Search results for "Xylobiose"

showing 3 items of 3 documents

Prebiotic effect of xylooligosaccharides produced from birchwood xylan by a novel fungal GH11 xylanase.

2017

34 p.-4 fig.-1 tab.

0106 biological sciences0301 basic medicineSCFAsBreast-fedStaphylococcus hominisMicroorganismmedicine.medical_treatmentOligosaccharidesXyloseBiologyXylosidase01 natural sciencesAnalytical Chemistry03 medical and health scienceschemistry.chemical_compound010608 biotechnologyXylobiosemedicineGlycoside hydrolaseEndo-14-beta XylanasesPrebioticHydrolysisGeneral MedicineXylanLactic acid030104 developmental biologyPrebioticschemistryBiochemistryTalaromycesXOSXylanaseXylansMicrobiomeBifidobacteriumFood ScienceFood chemistry
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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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Levansucrases from Pseudomonas syringae pv. tomato and P. chlororaphis subsp. aurantiaca: Substrate specificity, polymerizing properties and usage of…

2011

Levansucrases of Pseudomonas syringae pv. tomato DC3000 (Lsc3) and Pseudomonas chlororaphis subsp. aurantiaca (also Pseudomonas aurantiaca) (LscA) have 73% identity of protein sequences, similar substrate specificity and kinetic properties. Both enzymes produce levan and fructooligosaccharides (FOS) of varied length from sucrose, raffinose and sugar beet molasses. A novel high-throughput chip-based nanoelectrospray mass spectrometric method was applied to screen alternative fructosyl acceptors for levansucrases. Lsc3 and LscA could both transfructosylate D-xylose, D-fucose, L- and D-arabinose, D-ribose, D-sorbitol, xylitol, xylobiose, D-mannitol, D-galacturonic acid and methyl-α-D-glucopyra…

Spectrometry Mass Electrospray IonizationSucroseRecombinant Fusion ProteinsMolecular Sequence DataPseudomonas syringaeBioengineeringFructoseXylitolApplied Microbiology and BiotechnologySubstrate SpecificityStructure-Activity Relationshipchemistry.chemical_compoundRaffinoseBacterial ProteinsPseudomonasPseudomonas aurantiacaPseudomonas syringaeXylobioseHistidineAmino Acid SequenceRaffinoseHistidinebiologySubstrate (chemistry)General Medicinebiology.organism_classificationPseudomonas chlororaphisFructansHexosyltransferaseschemistryBiochemistryMutagenesis Site-DirectedChromatography Thin LayerOligopeptidesSequence AlignmentBiotechnologyJournal of Biotechnology
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