Search results for "Xylosidases"

showing 3 items of 3 documents

A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes

1999

The gene xynC encoding xylanase C from Bacillus sp. BP-23 was cloned and expressed in Escherichia coli. The nucleotide sequence of a 3538 bp DNA fragment containing xynC gene was determined, revealing an open reading frame of 3258 bp that encodes a protein of 120,567 Da. A comparison of the deduced amino acid sequence of xylanase C with known beta-glycanase sequences showed that the encoded enzyme is a modular protein containing three different domains. The central region of the enzyme is the catalytic domain, which shows high homology to family 10 xylanases. A domain homologous to family IX cellulose-binding domains is located in the C-terminal region of xylanase C, whilst the N-terminal r…

Molecular Sequence DataBacillusBiologymedicine.disease_causeMicrobiologyHomology (biology)Substrate Specificitychemistry.chemical_compoundCatalytic DomainEnzyme StabilityEscherichia colimedicineXylobioseAmino Acid SequenceCloning MolecularEscherichia coliPeptide sequencechemistry.chemical_classificationEndo-14-beta XylanasesSequence Homology Amino AcidThermophileTemperatureNucleic acid sequenceSequence Analysis DNAXylosidasesEnzymeBiochemistrychemistryGenes BacterialXylanaseSequence AlignmentMicrobiology
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Toxicological Assessment of Recombinant Xylanase X22 in Wine

1999

Toxicological evaluation of xylanase X(22) from Aspergillus nidulans expressed in a wine yeast strain was carried out. The safety of the X(22) intake was assessed by digestibility, bioinformatic, and mouse short-term repeated dosing studies, although X(22) shows resistance to proteolytic degradation in the gastrointestinal system, is a minority protein component (<0.5 10(-)(6) %) of the produced wine, and shows no significant amino acid sequence homology to any known food allergens. The 4-week oral toxicity study was performed in Swiss mice at a dose level of 0.01, 0.1, or 1 mg/kg/day (these dosages correlate to 8, 80, and 800 times, respectively, the enzyme amount contained in 250 mL of wi…

MaleDoseUrinalysisWineBiologyAspergillus nidulansMicrobiologyMiceOral administrationmedicineAnimalsFood scienceWineGastric JuiceDose-Response Relationship Drugmedicine.diagnostic_testGeneral ChemistryAllergensRecombinant ProteinsYeastYeast in winemakingXylosidasesXylanaseDigestionFemaleGeneral Agricultural and Biological SciencesDigestionFood HypersensitivityJournal of Agricultural and Food Chemistry
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Active Site Mapping of Xylan-Deconstructing Enzymes with Arabinoxylan Oligosaccharides Produced by Automated Glycan Assembly

2017

Xylan-degrading enzymes are crucial for the deconstruction of hemicellulosic biomass, making the hydrolysis products available for various industrial applications such as the production of biofuel. To determine the substrate specificities of these enzymes, we prepared a collection of complex xylan oligosaccharides by automated glycan assembly. Seven differentially protected building blocks provided the basis for the modular assembly of 2-substituted, 3-substituted, and 2-/3-substituted arabino- and glucuronoxylan oligosaccharides. Elongation of the xylan backbone relied on iterative additions of C4-fluorenylmethoxylcarbonyl (Fmoc) protected xylose building blocks to a linker-functionalized …

GlycanGlycoside HydrolasesStereochemistryOligosaccharidesSOLID-PHASE SYNTHESISXylose010402 general chemistryARABINOXYLANPLANT CELL WALL01 natural sciencesCatalysisSubstrate Specificity//purl.org/becyt/ford/1 [https]chemistry.chemical_compoundHydrolysisCellvibrioGlucuronoxylanCatalytic DomainArabinoxylan//purl.org/becyt/ford/1.4 [https]Organic chemistryBacteroidesGlycoside hydrolaseSolid-Phase Synthesis Techniqueschemistry.chemical_classificationbiology010405 organic chemistryHydrolysisCARBOHYDRATESOtras Ciencias QuímicasOrganic ChemistryCiencias QuímicasActive siteGeneral ChemistryXylan0104 chemical sciencescarbohydrates (lipids)Xylosidaseschemistrybiology.proteinXylansENZYMESCIENCIAS NATURALES Y EXACTAS
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