L-arabinofuranosidase (AbfA), xylanase (Xyn10C) and beta-xylosidase (XynB) achieves efficient hydrolysis of softwood xylans, which is instrumental for material- and cost-efficient processes for the generation of biofuels from lignocellulose-based streams. Cooperative enzymatic activities have important significance for enhancing the release of fermentable sugars and therefore generate an attractive sugar platform from lignocellulosic biomass to produce products such as bioethanol by fermentation, and for the production of hemicellulosic polymers and oligosaccharides with tailored molecular structures for material applications
biofuel production
application of this recombinant beta-xylosidase together with xylanase improves xylan hydrolysis efficiency, thus leading to increased biofuels productivity
biofuel production
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the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
biofuel production
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the enzyme has great potential for applications in the bioconversion of lignocellulose to sugars, fuel ethanol and chemicals
biofuel production
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the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production
biofuel production
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the enzyme has great potential for applications in the bioconversion of lignocellulose to sugars, fuel ethanol and chemicals
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biofuel production
Aspergillus niger DSM 22593
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the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production
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biofuel production
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the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
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biofuel production
Ceratocystis fimbriata RM 35
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the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
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biotechnology
coexpression of enzyme with Trichoderma reesei xylanase II in Saccharomyces cerevisiae allows for degradation of birchwood xylan to D-xylose
biotechnology
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use of strain for bioconversion of xylan-rich plant wastes to value-added products
biotechnology
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use of stable transgenic Medicago truncatula plants as an expression system for purification and characterization of proteins
biotechnology
the bifunctional beta-glucosidase/xylosidase can be used in simultaneous saccharification of cellulose ans xylan into fermenantable glucose and xylose
biotechnology
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a method for bioconversion of 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol into cycloastragenol is optimized. A green and efficient biotransformation method is established for 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol using beta-glucosidase Dth3 and beta-xylosidase Xln-DT
biotechnology
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the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
biotechnology
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use of strain for bioconversion of xylan-rich plant wastes to value-added products
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biotechnology
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a method for bioconversion of 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol into cycloastragenol is optimized. A green and efficient biotransformation method is established for 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol using beta-glucosidase Dth3 and beta-xylosidase Xln-DT
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biotechnology
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the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
-
biotechnology
Ceratocystis fimbriata RM 35
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the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
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degradation
hydrolysis of water-soluble and water-insoluble arabinoxylan and whole vinasse by an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-L-arabinofuranosidase from Humicola insolens, the GH51 alpha-L-arabinofuranosidase from M. giganteus, a GH10 endo-1,4-beta-xylanase from H. insolens, and a GH3 beta-xylosidase from Trichoderma reesei. The optimal dosages of the minimal enzyme cocktails are 0.4, 0.3, and 0.2 g enzyme protein per kilogram of substrate dry matter for the water-soluble wheat arabinoxylan, the water-insoluble wheat arabinoxylan, and the vinasse, respectively
degradation
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hydrolysis of xylan by co-action of enzyme and xylanase from Anoxybacillus flavithermus BC gives 63.6% conversion after 4 h. Beechwood xylan is the best substrate, main product is xylose
degradation
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in hydrolysis of corn stover hemicellulose, the xylose production increases by 94.9% and 140% when Trichoderma reesei hemicellulase is supplemented with purified beta-xylosidase and crude cell wall proteins of corn stover, respectively
degradation
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co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles
degradation
enzyme increases reducing sugar release of birchwood xylan, beechwood xylan, and arabinoxylan by 6.4%, 13%, 15.8%, respectively, in synergistic action with endoxylanase. The late addition of the enzyme into reaction with endoxylanase results in a larger increase of reducing sugar release from pretreated barley straw that addition at the start or by treatment with endoxylanases alone. The increases observed are 6.3% and 13.8%, respectively
degradation
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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
degradation
the enzyme has potential for promoting hemicellulose degradation and other industrial applications
degradation
the enzyme is useful for degradation of lignocellulosic biomass in bioethanol production, pulp bleaching process and beverage industry
degradation
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co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles
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degradation
Saccharolobus solfataricus Oalpha
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hydrolysis of xylan by co-action of enzyme and xylanase from Anoxybacillus flavithermus BC gives 63.6% conversion after 4 h. Beechwood xylan is the best substrate, main product is xylose
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degradation
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the enzyme is useful for degradation of lignocellulosic biomass in bioethanol production, pulp bleaching process and beverage industry
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food industry
-
the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
food industry
Weissella cibaria FB069
-
the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
-
industry
-
the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production
industry
Aspergillus niger DSM 22593
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the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production
-
nutrition
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enzyme efficiently releases monoterpenols from an aroma precursor extracted from muscat grape juice
nutrition
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the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
nutrition
Weissella cibaria FB069
-
the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
-
pharmacology
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cooperated transformation of ginsenoside extract to the pharmacologically active ginsenoside 20(S)-Rg3 with a beta-glucosidase. After transforming under optimal condition, the 20 g/l of ginsenoside extract is transformed into 6.28 g/l of Rg3 within 90 min, with a corresponding molar conversion of 95.0% and Rg3 productivity of 1793.49 mg/l/h, respectively
pharmacology
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cooperated transformation of ginsenoside extract to the pharmacologically active ginsenoside 20(S)-Rg3 with a beta-glucosidase. After transforming under optimal condition, the 20 g/l of ginsenoside extract is transformed into 6.28 g/l of Rg3 within 90 min, with a corresponding molar conversion of 95.0% and Rg3 productivity of 1793.49 mg/l/h, respectively
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synthesis
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synthesis of a group of uncommon xylosides via the transxylosylation activity
synthesis
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immobilization of enzyme on chitosan as best support material gives immobilization and activity yields of 94% and 87%, respectively, of initial activity, and also provides the highest stability, retaining 94% of its initial activity even after being recycled 25times. Maximal activity of immobilized enzyme is achieved at pH 8.0 and 53°C, whereas that for the free enzyme is obtained at pH 7.0 and 50°C. The immobilized enzyme is more thermostable than the free beta-xylosidase. Km values of the free enzyme increases from 2.37 mM to 3.42 mM at the immobilized state. Immobilized enzyme catalyzes the reverse hydrolysis reaction, forming xylooligosaccharides in the presence of a high concentration of xylose. Co-immobilized of beta-xylosidase and xylanase on chitosan leads to a continuous hydrolysis of 3% oat spelt xylan at 50°C and better hydrolysis yields and higher amount of xylose are obtained
synthesis
the enzyme immobilized by entrapment into alginate can be used for a continuous production of xylose from xylooligosaccharides at high temperature
synthesis
formation of xylooligosaccharides from alpha-D-xylopyranosyl fluoride in a conjugated reaction between beta-xylosidase E335G mutant enzyme and endo-1,4-beta-xylanase E265G mutant enzyme
synthesis
upon codon optimization for expression in Pichia pastoris, the expression level increases to 5.7 g/l in a fermenter system
synthesis
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the enzyme immobilized by entrapment into alginate can be used for a continuous production of xylose from xylooligosaccharides at high temperature
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synthesis
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upon codon optimization for expression in Pichia pastoris, the expression level increases to 5.7 g/l in a fermenter system
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synthesis
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formation of xylooligosaccharides from alpha-D-xylopyranosyl fluoride in a conjugated reaction between beta-xylosidase E335G mutant enzyme and endo-1,4-beta-xylanase E265G mutant enzyme
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additional information
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the beta-xylosidase from Aureobasidium pullulans CBS 135684 is a prospective enzyme for a wide range of applications, especially for the bioconversion of hemicellulose
additional information
the enzyme can be a suitable additive for hemicellulases in long-term hydrolysis reactions. Because of its moderate inhibition by monomeric sugars but its high inhibition by ethanol, the enzyme can be particularly more useful in separate hydrolysis and fermentation than in simultaneous saccharification and co-fermentation or consolidated bioprocessing
additional information
Aureobasidium pullulans CBS 135684
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the beta-xylosidase from Aureobasidium pullulans CBS 135684 is a prospective enzyme for a wide range of applications, especially for the bioconversion of hemicellulose
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