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商品描述
HighpurityPecticGalactan(Lupin)foruseinresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Highlypurified,water-solublepolysaccharideextractedwithalkalifromlupinfiber.Gal:Ara:Rha:Xyl:GalUA=77:14:3:0.6:5.4
Effectofnanocoatingwithrhamnogalacturonan‐Ionsurfacepropertiesandosteoblastsresponse.
Gurzawska,K.,Svava,R.,Syberg,S.,Yihua,Y.,Haugshøj,K.B.,Damager,I.,Ulvskov,P.,Christensen,L.H.,Gotfredsen,K.&Jørgensen,N.R.(2012).JournalofBiomedicalMaterialsResearchPartA,100(3),654-664.
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Long-termstABIlityoftitaniumimplantsaredependentonavarietyoffactors.Nanocoatingwithorganicmoleculesisoneofthemethodsusedtoimproveosseointegration.Therefore,theaimofthisstudyistoevaluatetheinvitroeffectofnanocoatingwithpecticrhamnogalacturonan-I(RG-I)onsurfacepropertiesandosteoblastsresponse.ThreedifferentRG-Isfromappleandlupinpectinsweremodifiedandcoatedonamino-functionalizedtissueculturepolystyreneplates(aminatedTCPS).Surfacepropertieswereevaluatedbyscanningelectronmicroscopy,contactanglemeasurement,atomicforcemicroscopy,andX-rayphotoelectronspectroscopy.Theeffectsofnanocoatingonproliferation,matrixformationandmineralization,andexpressionofgenes(real-timePCR)relatedtoosteoblastdifferentiationandactivityweretestedusinghumanosteoblast-likeSaOS-2cells.ItwasshownthatRG-Icoatingsaffectedthesurfaceproperties.AllthreeRG-Iinducedbonematrixformationandmineralization,whichwasalsosupportedbythefindingthatgeneexpressionlevelsofalkalinephosphatase,osteocalcin,andcollagentype-1wereincreasedincellsculturedontheRG-Icoatedsurface,indicatingamoredifferentiatedosteoblasticphenotype.ThismakesRG-Icoatingapromisingandnovelcandidatefornanocoatingsofimplants.
Characterizationofanexo-β-1,3-galactanasefromClostridiumThermocellum.
Ichinose,H.,Kuno,A.,Kotake,T.,Yoshida,M.,Sakka,K.,Hirabayashi,J.,Tsumuraya,Y.&Kaneko,S.(2006).AppliedandEnvironmentalMicroBIOLOGy,72(5),3515-3523.
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Ageneencodinganexo-β-1,3-galactanasefromClostridiumthermocellum,Ct1,3Gal43A,wasisolated.Thesequencehassimilaritywithanexo-β-1,3-galactanaseofPhanerochaetechrysosporium(Pc1,3Gal43A).ThegeneencodesamodularproteinconsistingofanN-terminalglycosidehydrolasefamily43(GH43)module,afamily13carbohydrate-bindingmodule(CBM13),andaC-terminaldockerindomain.ThegenecorrespondingtotheGH43modulewasexpressedinEscherichiacoli,andthegeneproductwascharacterized.TherecombinantenzymeshowsoptimalactivityatpH6.0and50°Candcatalyzeshydrolysisonlyofβ-1,3-linkedgalactosyloligosaccharidesandpolysaccharides.High-performanceliquidchromatographyanalysisofthehydrolysisproductsdemonstratedthattheenzymeproducesgalactosefromβ-1,3-galactaninanexo-actingmanner.Whentheenzymeactedonarabinogalactanproteins(AGPs),theenzymeproducedoligosaccharidestogetherwithgalactose,suggestingthattheenzymeisabletoaccommodateaβ-1,6-linkedgalactosylsidechain.ThesubstratespecificityoftheenzymeisverysimilartothatofPc1,3Gal43A,suggestingthattheenzymeisanexo-β-1,3-galactanase.AffinitygelelectrophoresisoftheC-terminalCBM13didnotshowanyaffinityforpolysaccharides,includingβ-1,3-galactan.However,frontalaffinitychromatographyfortheCBM13indicatedthattheCBM13specificallyinteractswitholigosaccharidescontainingaβ-1,3-galactobiose,β-1,4-galactosylglucose,orβ-1,4-galactosylN-acetylglucosaminidemoietyatthenonreducingend.Interestingly,CBM13intheCterminusofCt1,3Gal43Aappearedtointerferewiththeenzymeactivitytowardβ-1,3-galactanandα-L-arabinofuranosidase-treatedAGP.
Anexo-β-1,3-galactanasehavinganovelβ-1,3-galactan-bindingmodulefromPhanerochaetechrysosporium.
Ichinose,H.,Yoshida,M.,Kotake,T.,Kuno,A.,Igarashi,K.,Tsumuraya,Y.,Samejima,M.,Hirabayashi,J.,Kobayashi,H.&Kaneko,S.(2005).JournalofBiologicalChemistry,280(27),25820-25829.
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Anexo-β-1,3-galactanasegenefromPhanerochaetechrysosporiumhasbeencloned,sequenced,andexpressedinPichiapastoris.Thecompleteaminoacidsequenceoftheexo-β-1,3-galactanaseindicatedthattheenzymeconsistsofanN-terminalcatalyticmodulewithsimilaritytoglycosidehydrolasefamily43andanadditionalunknownfunctionaldomainsimilartocarbohydrate-bindingmodulefamily6(CBM6)intheC-terminalregion.Themolecularmassoftherecombinantenzymewasestimatedas55kDabasedonSDS-PAGE.Theenzymeshowedreactivityonlytowardβ-1,3-linkedgalactosyloligosaccharidesandpolysaccharideassubstratesbutdidnothydrolyzeβ-1,4-linkedgalacto-oligosaccharides,β-1,6-linkedgalacto-oligosaccharides,pecticgalactan,larcharabinogalactan,arabinan,gumarabic,debranchedarabinan,laminarin,solublebirchwoodxylan,orsolubleoatspelledxylan.Theenzymealsodidnothydrolyzeβ-1,3-galactosylgalactosaminide,β-1,3-galactosylglucosaminide,orβ-1,3-galactosylarabinofuranoside,suggestingthatitspecificallycleavestheinternalβ-1,3-linkageoftwogalactosylresidues.Highperformanceliquidchromatographicanalysisofthehydrolysisproductsshowedthattheenzymeproducedgalactosefromβ-1,3-galactaninanexo-actingmanner.However,noactivitytowardp-nitrophenylβ-galactopyranosidewasdetected.Whenincubatedwitharabinogalactanproteins,theenzymeproducedoligosaccharidestogetherwithgalactose,suggestingthatitisabletobypassβ-1,6-linkedgalactosylsidechains.TheC-terminalCBM6didnotshowanyaffinityforknownsubstratesofCBM6suchasxylan,cellulose,andβ-1,3-glucan,althoughitboundβ-1,3-galactanwhenanalyzedbyaffinityelectrophoresis.FrontalaffinitychromatographyfortheCBM6moietyusingseveralkindsofterminalgalactose-containingoligosaccharidesastheanalytesclearlyindicatedthattheCBM6specificallyinteractedwitholigosaccharidescontainingaβ-1,3-galactobiosemoiety.Whenthedegreeofpolymerizationofgalactoseoligomerswasincreased,thebindingaffinityoftheCBM6showednomarkedchange.
Family6carbohydrate‐bindingmodulesdisplaymultipleβ1,3‐linkedglucan‐specificbindinginterfaces.
Correia,M.A.S.,Pires,V.M.R.,Gilbert,H.J.,Bolam,D.N.,Fernandes,V.O.,Alves,V.D.,Prates,J.A.M.,Ferreira,L.M.A.&Fontes,C.M.G.(2009).FEMSMicrobiologyLetters,300(1),48-57.
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Noncatalyticcarbohydrate-bindingmodules(CBMs),whicharefoundinavarietyofcarbohydrate-degrADIngenzymes,havebeengroupedintosequence-basedfamilies.CBMs,byrecruitingtheirappendedenzymesontothesurfaceofthetargetsubstrate,potentiatecatalysisparticularlyagainstinsolublesubstrates.Family6CBMs(CBM6s)displayunusualpropertiesinthattheypresenttwopotentialligand-bindingsitestermedcleftsAandB,respectively.CleftBislocatedontheconcavesurfaceoftheβ-sandwichfoldwhilecleftA,themorecommonbindingsite,isformedbytheloopsthatconnecttheinnerandtheouterβ-sheets.Here,wereportthebiochemicalpropertiesofCBM6-1fromCellvibriomixtusCmCel5A.ThedatarevealthatCBM6-1specificallyrecognizesβ1,3-glucansthroughresidueslocatedbothincleftAandincleftB.Incontrast,apreviousreportshowedthataCBM6derivedfromaBacillushaloduranslaminarinasebindstoβ1,3-glucansonlyincleftA.Thesestudiesrevealadifferentmechanismbywhichahighlyconservedproteinplatformcanrecognizeβ1,3-glucans.
Real-timeimagingofcellulosereorientationduringcellwallexpansioninArabidopsisroots.
Anderson,C.T.,Carroll,A.,Akhmetova,L.&Somerville,C.(2010).PlantPhysiology,152(2),787-796.
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Celluloseformsthemajorload-bearingnetworkoftheplantcellwall,whichsimultaneouslyprotectsthecellanddirectsitsgrowth.Althoughtheprocessofcellulosesynthesishasbeenobserved,littleisknownaboutthebehaviorofcelluloseinthewallaftersynthesis.UsingPontamineFastScarlet4B,adyethatfluorescespreferentiallyinthepresenceofcelluloseandhasexcitationandemissionwavelengthssuitableforconfocalmicroscopy,weimagedthearchitectureanddynamicsofcelluloseinthecellwallsofexpandingrootcells.WefoundthatcelluloseexistsinArabidopsis(Arabidopsisthaliana)cellwallsinlargefibrillarbundlesthatvaryinorientation.Duringanisotropicwallexpansioninwild-typeplants,weobservedthatthesecellulosebundlesrotateinatransversetolongitudinaldirection.Wealsofoundthatcelluloseorganizationissignificantlyalteredinmutantslackingeitheracellulosesynthasesubunitortwoxyloglucanxylosyltransferaseisoforms.Ourresultssupportamodelinwhichcelluloseisdepositedtransverselytoaccommodatelongitudinalcellexpansionandreorientedduringexpansiontogenerateacellwallthatisfortifiedagainststrainfromanydirection.
