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蚂蚁淘在线 / 品牌中心 / Megazyme / Megazyme/甘露聚糖（象牙坚果）/P-MANIV/3克

Megazyme/甘露聚糖（象牙坚果）/P-MANIV/3克

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HighpurityMannan(IvoryNut)foruseinresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.

Purity>98%.1,4-β-D-Mannan.Treatedwithsodiumborohydridetolowerreducingsugarlevels.TracesofarABInoseandxylose.

Roleof(1,3)(1,4)β-glucanincellwalls:Interactionwithcellulose.

Kiemle,S.N.,Zhang,X.,Esker,A.R.,Toriz,G.,Gatenholm,P.&Cosgrove,D.J.(2014).Biomacromolecules,15(5),1727-1736.
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(1,3)(1,4)-β-D-Glucan(mixed-linkageglucanorMLG),acharacteristichemicelluloseinprimarycellwallsofgrasses,wasinvestigatedtodeterminebothitsroleincellwallsanditsinteractionwithcelluloseandothercellwallpolysaccharidesinvitro.BindingisothermsshowedthatMLGadsorptionontomicrocrystallinecelluloseisslow,irreversIBLe,andtemperature-dependent.MeasurementsusingquartzcrystalmicrobalancewithdissipationmonitoringshowedthatMLGadsorbedirreversiblyontoamorphousregeneratedcellulose,formingathickhydrogel.Oligosaccharideprofilingusingendo-(1,3)(1,4)-β-glucanaseindicatedthattherewasnodifferenceinthefrequencyanddistributionof(1,3)and(1,4)linksinboundandunboundMLG.ThebindingofMLGtocellulosewasreducedifthecellulosesampleswerefirsttreatedwithcertaincellwallpolysaccharides,suchasxyloglucanandglucuronoarabinoxylan.ThetetheringfunctionofMLGincellwallswastestedbyapplyingendo-(1,3)(1,4)-β-glucanasetowallsamplesinaconstantforceextensometer.Cellwallextensionwasnotinduced,whichindicatesthatenzyme-accessibleMLGdoesnottethercellulosefibrilsintoaload-bearingnetwork.

endo-β-1,4-Mannanasesfrombluemussel,Mytilusedulis:purification,characterization,andmodeofaction.

Xu,B.,Hägglund,P.,Stålbrand,H.&Janson,J.C.(2002).JournalofBiotechnology,92(3),267-277.
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Twovariantsofanendo-β-1,4-mannanasefromthedigestivetractofbluemussel,Mytilusedulis,werepurifiedbyacombinationofimmobilizedmetalionaffinitychromatography,sizeexclusionchromatographyintheabsenceandpresenceofguanidinehydrochlorideandionexchangechromatography.Thepurifiedenzymeswerecharacterizedwithregardtoenzymaticproperties,molecularweight,isoelectricpoint,aminoacidcompositionandN-terminalsequence.Theyaremonomericproteinswithmolecularmassesof39 216and39 265Da,respectively,asmeasuredbyMALDI-TOFmassspectrometry.Theisoelectricpointsofbothenzymeswereestimatedtobearound7.8,howeverslightlydifferent,byisoelectricfocusinginpolyacrylamidegel.TheenzymesarestablefrompH4.0to9.0andhavetheirmaximumactivitiesatapHabout5.2.Theoptimumtemperatureofbothenzymesisaround50–55°C.Theirstabilitydecreasesrapidlywhengoingfrom40to50°C.TheN-terminalsequences(12residues)wereidenticalforthetwovariants.Theycanbecompletelyrenaturedafterdenaturationin6Mguanidinehydrochloride.TheenzymesreADIlydegradethegalactomannansfromlocustbeangumandivorynutmannanbutshownocross-specificityforxylanandcarboxymethylcellulose.Thereisnobindingabilityobservedtowardscelluloseandmannan.

Introducingporousgraphitizedcarbonliquidchromatographywithevaporativelightscatteringandmassspectrometrydetectionintocellwalloligosaccharideanalysis.

Westphal,Y.,Schols,H.A.,Voragen,A.G.J.&Gruppen,H.(2010).JournalofChromatographyA,1217(5),689-695.
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Separationandcharacterizationofcomplexmixturesofoligosaccharidesisquitedifficultand,dependingonelutionconditions,structuralinformationisoftenlost.Therefore,theuseofaporous-graphitized-carbon(PGC)-HPLC-ELSD-MSn-methodasanalyticaltoolfortheanalysisofoligosaccharidesderivedfromplantcellwallpolysaccharideshasbeeninvestigated.ItisdemonstratedthatPGC-HPLCcanbewidelyusedforneutralandacidicoligosaccharidesderivedfromcellwallpolysaccharides.FurThermore,itisanon-modifyingtechniquethatenablesthecharacterizationofcellwalloligosaccharidescarrying,e.g.acetylgroupsandmethylesters.Neutraloligosaccharidesareseparatedbasedontheirsizeaswellasontheirtypeoflinkageandresulting3D-structure.Seriesoftheplanarβ-(1,4)-xylo-andβ-(1,4)-gluco-oligosaccharidesareretainedmuchmorebythePGCmaterialthantheseriesofβ-(1,4)-galacto-,β-(1,4)-manno-andα-(1,4)-gluco-oligosaccharides.Chargedoligomerssuchasα-(1,4)-galacturonicacidoligosaccharidesarestronglyretainedandareelutedonlyafteradditionoftrifluoroaceticaciddependingontheirnetcharge.Online-MS-couplingusinga1:1splitterenablesquantitativedetectionofELSDaswellassimpleidentificationofmanyoligosaccharides,evenwhenseparationofoligosaccharideswithinacomplexmixtureisnotcomplete.Consequently,PGC-HPLC-separationincombinationwithMS-detectiongivesapowerfultooltoidentifyawiderangeofneutralandacidicoligosaccharidesderivedfromvariouscellwallpolysaccharides.

Influenceofamannanbindingfamily32carbohydratebindingmoduleontheactivityoftheappendedmannanase.

Mizutani,K.,Fernandes,V.O.,Karita,S.,Luís,A.S.,Sakka,M.,Kimura,T.,Jackson,A.,Zhang,X.,Fontes,C.M.G.A.,Gilbert,H.J.&Sakka,K.(2012).AppliedandEnvironmentalMicroBIOLOGy,78(14),4781-4787.
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Ingeneral,cellulasesandhemicellulasesaremodularenzymesinwhichthecatalyticdomainisappendedtooneormorenoncatalyticcarbohydratebindingmodules(CBMs).CBMs,byconcentratingtheparentalenzymeattheirtargetpolysaccharide,increasethecapacityofthecatalyticmoduletobindthesubstrate,leadingtoapotentiationincatalysis.ClostridiumthermocellumhypotheticalproteinCthe_0821,definedhereasC.thermocellumMan5A,isamodularproteincomprisinganN-terminalsignalpeptide,afamily5glycosidehydrolase(GH5)catalyticmodule,afamily32CBM(CBM32),andaC-terminaltypeIdockerinmodule.RecentproteomicstudiesrevealedthatCthe_0821isoneofthemajorcellulosomalenzymeswhenC.thermocellumisculturedoncellulose.HereweshowthattheGH5catalyticmoduleofCthe_0821displaysendomannanaseactivity.C.thermocellumMan5Ahydrolyzessolublekonjacglucomannan,solublecarobgalactomannan,andinsolubleivorynutmannanbutdoesnotattackthehighlygalactosylatedmannanfromguargum,suggestingthattheenzymeprefersunsubstitutedβ-1,4-mannosidelinkages.TheCBM32ofC.thermocellumMan5Adisplaysapreferenceforthenonreducingendsofmannooligosaccharides,althoughtheproteinmoduleexhibitsmeasurableaffinityfortheterminiofβ-1,4-linkedglucooligosaccharidessuchascellobiose.CBM32potentiatestheactivityofC.thermocellumMan5Aagainstinsolublemannansbuthasnosignificanteffectonthecapacityoftheenzymetohydrolyzesolublegalactomannansandglucomannans.TheproductprofileofC.thermocellumMan5AisaffectedbythepresenceofCBM32.

Anon-modularendo-β-1,4-mannanasefromPseudomonasfluorescenssubspeciescellulosa.

Braithwaite,K.L.,Black,G.W.,Hazlewood,G.P.,Ali,B.R.S.&Gilbert,H.J.(1995).Biochem.J,305,1005-1010.
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Pseudomonasfluorescenssubsp.cellulosawhenculturedinthepresenceofcarobgalactomannandegradedthepolysaccharide.Toisolategene(s)fromP.fluorescenssubsp.cellulosaencodingendo-β-1,4-mannanase(mannanase)activity,agenomiclibraryofPseudomonasDNA,constructedinlamBDaZAPII,wasscreenedformannanase-expressingclonesusingthedye-labelledsubstrate,azo-carobgalactomannan.Thenucleotidesequenceofthepseudomonadinsertfromamannanase-positiveclonerevealedasingleopenreadingframeof1257bpencodingaproteinofMr46,938.ThededucedN-terminalsequenceoftheputativepolypeptideconformedtoatypicalprokaryoticsignalpeptide.Truncatedderivativesofthemannanase,lacking54and16residuesfromtheN-andC-terminusrespectivelyofthematureformoftheenzyme,didnotexhibitcatalyticactivity.Inspectionoftheprimarystructureofthemannanasedidnotrevealanyobviouslinkersequencesorproteinmotifscharacteristicofthenon-catalyticdomainslocatedinotherPseudomonasplantcellwallhydrolases.Thesedataindicatethatthemannanaseisnon-modulator,comprisingasinglecatalyticdomain.ComparisonofthemannanasesequencewiththoseintheSWISSPROTdatabaserevealedgreatestsequencehomologywiththemannanasefromBacillussp.ThusthePseudomonasenzymebelongstoglycosylhydrolaseFamily26,afamilycontainingmannanasesandendoglucanases.Analysisofthesubstratespecificityofthemannanaseshowedthattheenzymehydrolysedmannanandgalactomannan,butdisplayedlittleactivitytowardsotherpolysaccharideslocatedintheplantcellwall.TheenzymehadapHoptimumofapprox.7.0,wasresistanttoproteolysisandhadanMrof46,000whenexpressedbyEscherichiacoli.

Restrictedaccessofproteinstomannanpolysaccharidesinintactplantcellwalls.

Marcus,S.E.,Blake,A.W.,Benians,T.A.S,Lee,K.J.,Poyser,C.,Donaldson,L.,Leroux,O.,Rogowski,A.,Petersen,H.L.,Boraston,A.,Gilbert,H.J.,Willats,W.G.T.&PaulKnox,J.(2010).ThePlantJournal,64(2),191-203.
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Howthediversepolysaccharidespresentinplantcellwallsareassembledandinterlinkedintofunctionalcompositesisnotknownindetail.Here,usingtwonovelmonoclonalantibodiesandacarbohydrate-bindingmoduledirectedagainstthemannangroupofhemicellulosecellwallpolysaccharides,weshowthatmolecularrecognitionofmannanpolysaccharidespresentinintactcellwallsisseverelyrestricted.Insecondarycellwalls,mannanesterificationcanpreventproberecognitionofepitopes/ligands,anddetectionofmannansinprimarycellwallscanbeeffectivelyblockedbythepresenceofpectichomogalacturonan.Maskingbypectichomogalacturonanisshowntobeawidespreadphenomenoninparenchymasystems,andmaskedmannanwasfoundtobeafeatureofcellwallregionsatpitfields.Directfluorescenceimagingusingamannan-specificcarbohydrate-bindingmoduleandsequentialenzymetreatmentswithanendo-β-mannanaseconfirmedthepresenceofcrypticepitopesandthatthemaskingofprimarycellwallmannanbypectinisapotentialmechanismforcontrollingcellwallmicro-environments.

Acarbohydratebindingmoduleasadiversity‐carryingscaffold.

Gunnarsson,L.C.,Karlsson,E.N.,Albrekt,A.-S.,Andersson,M.,Holst,O.&Ohlin,M.(2004).ProteinEngineering,Design&Selection,17(3),213-221.
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Thegrowingfieldofbiotechnologyisinconstantneedofbindingproteinswithnovelproperties.Notjustbindingspecificitiesandaffinitiesbutalsostructuralstabilityandproductivityareimportantcharacteristicsforthepurposeoflarge‐scaleapplications.Inordertofindsuchmolecules,librariesarecreatedbydiversifyingnaturallyoccurringbindingproteins,whichinthosecasesserveasscaffolds.Inthisstudy,weinvestigatedtheuseofathermostablecarbohydratebindingmodule,CBM4‐2,fromaxylanasefoundinRhodothermusmarinus,asadiversity‐carryingscaffold.Acombinatoriallibrarywascreatedbyintroducingrestrictedvariationat12positionsinthecarbohydratebindingsiteoftheCBM4‐2.Despitethesmallsizeofthelibrary(1.6×106clones),variantsspecifictowardsdifferentcarbohydratepolymers(birchwoodxylan,Avicelandivorynutmannan)aswellasaglycoprotein(humanIgG4)weresuccessfullyselectedfor,usingthephagedisplaymethod.Investigatedclonesshowedahighproductivity(onaverage69mgofpurifiedprotein/lshakeflaskculture)whenproducedinEscherichiacoliandtheywereallstablemoleculesdisplayingahighmeltingtransitiontemperature(75.7±5.3°C).AllourresultsdemonstratethattheCBM4‐2moleculeisasuitablescaffoldforcreatingvariantsusefulindifferentbiotechnologicalapplications.

Purificationandsomepropertiesofathermostableacidicendo‐β‐1,4‐D‐mannanasefromSclerotium(Athelia)rolfsii.

Sachslehner,A.&Haltrich,D.(1999).FEMSMicrobiologyLetters,177(1),47-55.
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ThephytopathogenicfungusSclerotium(Athelia)rolfsiiformsonemajorendo-β-1,4-D-mannanase(EC3.2.1.78)undernon-inducedandderepressedconditions,i.e.afterdepletionofglucosewhichwasusedastheonlycarbohydratesubstrateforitscultivation.Thismannanasewaspurifiedtoelectrophoretichomogeneitybyammoniumsulfateprecipitation,hydrophobicinteractionchromatography,anionexchangechromatographyandgelfiltration.Theenzymeisaglycoproteinwithamolecularmassof46.5±2kDa(SDS-PAGE),anisoelectricpointof2.75,andapHoptimumof3.0–3.5.Theenzymeisespeciallystableintheacidicregionwithanexceptionalhalf-lifeofactivityof41daysatpH4.5and50°C.Itexertsactivityonβ-1,4-mannanfromivorynut,whichishydrolyzedmainlytomannobioseandmannotriose,aswellasonglucomannan,galactomannan,galactoglucomannan,andmannooligosaccharidesnotsmallerthanmannotetraose.Themainend-productsmannotrioseandtoalesserextentmannobioseinhibititsactivitymoderately.

X4modulesrepresentanewfamilyofcarbohydrate-bindingmodulesthatdisplaynovelproperties.

Bolam,D.N.,Xie,H.,Pell,G.,Hogg,D.,Galbraith,G.,Henrissat,B.&Gilbert,H.J.(2004).JournalofBiologicalChemistry,279(22),22953-22963.
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Thehydrolysisoftheplantcellwallbymicrobialglycosidehydrolasesandesterasesistheprimarymechanismbywhichstoredorganiccarbonisutilizedinthebiosphere,andthustheseenzymesareofconsiderablebiologicalandindustrialimportance.Plantcellwall-degradingenzymesingeneraldisplayamodulararchitecturecomprisingcatalyticandnon-catalyticmodules.TheX4modulesinglycosidehydrolasesrepresentalargefamilyofnon-catalyticmoduleswhosefunctionisunknown.HereweshowthattheX4modulesfromaCellvibriojaponicusmannanase(Man5C)andarabinofuranosidase(Abf62A)bindtopolysaccharides,andthustheseproteinscompriseanewfamilyofcarbohydrate-bindingmodules(CBMs),designatedCBM35.TheMan5C-CBM35bindstogalactomannan,insolubleamorphousmannan,glucomannan,andmanno-oligosaccharidesbutdoesnotinteractwithcrystallinemannan,cellulose,cello-oligosaccharides,orotherpolysaccharidesderivedfromtheplantcellwall.Man5C-CBM35alsopotentiatesmannanaseactivityagainstinsolubleamorphousmannan.Abf62A-CBM35interactswithunsubstitutedoat-speltxylanbutnotsubstitutedformsofthehemicelluloseorxylo-oligosaccharides,andrequirescalciumforbinding.Thisisinsharpcontrasttootherxylan-bindingCBMs,whichinteractinacalcium-independentmannerwithbothxylo-oligosaccharidesanddecoratedxylans.

DigestionofsinglecrystalsofmannanIbyanendo‐mannanasefromTrichodermareesei.

Sabini,E.,Wilson,K.S.,Siika‐aho,M.,Boisset,C.&Chanzy,H.(2000).EuropeanJournalofBiochemistry,267(8),2340-2344.
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TheenzymaticdegradationofsinglecrystalsofmannanIwiththecatalyticcoredomainofaβ-mannanase(EC3.2.1.78orMan5A)fromTrichodermareeseiwasinvestigatedbytransmissionelectronmicroscopyandelectrondiffraction.Theenzymeattacktookplaceattheedgeofthecrystalsandprogressedtowardstheircentres.Quiteremarkablythecrystallineintegrityofthecrystalswaspreservedalmosttotheendofthedigestionprocess.Thisbehaviourisconsistentwithanendo-mechanism,wheretheenzymeinteractswiththeaccessiblemannanchainslocatedatthecrystalperipheryandcleavesonemannanmoleculeatatime.Theendomodeofdigestionofthecrystalswasconfirmedbyananalysisofthesolubledegradationproducts.

DoescelluloseIIexistinnativealgacellwalls?CellulosestructureofDerbesiacellwallsstudiedwithSFG,IRandXRD.

Park,Y.B.,Kafle,K.,Lee,C.M.,Cosgrove,D.J.,&Kim,S.H.(2015).Cellulose,22(6),3531-3540.
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Innature,algaeproducecelluloseIwhereallglucanchainsarealignedparallel.However,thepresenceofcelluloseIIwithanti-parallelglucanchainshasbeenreportedforcertainDerbesia(Chlorophyceaealgae)cellwalls;ifthisistrue,itwouldmeananewbiologicalprocessforsynthesizingcellulosethathasnotyetbeenrecognized.Toanswerthisquestion,weexaminedcellulosestructureinDerbesiacellwalls,intactaswellastreatedwithcelluloseisolationprocedures,usingsum-frequency-generationspectroscopy,infrared(IR)spectroscopyandX-raydiffraction(XRD).Derbesiawallscontainlargeamountsofmannanandsmallamountsofcrystallinecellulose.EvidenceforcelluloseIIintheintactcellwallswasnotfound,whereascelluloseIIinthetrifluoroaceticacid(TFA)treatedcellwallsamplesweredetectedbyIRandXRD.Acontrolexperimentconductedwithball-milledAvicelcellulosesamplesshowedthatcelluloseIIstructurecouldbeformedasaresultofTFAtreatmentanddryingofamorphouscellulose.ThesedatasuggestthatthecelluloseIIstructuredetectedintheTFA-treatedDerbesiagametophytewallsamplesismostlikelyduetoreorganizationofamorphouscelluloseduringthesamplepreparation.OurresultscontradictthepreviousreportofcelluloseIIinnativealgacellwalls.EvenifthecrystallinecelluloseIIexistsinintactDerbesiagametophytecellwalls,itsamountwouldbeverysmall(belowthedetectionlimit)andthusbiologicallyinsignificant.

PurificationandCharacterizationofaThermostableβ-mannanasefromBacillussubtilisBE-91:PotentialApplicationinInflammatoryDiseases.

Cheng,L.,Duan,S.,Feng,X.,Zheng,K.,Yang,Q.&Liu,Z.(2016).BioMedResearchInternational,ArticleID6380147.
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β-mannanasehasshowncompellingbiologicalfunctionsbecauseofitsregulatoryrolesinmetabolism,inflammation,andoxidation.Thisstudyseparatedandpurifiedtheβ-mannanasefromBacillussubtilisBE-91,whichisapowerfulhemicellulose-degradingbacteriumusinga“two-step”methodcomprisingultrafiltrationandgelchromatography.Thepurifiedβ-mannanase(about28.2 kDa)showedhighspecificactivity(79,859.2 IU/mg).TheoptimumtemperatureandpHwere65°Cand6.0,respectively.Moreover,theenzymewashighlystableattemperaturesupto70°CandpH4.5-7.0.Theβ-mannanaseactivitywassignificantlyenhancedinthepresenceofMn+,Cu2+,Zn2+,Ca2+,Mg2+,andAl3+andstronglyinhibitedbyBa2+,andPb2+.KmandVmaxvaluesforlocustbeangumwere7.14 mg/mLand107.5 μmol/min/mLversus1.749 mg/mLand33.45 µmol/min/mLforKonjacglucomannan,respectively.Therefore,β-mannanasepurifiedbythisworkshowsstabilityathightemperaturesandinweaklyacidicorneutralenvironments.Basedonsuchdata,theβ-mannanasewillhavepotentialapplicationsasadietarysupplementintreatmentofinflammatoryprocesses.

InfluenceofStereochemistryonRelativeReactivitiesofGlucosylandMannosylResiduesinKonjacGlucomannan(KGM).

Zhang,Q.&Mischnick,P.(2017).MacromolecularChemistryandPhysics,218(17),1700119.
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MethylationinwaterwithNaOH/MeIisappliedtostudytheinfluenceofthestereochemistryonrelativereactivitiesofD-mannosyl(M)comparedtoD-glucosyl(G)unitsinkonjacglucomannan(KGM).ThepHiskeptconstantat13.6overthecourseofthereactionandaliquotsareremovedaftervarioustimeintervals.MethyldistributioninGandMresiduesisdeterminedafterperethylation,hydrolysis,andconversiontoO-ethyl-O-methyl-alditolacetates.TheorderofrelativerateconstantsdeterminedfortheO-methylKonjacglucomannans(M-KGMs)indegreeofsubstitution(DS)range0.3–0.8isG-k6>M-k6>G-k2≈M-k2>M-k3>G-k3.OligosaccharidesobtainedbypartialhydrolysisafterfullprotectionofM-KGMwithMeI-d3arelabeledwithm-amino-benzoicacidandmeasuredbyliquidchromatography–electrosprayionization–massspectrometry.DS/DPprofilesareinfullagreementwithrandomdistributionofmethylgroups.ThermalpropertiesofM-KGMsareanalyzedbydifferentialscanningcalorimetryandthermogravimetricanalysis.DecompositiontemperatureincreaseswithDS,whilethetemperatureofanendothermicchangedecreases.

GeneticandfunctionalcharacterizationofanovelGH10endo-β-1,4-xylanasewitharicin-typeβ-trefoildomain-likedomainfromLuteimicrobiumxylanilyticumHY-24.(2017).

Kim,D.Y.,Lee,S.H.,Lee,M.J.,Cho,H.Y.,Lee,J.S.,Rhee,Y.H.,Shin,D.H.,SonK.H.&Park,H.Y.InternationalJournalofBiologicalMacromolecules,InPress.
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Thegene(1488-bp)encodinganovelGH10endo-β-1,4-xylanase(XylM)consistingofanN-terminalcatalyticGH10domainandaC-terminalricin-typeβ-trefoillectindomain-like(RICIN)domainwasidentifiedfromLuteimicrobiumxylanilyticumHY-24.TheGH10domainofXylMwas72%identicaltothatofMicromonosporalupineendo-β-1,4-xylanaseandtheRICINdomainwas67%identicaltothatofActinospicarobiniaehypotheticalprotein.Therecombinantenzyme(rXylM:49kDa)exhibitedmaximumactivitytowardbeechwoodxylanat65°CandpH6.0,whiletheoptimumtemperatureandpHofitsC-terminaltruncatedmutant(rXylM△RICIN:35kDa)were45°Cand5.0,respectively.Afterpre-incubationof1hat60°C,rXylMretainedover80%ofitsinitialactivity,butthethermostabilityofrXylM△RICINwassharplydecreasedattemperaturesexceeding40°C.Thespecificactivity(254.1Umg-1)ofrXylMtowardoatspeltsxylanwas3.4-foldhigherthanthat(74.8Umg-1)ofrXylM△RICINwhenthesamesubstratewasused.rXylMdisplayedsuperiorbindingcapacitiestoligninandinsolublepolysaccharidescomparedtorXylM△RICIN.Enzymatichydrolysisofβ-1,4-D-xylooligosaccharides(X3-X6)andbirchwoodxylanyieldedX3asthemajorproduct.TheresultssuggestthattheRICINdomaininXylMmightplayanimportantroleinsubstrate-bindingandbiocatalysis.
megazyme 官网megazyme 中国代理 Megazyme代理，Megazyme上海代理，Megazyme北京代理，Megazyme广州代理，Megazyme总代理，Megazyme一级代理，Megazyme特约代理，Megazyme授权代理 Megazyme现货上海金畔生物科技有限公司是Megazyme专业代理商。    爱尔兰Megazyme是一家全球*的制造和供应高品质和创新的检测谷物，食品，饲料，发酵，乳制品和葡萄酒行业的技术。Megazyme成立于1988年，该公司目前提供了超过70种诊断试剂盒和超过300种其他试剂和底物。 该公司产品分以下系列： 1. 生物及食品酶法分析试剂盒 (Diagnostic Kits) 2. 试剂混合物(Reagent Mixtures) 3. 协同因子(Cofactors) 4. 糖酶片剂试验(Carbohydrase Tablet Tests) 5. 蛋白酶片剂试验(Protease Test Tablets) 6. 可溶性呈色底物(Soluble Chromogenic Substrates) 7. 不可溶性（交联的）呈色底物(Insoluble (Crosslinked) Chromogenic Substrates) 8. 酶(Enzymes) 9. 植物凝血素(Lectins) 10. 多聚糖(Polysaccharides) 11. 低聚糖(Oligosaccharides) 12. 相关产品 (General) Megazyme公司简介： Megazyme公司位于美丽的爱尔兰 ，是全球知名的酶及酶法分析试剂盒供应商， 他们的很多产品都被AOAC(Association of Official Analytical Chemists)、(European Brewing Convention)、RACI (Royal Australian Chemical Institute) 等国际组织采用，Megazyme公司分析试剂盒广泛应用于食品、饲料、乳品、发酵工业、葡萄糖生产及成品控制，其中欧洲检测果汁及葡萄酒等发酵产品基本都采用Megazyme公司的产品。 Lumiprobe代理（Cy系列活性荧光染料） wako日本和光代理(表面张力测试试剂、日立氨基酸分析仪配套试剂、低聚果糖标准品、Anti Iba1, Rabbit抗体)  日本关东化学Kanto试剂代理  日本柴田科学Sibata代理 日本Advantec滤纸滤膜代理 日本共立理化学代理  Megazyme代理  Hampton代理（蛋白结晶） whatman代理（whatman滤膜、whatman滤纸） 金畔生物修饰性PEG(单分散短链小分子PEG)  Laysan bio修饰性PEG代理  NANOC进口PEG代理  Avanti进口修饰性PEG代理  GE代理（蛋白纯化柱及填料）  Amresco代理  Sigma优势代理  Roche酶代理 TCI代理  MPbio代理（动物肠膜炎DSS） Merck Millipore代理   NEB酶代理  Abcam代理  CST代理  Santa Cruz代理  Biolegend代理 Invitrogen代理   millipore代理  BD流式抗体代理   GeneTe x抗体代理  Novus抗体代理  R&D代理  ebioscience代理  Biovison代理  Jackson代理  MBL抗体代理  ProSpec抗体代理  Bethyl抗体代理  Antibody Revolution抗体代理  Torrey?Pines?Biolabs代理 Toyobo酶代理  TRC标准品代理 USP代理  EP代理  Dr代理 Reagecon代理   Corning康宁（培养皿、培养板）代理  Axygen代理  Falcon耗材代理   Nunc耗材代理 Nalgene耐洁耗材代理  NEST耗材代理  OXOID代理 NISSUI日水培养基代理 Himedia培养基代理 BD培养基代理（灭活结核杆菌231141） Cellgro培养基代理   Eppendorf代理  Bio-Rad伯乐代理  wheaton代理 Labnet代理  Rearch dites、Harlan品牌动物饲料代理 标准品代理 抗体代理 酶试剂代理Elisa试剂盒代理、柔软型灌胃针 小鼠灌胃针、小鼠记号笔、进口动物玩具 动物投药胶囊。 公司简介 上海金畔生物科技有限公司提供生命科学研究领域系列产品，包括色谱标准品、生化试剂、诊断试剂、实验耗材和仪器。Laysanbio、Avanti、NANOCS品牌的修饰性PEG（修饰性聚乙二醇）、WAKO品牌的表面张力测试剂、WAKO品牌的日立氨基酸分析仪配套试剂-缓冲液、显色液、Lumiprobe品牌的标记分子氨基活性染料。免疫诊断试剂包括Roche、TOYOBO、NEB品牌的酶、Abcam、CST、Santa Cruz品牌的单克隆抗体、多克隆抗体RDh和Biovison品牌的ELisa试剂盒、MP bio品牌的DNA提取试剂盒等多种产品。标准品包括美国APSC品牌分子质量测量高分子量标准品、德国DR和TRC以及药典USP、EP、中检所品牌标准品、Reagecon品牌的离子和各种金属标准品、耗材和仪器包括NUSSUI、BD difco、OXIOD品牌的培养基、whatmna、Millipore品牌的各种滤膜、滤器和柱子填料等、Reseach diets品牌的动物饲料、Labnet、康宁Coring、Axygen、Falcon 、Eppendorf品牌的离心机离心管、移液枪及枪头等实验室常用仪器耗材。