Megazyme/去支链阿拉伯多糖（甜菜）/P-DBAR/2克
商品编号：
P-DBAR
品牌：
Megazyme INC
市场价：
¥2472.00
美元价：
1483.20
产品分类：
其他试剂
公司分类：
Other_reagents
联系Q Q：
3392242852
电话号码：
4000-520-616
电子邮箱：
info@ebiomall.com
商品介绍
HighpurityDebranchedArABInan(SugarBeet)foruseinresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Purity~95%.1,5-α-L-Arabinan.Ara:Gal:Rha:GalUA=88:4:2:6
Hydrolysisofwheatflourarabinoxylan,acid-debranchedwheatflourarabinoxylanandarabino-xylo-oligosaccharidesbyβ-xylanase,α-L-arabinofuranosidaseandβ-xylosidase.
McCleary,B.V.,McKie,V.A.,Draga,A.,Rooney,E.,Mangan,D.&Larkin,J.(2015).CarbohydrateResearch,407,79-96.
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Arangeofα-L-arabinofuranosyl-(1-4)-β-D-xylo-oligosaccharides(AXOS)wereproducedbyhydrolysisofwheatflourarabinoxylan(WAX)andaciddebranchedarabinoxylan(ADWAX),inthepresenceandabsenceofanAXH-d3α-L-arabinofuranosidase,byseveralGH10andGH11β-xylanases.ThestructuresoftheoligosaccharideswerecharacterisedbyGC-MSandNMRandbyhydrolysisbyarangeofα-L-arabinofuranosidasesandβ-xylosidase.TheAXOSwerepurifiedandusedtocharacterisetheactionpatternsofthespecificα-L-arabinofuranosidases.Theseenzymes,incombinationwitheitherCellvibriomixtusorNeocallimastixpatriciarumβ-xylanase,wereusedtoproduceelevatedlevelsofspecificAXOSonhydrolysisofWAX,suchas32-α-L-Araf-(1-4)-β-D-xylobiose(A3X),23-α-L-Araf-(1-4)-β-D-xylotriose(A2XX),33-α-L-Araf-(1-4)-β-D-xylotriose(A3XX),22-α-L-Araf-(1-4)-β-D-xylotriose(XA2X),32-α-L-Araf(1-4)-β-D-xylotriose(XA3X),23-α-L-Araf-(1-4)-β-D-xylotetraose(XA2XX),33-α-L-Araf-(1-4)-β-D-xylotetraose(XA3XX),23,33-di-α-L-Araf-(1-4)-β-D-xylotriose(A2+3XX),23,33-di-α-L-Araf-(1-4)-β-D-xylotetraose(XA2+3XX),24,34-di-α-L-Araf-(1-4)-β-D-xylopentaose(XA2+3XXX)and33,34-di-α-L-Araf-(1-4)-β-D-xylopentaose(XA3A3XX),manyofwhichhavenotpreviouslybeenproducedinsufficientquantitiestoallowtheiruseassubstratesinfurtherenzymicstudies.ForA2,3XX,yieldsofapproximately16%ofthestartingmaterial(wheatarabinoxylan)havebeenachieved.Mixturesoftheα-L-arabinofuranosidases,withspecificactiononAXOS,havebeencombinedwithβ-xylosidaseandβ-xylanasetoobtainanoptimalmixtureforhydrolysisofarabinoxylantoL-arabinoseandD-xylose.
Developmentalcomplexityofarabinanpolysaccharidesandtheirprocessinginplantcellwalls.
Verhertbruggen,Y.,Marcus,S.E.,Haeger,A.,Verhoef,R.,Schols,H.A.,McCleary,B.V.,McKee,L.,Gilbert,H.J.&PaulKnox,J.(2009).ThePlantJournal,59(3),413-425.
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Plantcellwallsareconstructedfromadiversityofpolysaccharidecomponents.Molecularprobesdirectedtostructuralelementsofthesepolymersarerequiredtoassaypolysaccharidestructuresinsitu,andtodeterminepolymerrolesinthecontextofcellwallBIOLOGy.Here,wereportontheisolationandthecharacterizationofthreeratmonoclonalantibodiesthataredirectedto1,5-linkedarabinansandrelatedpolymers.LM13,LM16andLM17,togetherwithLM6,constituteasetofantibodiesthatcandetectdifferingaspectsofarabinanstructureswithincellwalls.EachoftheseantibodiesbindsstronglytoisolatedsugarbeetarabinansamplesinELISAs.Competitive-inhibitionELISAsindicatetheantibodiesbinddifferentiallytoarabinanswiththebindingofLM6andLM17beingeffectivelyinhibitedbyshortoligoarabinosides.LM13bindspreferentiallytolongeroligoarabinosides,anditsbindingishighlysensitivetoarabinanaseaction,indicatingtherecognitionofalongerlinearizedarabinanepitope.Incontrast,thebindingofLM16tobranchedarabinanandtocellwallsisincreasedbyarabinofuranosidaseaction.Thepresenceofallepitopescanbedifferentiallymodulatedinvitrousingglycosidehydrolasefamily43andfamily51arabinofuranosidases.Inaddition,theLM16epitopeissensitivetotheactionofβ-galactosidase.Immunofluorescencemicroscopyindicatesthattheantibodiescanbeusedtodetectepitopesincellwalls,andthatthefourantibodiesrevealcomplexpatternsofepitopeoccurrencethatvarybetweenorgansandspecies,andrelatebothtotheprobableprocessingofarabinanstructuralelementsandthedifferingmechanicalpropertiesofcellwalls.
Exo-arabinanaseofPenicilliumchrysogenumabletoreleasearabinobiosefromα-1,5-L-arabinan.
Sakamoto,T.&Thibault,J.F.(2001).AppliedandEnvironmentalMicrobiology,67(7),3319-3321.
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Anexo-arabinanase,designatedAbnx,waspurifiedfromaculturefiltrateofPenicilliumchrysogenum31Bbyammoniumsulfateprecipitation,anion-exchangechromatography,andhydrophobicchromatography.Abnxhadanapparentmolecularmassof47kDa.Theenzymereleasedonlyarabinobiosefromthenonreducingterminusofα-1,5-L-arabinanandshowednoactivitytowardsp-nitrophenyl-α-L-arabinofuranosideandα-1,5-L-arabinofuranobiose.Abnxisthefirstenzymewiththismodeofaction.
Organizationofpecticarabinanandgalactansidechainsinassociationwithcellulosemicrofibrilsinprimarycellwallsandrelatedmodelsenvisaged.
Zykwinska,A.,Thibault,J.F.&Ralet,M.C.(2007).JournalofExperimentalBotany,58(7),1795-1802.
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Thestructureofarabinanandgalactandomainsinassociationwithcellulosemicrofibrilswasinvestigatedusingenzymaticandalkalidegradationprocedures.Sugarbeetandpotatocellwallresidues(called‘natural’composites),richinpecticneutralsugarsidechainsandcellulose,aswellas‘artificial’composites,createdbyinvitroadsorptionofarabinanandgalactansidechainsontoprimarycellwallcellulose,werestudied.Thesecompositesweresequentiallytreatedwithenzymesspecificforpecticsidechainsandhotalkali.Thedegradationapproachusedshowedthatmostofthearabinanandgalactansidechainsareinstronginteractionwithcelluloseandarenothydrolysedbypecticsidechain-degrADIngenzymes.Itseemsunlikelythatisolatedarabinanandgalactanchainsareabletotetheradjacentmicrofibrils.However,cellulosemicrofibrilsmaybetetheredbydifferentpecticsidechainsbelongingtothesamepecticmacromolecule.
Evidenceforinvitrobindingofpectinsidechainstocellulose.
Zykwinska,A.W.,Ralet,M.C.J.,Garnier,C.D.&Thibault,J.F.J.(2005).PlantPhysiology,139(1),397-407.
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Pectinsofvaryingstructuresweretestedfortheirabilitytointeractwithcelluloseincomparisontothewell-knownadsorptionofxyloglucan.Ourresultsrevealthatsugarbeet(Betavulgaris)andpotato(Solanumtuberosum)pectins,whicharerichinneutralsugarsidechains,canbindinvitrotocellulose.Theextentofbindingvarieswithrespecttothenatureandstructureofthesidechains.Additionally,branchedarabinans(Br-Arabinans)ordebranchedarabinans(Deb-Arabinans;isolatedfromsugarbeet)andgalactans(isolatedfrompotato)wereshownbindtocellulosemicrofibrils.TheadsorptionofBr-ArabinanandgalactanwaslowerthanthatofDeb-Arabinan.ThemaximumadsorptionaffinityofDeb-Arabinantocellulosewascomparabletothatofxyloglucan.Thestudyofsugarbeetandpotatoalkali-treatedcellwallssupportsthehypothesisofpectin-celluloseinteraction.Naturalcompositesenrichedinarabinansorgalactansandcellulosewererecovered.Thebindingofpectinstocellulosemicrofibrilsmaybeofconsiderablesignificanceinthemodelingofprimarycellwallsofplantsaswellasintheprocessofcellwallassembly.
DirectinterferencewithrhamnogalacturonanIbiosynthesisinGolgivesicles.
Skjøt,M.,Pauly,M.,Bush,M.S.,Borkhardt,B.,McCann,M.C.&Ulvskov,P.(2002).PlantPhysiology,129(1),95-102.
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Pectinisaclassofcomplexcellwallpolysaccharideswithmultiplerolesduringcelldevelopment.Assigningspecificfunctionstoparticularpolysaccharidesisinitsinfancy,inpart,becauseofthelimitednumberofmutantsandtransformantsavailablewithmodifiedpecticpolymersintheirwalls.Pectinsarealsoimportantpolymerswithdiverseapplicationsinthefoodandpharmaceuticalindustries,whichwouldbenefitfromtechnologyforproducingpectinswithspecificfunctionalproperties.Inthisreport,wedescribethegenerationofpotato(SolanumtuberosumL.cvPosmo)tubertransformantsproducingpecticrhamnogalacturonanI(RGI)withalowlevelofarabinosylation.ThiswasachievedbytheexpressionofaGolgimembrane-anchoredendo-α-1,5-arabinanase.SugarcompositionanalysisofRGIisolatedfromtransformedandwild-typetubersshowedthatthearabinosecontentwasdecreasedbyapproximately70%intransformedcellwallscomparedwithwildtype.ThemodificationoftheRGIwasconfirmedbyimmunolabelingwithanantibodyrecognizingα-1,5-arabinan.Thisisthefirsttime,toourknowledge,thatthebiosynthesisofaplantcellwallpolysaccharidehasbeenmanipulatedthroughtheactionofaglycosylhydrolasetargetedtotheGolgicompartment.
Characterizationofamodularenzymeofexo-1,5-α-L-arabinofuranosidaseandarabinanbindingmodulefromStreptomycesavermitilisNBRC14893.
Ichinose,H.,Yoshida,M.,Fujimoto,Z.&Kaneko,S.(2008).AppliedMicrobiologyandBiotechnology,80(3),399-408.
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Ageneencodinganα-L-arabinofuranosidase,designatedSaAraf43A,wasclonedfromStreptomycesavermitilis.ThededucedaminoacidsequenceimpliesamodularstructureconsistingofanN-terminalglycosidehydrolasefamily43moduleandaC-terminalfamily42carbohydrate-bindingmodule(CBM42).TherecombinantenzymeshowedoptimalactivityatpH6.0and45°CandwasstableoverthepHrangeof5.0–6.5at30°C.Theenzymehydrolysedp-nitrophenol(PNP)-α-L-arabinofuranosidebutdidnothydrolyzePNP-α-L-arabinopyranoside,PNP-β-D-xylopyranoside,orPNP-β-D-galactopyranoside.Debranched1,5-arabinanwashydrolyzedbytheenzymebutarabinoxylan,arabinogalactan,gumarabic,andarabinanwerenot.Amongthesyntheticregioisomersofarabinofuranobiosides,onlymethyl5-O-α-L-arabinofuranosyl-α-L-arabinofuranosidewashydrolyzedbytheenzyme,whilemethyl2-O-α-L-arabinofuranosyl-α-L-arabinofuranosideandmethyl3-O-α-L-arabinofuranosyl-α-L-arabinofuranosidewerenot.Thesedatasuggestedthattheenzymeonlycleavesα-1,5-linkedarabinofuranosyllinkages.Theanalysisofthehydrolysisproductofarabinofuranopentaosesuggestedthattheenzymereleasesarabinoseinexo-actingmanner.Theseresultsindicatethattheenzymeisdefinitelyanexo-1,5-α-L-arabinofuranosidase.TheC-terminalCBM42didnotshowanyaffinityforarabinogalactananddebranchedarabinan,althoughitboundarabinanandarabinoxylan,suggestingthattheCBM42boundtobranchedarabinofuranosylresidues.Removalofthemoduledecreasedtheactivityoftheenzymewithregardtodebranchedarabinan.TheCBM42playsaroleinenhancingthedebranchedarabinanhydrolyticactionofthecatalyticmoduleinspiteofitspreferenceforbindingarabinofuranosylsidechains.
Afamily51α-L-arabinofuranosidasefromPenicilliumpurpurogenum:purification,propertiesandaminoacidsequence.
Fritz,M.,Ravanal,M.C.,Braet,C.&Eyzaguirre,J.(2008).MycologicalResearch,112(8),933-942.
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ThesoftrotfungusPenicilliumpurpurogenumsecretesawidevarietyofxylanolyticenzymestothemedium,amongthemthreeα-L-arabinofuranosidases.Thisworkreferstoarabinofuranosidase2(ABF2).Thisenzymewaspurifiedtohomogeneityandcharacterized;itisaglycosylatedmonomerwithamolecularweightof70 000andanisoelectricpointof5.3.Whenassayedwithp-nitrophenylα-L-arabinofuranoside(pNPAra)theenzymefollowedMichaelis–MentenkineticswithaKMof0.098mm.TheoptimumpHis5andtheoptimaltemperature60°C.ABF2showedweakactivityonnaturalpolymericsubstrates,suchassugarbeetarabinan,debranchedarabinan,andarabinoxylan.Theseresults,togetherwithitslowKM(pNPAra)anditsactivitytowardsshortarabinooligosaccharides,suggestthattheenzymebelongstotheexoα-L-arabinosylhydrolasesnotactiveonpolymers.Theabf2geneanditsCDNAweresequenced,andthegenewasfoundtopossesssevenintrons.Thematureproteinis618aminoacidslongwithacalculatedmolecularweightof67 212.Aminoacidsequencealignmentsshowthattheenzymebelongstofamily51oftheglycosylhydrolases,althoughitdiffersinsomepropertiesfromotherenzymesofthisfamily.
AmultitaskATPaseservingdifferentABC-typesugarimportersinBacillussubtilis.
Ferreira,M.J.&deSá-Nogueira,I.(2010).JournalofBacteriology,192(20),5312-5318.
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Bacillussubtilisisabletoutilizearabinopolysaccharidesderivedfromplantbiomass.Here,bycombininggeneticandphysiologicalanalyseswecharacterizetheAraNPQimporterandidentifyprimaryandsecondarytransportersofB.subtilisinvolvedintheuptakeofarabinosaccharides.WeshowthattheABC-typeimporterAraNPQisinvolvedintheuptakeofα-1,5-arabinooligosaccharides,atleastuptofourL-arabinosylunits.Althoughthissystemisthekeytransporterforα-1,5-arabinotrioseandα-1,5-arabinotetraose,theresultsindicatethatα-1,5-arabinobiosealsoistranslocatedbythesecondarytransporterAraE.Thisbroad-specificityprotonsymporteristhemajortransporterforarabinoseandalsoisaccountablefortheuptakeofxyloseandgalactose.Inaddition,MsmXisshowntobetheATPasethatenergizestheincompleteAraNPQimporter.FurThermore,theresultssuggesttheexistenceofatleastonemoreunidentifiedMsmX-dependentABCimporterresponsIBLefortheuptakeofnonlinearα-1,2-andα-1,3-arabinooligosaccharides.ThisstudyassignsMsmXasamultipurposeB.subtilisATPaserequiredtoenergizedifferentsaccharidetransporters,thearabinooligosaccharide-specificAraNPQ-MsmXsystem,aputativeMsmX-dependentABCtransporterspecificfornonlineararabinooligosaccharides,andthepreviouslycharacterizedmaltodextrin-specificMdxEFG-MsmXsystem.
Purification,characterizationandfunctionalanalysisofanendo‐arabinanase(AbnA)fromBacillussubtilis.
Leal,T.F.&Sá‐Nogueira,I.(2004).FEMSMicrobiologyLetters,241(1),41-48.
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BacillussubtilissynthesizesatleastonearabinanaseencodedbytheabnAgenethatisabletodegradethepolysaccharidearabinan.Here,wereporttheexpressioninEscherichiacoliofthefull-lengthabnAcodingregionwithaHis6-tagfusedtotheC-terminus.TherecombinantproteinwassecretedtotheperiplasmicspaceandcorrectlyprocessedbytheE.colisignalpeptidase.ThesubstratespecificityofpurifiedAbnA,thephysico-chemicalpropertiesandkineticparametersweredetermined.FunctionalanalysisstudiesrevealedGlu215asakeyresidueforAbnAhydrolyticactivityandindicatedthatinadditiontoAbnAB.subtilissecretesotherenzyme(s)abletodegradelinear1,5-α-L-arabinan.
Purificationandcharacterizationofthermostableendo-1,5-α-L-arabinasefromastrainofBacillusthermodenitrificans.
Takao,M.,Akiyama,K.&Sakai,T.(2002).AppliedandEnvironmentalMicrobiology,68(4),1639-1646.
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Astrainofathermophilicbacterium,tentativelydesignatedBacillusthermodenitrificansTS-3,witharabinan-degradingactivitywasisolated.Itproducedanendo-arabinase(ABN)(EC3.2.1.99)andtwoarabinofuranosidases(EC3.2.1.55)extracellularlywhengrownat60°Conamediumcontainingsugarbeetarabinan.TheABN(tentativelycalledanABN-TS)waspurified7,417-foldbyanion-exchange,hydrophobic,sizeexclusion,andhydroxyapatitechromatographies.ThemolecularmassofABN-TSwas35kDaasdeterminedbysodiumdodecylsulfate-polyacrylamidegelelectrophoresis,andtheisoelectricpointwaspH4.5.TheenzymewasobservedtobemorethermostablethanknownABNs;ithadahalf-lifeof4hat75°C.Theenzymehadoptimalactivityat70°CandpH6.0.TheenzymehadapparentKmvaluesof8.5and45mg/mlandapparentVmaxvaluesof1.6and1.1mmol/min/mgofproteinagainstdebranchedarabinan(α-1,5-arabinan)andarabinan,respectively.Theenzymehadnopectin-releasingactivity(protopectinaseactivity)fromsugarbeetprotopectin,differingfromanABN(protopectinase-C)frommesophilicBacillussubtilisIFO3134.ThepatternofdegradationofdebranchedarabinanbyABN-TSindicatedthattheenzymewasanendo-actingenzymeandthemainendproductswerearabinobioseandarabinose.TheresultsofpreliminaryexperimentsindicatedthattheculturefiltrateofstrainTS-3issuitableforL-arabinoseproductionfromsugarbeetpulpathightemperature.
AspergillusfumigatusProducesTwoArabinofuranosidasesFromGlycosylHydrolaseFamily62:ComparativePropertiesoftheRecombinantEnzymes.
Pérez,R.&Eyzaguirre,J.(2016).Appliedbiochemistryandbiotechnology,179(1),143-154.
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Thegenesoftwoα-L-arabinofuranosidases(AbfI andII)fromfamilyGH62havebeenidentifiedinthegenomeofAspergillusfumigatuswmo.BothgeneshavebeenexpressedinPichiapastorisandtheenzymeshavebeenpurifiedandcharacterized.AbfIiscomposedof999 bp,doesnotcontainintronsandcodesforaprotein(ABFI)of332aminoacidresidues.abfIIhas1246 bp,includinganintronof51 bp;theproteinABFIIhas396aminoacidresidues;itincludesafamily1carbohydrate-bindingmodule(CBM)intheN-terminalregion,followedbyacatalyticmodule.ThesequenceofABFIandthecatalyticmoduleofABFIIshowa79 %identity.Bothenzymesareactiveonp-nitrophenylα-L-arabinofuranoside(pNPAra)withKMof94.2and3.9 mMforABFIandII,respectively.OptimaltemperatureforABFIis37°CandforABFII42°C,whilethepHoptimumisabout4.5to5forbothenzymes.ABFIIshowsahigherthermostability.Whenassayedusingnaturalsubstrates,bothshowhigheractivityoverryearabinoxylanascomparedtowheatarabinoxylan.ABFIIonlyisactiveonsugarbeetpulparabinanandbothareinactivetowardsdebranchedarabinan.Thehigherthermostability,higheraffinityforpNPAraandwideractivityovernaturalsubstratesshownbyABFIImayberelatedtothepresenceofaCBM.Theavailabilityoftherecombinantenzymesmaybeusefulinbiotechnologicalapplicationsfortheproductionofarabinose.
Screeningofthermotolerantandthermophilicfungiaimingβ-xylosidaseandarabinanaseproduction.
Benassi,V.M.,Lucas,R.C.D.,Jorge,J.A.&Polizeli,M.D.L.T.D.(2014).BrazilianJournalofMicrobiology,45(4),1459-1467.
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Plantcellwallismainlycomposedbycellulose,hemicelluloseandlignin.Theheterogeneousstructureandcompositionofthehemicellulosearekeyimpedimentstoitsdepolymerizationandsubsequentuseinfermentationprocesses.Thus,thisstudyaimedtoperformascreeningofthermophilicandthermotolerantfilamentousfungicollectedfromdifferentregionsoftheSãoPaulostate,andanalyzetheproductionofβ-xylosidaseandarabinanaseatdifferenttemperatures.Theseenzymesareimportanttocellwalldegradationandsynthesisofendproductsasxyloseandarabinose,respectively,whicharesignificantsugarstofermentationandethanolproduction.Atotalof12fungalspecieswereanalyzedand9ofthemgrewat45°C,suggestingathermophilicorthermotolerantcharacter.AdditionallyAspergillusthermomutatusanamorphofNeosartoryaandA.parasiticusgrewat50°C.AspergillusnigerandAspergillusthermomutatuswerethefilamentousfungiwiththemostexpressiveproductionofβ-xylosidaseandarabinanase,respectively.Ingeneralformostofthetestedmicroorganisms,β-xylosidaseandarabinanaseactivitiesfrommycelialextract(intracellularform)werehigherinculturesgrownathightemperatures(35-40°C),whilethecorrespondentextracellularactivitieswerefavorablysecretedfromculturesat30°C.ThisstudycontributestocatalogueisolatedfungiofthestateofSãoPaulo,andthesefindingscouldbepromisingsourcesforthermophilicandthermotolerantmicroorganisms,whichareindustriallyimportantduetotheirenzymes.
HeterologousexpressionofaPenicilliumpurpurogenumexo-arabinanaseinPichiapastorisanditsbiochemicalcharacterization.
Mardones,W.,Callegari,E.&Eyzaguirre,J.(2015).Fungalbiology,119(12),1267-1278.
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Arabinanisacomponentofpectin,whichisoneofthepolysaccharidespresentinlignocelluose.Theenzymesdegradingthemainchainofarabinanaretheendo-(EC3.2.1.99)andexo-arabinanases(3.2.1.-).Onlythreeexo-arabinanaseshavebeenbiochemicallycharacterized;theybelongtoglycosylhydrolasefamily93.Inthiswork,thecDNAofanexo-arabinanase(Arap2)fromPenicilliumpurpurogenumhasbeenheterologouslyexpressedinPichiapastoris.Thegeneis1310 bplong,hasthreeintronsandcodesforaproteinof380aminoacidresidues;thematureproteinhasacalculatedmolecularmassof39 823 Da.TheheterologouslyexpressedArap2hasamolecularmassintherangeof60-80 kDaduetoheterogeneousglycosylation.TheenzymeisactiveondebranchedarabinanwithoptimumpHof4-5.5andoptimaltemperatureof40°C,andhasanexo-typeactionmode,releasingarabinobiosefromitssubstrates.Theexpressionprofileofarap2incorncobandsugarbeetpulpfollowsadifferentpatternandisnotrelatedtothepresenceofarabinan.Thisisthefirstexo-arabinanasestudiedfromP.purpurogenumandthefirstexpressedinyeast.TheavailabilityofheterologousArap2maybeusefulforbiotechnologicalapplicationsrequiringacidicconditions.
Synergistichydrolysisofxylanusingnovelxylanases,β-xylosidases,andanα-L-arabinofuranosidasefromGeobacillusthermodenitrificansNG80-2.
Huang,D.,Liu,J.,Qi,Y.,Yang,K.,Xu,Y.&Feng,L.(2017).AppliedMicrobiologyandBiotechnology,1-15.
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Lignocellulosicbiomassfromvarioustypesofwoodhasbecomearenewableresourceforproductionofbiofuelsandbiobasedchemicals.Becausexylanisthemajorcomponentofwoodhemicelluloses,highlyefficientenzymestoenhancexylanhydrolysiscanimprovetheuseoflignocellulosicbiomass.Inthisstudy,axylanolyticgeneclusterwasidentifiedfromthecrudeoil-degradingthermophilicstrainGeobacillusthermodenitrificansNG80-2.Theenzymesinvolvedinxylanhydrolysis,whichincludetwoxylanases(XynA1,XynA2),threeβ-xylosidases(XynB1,XynB2,XynB3),andoneα-L-arabinofuranosidase(AbfA),havemanyuniquefeatures,suchashighpHtolerance,highthermostability,andabroadsubstraterange.Thethreeβ-xylosidaseswerehighlyresistanttoinhibitionbyproduct(xylose)accumulation.Moreover,thecombinationofxylanase,β-xylosidase,andα-L-arabinofuranosidaseexhibitedthelargestsynergisticactiononxylandegradation(XynA2,XynB1,andAbfAonoatspeltorbeechwoodxylan;XynA2,XynB3,andAbfAonbirchwoodxylan).Wehavedemonstratedthattheproposedenzymaticcocktailalmostcompletelyconvertscomplexxylantoxyloseandarabinofuranoseandhasgreatpotentialforuseintheconversionofplantbiomassintobiofuelsandbiochemicals.
品牌介绍
Megazyme品牌产品简介
来源：作者：人气：2149发表时间：2016-05-19 10:59:00【大 中 小】
Megazyme是一家全球性公司，专注于开发和提供用于饮料、谷物、乳制品、食品、饲料、发酵、生物燃料和葡萄酒产业用的分析试剂、酶和检测试剂盒。Megazyme的许多检测试剂盒产品已经为众多官方科学协会（包括AOAC, AACC , RACI, EBC和ICC等），经过严格的审核，批准认证为官方标准方法，确保以准确、可靠、定量和易于使用的测试方法，满足客户的质量诉求。
Megazyme的主要产品线包括：
◆ 检测试剂盒
◆ 酶
◆ 酶底物
◆ 碳水化合物
◆ 化学品/仪器
官网地址：http://www.megazyme.com
检测试剂盒特色产品：
货号
中文品名
用途
K-ACETAF
乙酸[AF法]检测试剂盒
酶法定量分析乙酸最广泛使用的方法
K-ACHDF
可吸收糖/膳食纤维检测试剂盒
酒精沉淀法测定膳食纤维
K-AMIAR
氨快速检测试剂盒
用于包括葡萄汁、葡萄酒以及其它食品饮料样品中氨含量的快速检测分析。
K-AMYL
直链淀粉/支链淀粉检测试剂盒
谷物淀粉和而粉中直链淀粉/支链淀粉比例和含量检测
K-ARAB
阿拉伯聚糖检测试剂盒
果汁浓缩液中阿拉伯聚糖的检测
K-ASNAM
L-天冬酰胺/L-谷氨酰胺和氨快速检测试剂盒
用于食品工业中丙烯酰胺前体、细胞培养基、以及上清液组分中、L-天冬酰胺，谷氨酰胺和氨的检测分析
K-ASPTM
阿斯巴甜检测试剂盒
专业用于测定饮料和食品中阿斯巴甜含量，操作简单
K-BETA3
β-淀粉酶检测试剂盒
适用于麦芽粉中β-淀粉酶的测定
K-BGLU
混合键β-葡聚糖检测试剂盒
测定谷物、荞麦粉、麦汁、啤酒及其它食品中混合键β-葡聚糖(1,3:1,4-β-D-葡聚糖)的含量
K-CERA
α-淀粉酶检测试剂盒
谷物和发酵液（真菌和细菌）中α-淀粉酶的分析测定
K-CITR
柠檬酸检测试剂盒
快速、可靠地检测食品、饮料和其它物料中柠檬酸（柠檬酸盐）含量
K-DLATE
乳酸快速检测试剂盒
快速、特异性检测饮料、肉类、奶制品和其它食品中L-乳酸和D-乳酸(乳酸盐）含量
K-EBHLG
酵母β-葡聚糖酶检测试剂盒
用于测量和分析酵母中1,3:1,6?-β-葡聚糖，也可以检测1,3-葡聚糖
K-ETSULPH
总亚硫酸检测试剂盒
测定葡萄酒、饮料、食品和其他物料中总亚硫酸含量（按二氧化硫计）的一种简单，高效，可靠的酶法检测方法
K-FRGLMQ
D-果糖/D-葡萄糖[MegaQuant法]检测试剂盒
适用于使用megaquant?色度计（505nm下）测定葡萄、葡萄汁和葡萄酒中D-果糖和D-葡萄糖的含量。
K-FRUC
果聚糖检测试剂盒
含有淀粉、蔗糖和其他糖类的植物提取物和食品中果聚糖的含量测定。
K-FRUGL
D-果糖/D-葡萄糖检测试剂盒
对植物和食品中果糖或葡萄糖含量的酶法紫外分光测定。
K-GALM
半乳甘露聚糖检测试剂盒
食品和植物产品中半乳甘露聚糖的含量检测
K-GLUC
D-葡萄糖[GOPOD]检测试剂盒
谷物提取物中D-葡萄糖的含量测定，可以和其它Megazyme检测试剂盒联合使用。
K-GLUHK
D-葡萄糖[HK]检测试剂盒
植物和食品中D-葡萄糖的含量测定，可以和其它Megazyme检测试剂盒联合使用。
K-GLUM
葡甘聚糖检测试剂盒
植物和食品中葡甘聚糖的含量测定。
K-INTDF
总膳食纤维检测试剂盒
总膳食纤维特定检测和分析
K-LACGAR
乳糖/D-半乳糖快速检测试剂盒
用于快速检测食品和植物产品中乳糖、D-半乳糖和L-阿拉伯糖
K-LACSU
乳糖/蔗糖/D-葡萄糖检测试剂盒
混合面粉和其它物料中蔗糖、乳糖和D-葡萄糖的测定
K-LACTUL
乳果糖检测试剂盒
特异性、快速和灵敏测量奶基样品中乳果糖含量
K-MANGL
D-甘露糖/D-果糖/D-葡萄糖检测试剂盒
适合测定植物产品和多糖酸性水解产物中D-甘露糖含量
K-MASUG
麦芽糖/蔗糖/D-葡萄糖检测试剂盒
在植物和食品中麦芽糖，蔗糖和葡萄糖的含量检测
K-PECID
胶质识别检测试剂盒
食品配料中果胶的鉴别
K-PHYT
植酸(总磷)检测试剂盒
食品和饲料样品植酸/总磷含量测量的简便方法。不需要通过阴离子交换色谱对植酸纯化，适合于大量样本分析
K-PYRUV
丙酮酸检测试剂盒
在啤酒、葡萄酒、果汁、食品和体液中丙酮酸分析
K-RAFGA
棉子糖/D-半乳糖检测试剂盒
快速测量植物材料和食品中棉子糖和半乳糖含量
K-RAFGL
棉子糖/蔗糖/D-半乳糖检测试剂盒
分析种子和种子粉中D-葡萄糖、蔗糖、棉子糖、水苏糖和毛蕊花糖含量。通过将棉子糖、水苏糖和毛蕊花糖酶解D-葡萄糖、D-果糖和半乳糖，从而测定葡萄糖含量来确定
K-SDAM
淀粉损伤检测试剂盒
谷物面粉中淀粉损伤的检测和分析
K-SUCGL
蔗糖/D-葡萄糖检测试剂盒
饮料、果汁、蜂蜜和食品中蔗糖和葡萄糖的分析
K-SUFRG
蔗糖/D-果糖/D-葡萄糖检测试剂盒
适用于植物和食品中蔗糖、D-葡萄糖和D-果糖的测定
K-TDFR
总膳食纤维检测试剂盒
总膳食纤维检测
K-TREH
海藻糖检测试剂盒
快速、可靠地检测食品、饮料和其它物料中海藻糖含量
K-URAMR
尿素/氨快速检测试剂盒
适用于水、饮料、乳制品和食品中尿素和氨的快速测定
K-URONIC
D-葡萄糖醛酸/D-半乳糖醛酸检测试剂盒
简单、可靠、精确测定植物提取物、培养基/上清液以及其它物料中六元糖醛酸含量（D-葡萄糖醛酸和D-半乳糖醛酸）
K-XYLOSE
D-木糖检测试剂盒
简单、可靠、精确测定植物提取物、培养基/上清液以及其它物料中D-木糖含量
K-YBGL
Beta葡聚糖[酵母和蘑菇]检测试剂盒
检测酵母和蘑菇制品中1,3:1,6-beta-葡聚糖和α-葡聚糖含量
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