Megazyme/Curdlan/P-CURDL/8 grams
商品编号：
P-CURDL
品牌：
Megazyme INC
市场价：
¥3288.00
美元价：
1972.80
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
HighpurityCurdlanforuseinresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Purity>95%.1,3-β-D-Glucan.Fortheassayofendo-1,3-β-D-glucanase.
UnravellingGlucanRecognitionSystemsbyGlycomeMicroarraysUsingtheDesignerApproachandMassSpectrometry.
Palma,A.S.,Liu,Y.,Zhang,H.,Zhang,Y.,McCleary,B.V.,Yu,G.,Huang,Q.,Guidolin,L.S.,Ciocchini,A.E.,Torosantucci,A.,Wang,D.,Carvalho,A.L.,Fontes,C.M.G.A.,Mulloy,B.,Childs,R.A.,Feizi,T.&Chai,W.(2015).Mol.CellProteomics,14(4),974-988.
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GlucansarepolymersofD-glucosewithdifferinglinkagesinlinearorbranchedsequences.Theyareconstituentsofmicrobialandplantcell-wallsandinvolvedinimportantbio-recognitionprocesses,includingimmunomodulation,anticanceractivities,pathogenvirulence,andplantcell-wallbiodegradation.Translationalpossibilitiesfortheseactivitiesinmedicineandbiotechnologyareconsiderable.High-throughputmicro-methodsareneededtoscreenproteinsforrecognitionofspecificglucansequencesasaleadtostructure–functionstudiesandtheirexploitation.Wedescribeconstructionofa“glucome”microarray,thefirstsequence-definedglycome-scalemicroarray,usinga“designer”approachfromtargetedligand-bearingglucansinconjunctionwithanovelhigh-sensitivitymassspectrometricsequencingmethod,asascreeningtooltoassignglucanrecognitionmotifs.Theglucomemicroarraycomprises153oligosaccharideprobeswithhighpurity,representingmajorsequencesinglucans.Negative-ionelectrospraytandemmassspectrometrywithcollision-induceddissociationwasusedforcompletelinkageanalysisofgluco-oligosaccharidesinlinear“homo”and“hetero”andbranchedsequences.Thesystemisvalidatedusingantibodiesandcarbohydrate-bindingmodulesknowntotargetα-orβ-glucansindifferentBIOLOGicalcontexts,extendingknowledgeontheirspecificities,andappliedtorevealnewinformationonglucanrecognitionbytwosignalingmoleculesoftheimmunesystemagainstpathogens:Dectin-1andDC-SIGN.ThesequencingoftheglucanoligosaccharidesbytheMSmethodandtheirinterrogationonthemicroarraysprovidesdetailedinformationonlinkage,sequenceandchainlengthrequirementsofglucan-recognizingproteins,andareasensitivemeansofrevealingunsUSPectedsequencesinthepolysaccharides.
Molecularcharacterizationofpolysaccharidesinhot-waterextractsofGanodermalucidumfruitingbodies.
Chang,Y.W.&Lu,T.J.(2004).JournalofFoodandDrugAnalysis,12(1),59-67.
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Polysaccharidecomponentsinhot-waterextractofGanodermalucidumfruitingbodieswereseparatedandtheirmolecularweightsanddistributionprofilesweremeasuredusinghigh-performancesize-exclusionchromatographywithmulti-anglelaserlightscatteringdetection(HPSEC-MALLS).Threepolysaccharidegroupswerefoundintheextractwithaweightpercentageof31,46and23%respectively.Theweight-averagemolecularweightsofthesegroupswere2.08x106,2.3x104,and1.2x104g/mol,respectively.Therepresentativefractionsofthese3groupswereobtainedusingdifferentialprecipitationwithethanolat20,60and80%(v/v)concentrationsforfurtherpropertystudy.Thefirstgroupthathadthelargestmolecularsizewasbranched(1→3)-β-D-glucanwithsingleβ-DglucosylsidechainsattheO-6positions,asrevealedfromsugarcompositionanalysis,anilineblueassayand1H-and13C-NMRspectroscopy.(1→3,1→6)-β-D-glucanwasthemajoractivepolysaccharideandshowedsignificanttumornecrosisfactor-α(TNF-α)releasingstimulationactivityfromhumanmononuclearcells(MNC).Theglucanwasslightlysolubleinwateratambienttemperature.ThesecondandthirdgroupsthatshowedslightmodulatingactivityconsistedofD-glucose,D-galactoseandD-mannoseatdifferentratios.AggregationofpolysaccharidemoleculeswasalsorevealedbyHPSEC-MALLSstudy.
Endo-β-1,3-glucanaseGLU1,fromthefruitingbodyofLentinulaedodes,belongstoanewglycosidehydrolasefamily.
Sakamoto,Y.,Nakade,K.&Konno,N.(2011).AppliedandEnvironmentalMicrobiology,77(23),8350-8354.
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ThecellwallofthefruitingbodyofthemushroomLentinulaedodesisdegradedafterharvestingbyenzymessuchasβ-1,3-glucanase.Inthisstudy,anovelendo-typeβ-1,3-glucanase,GLU1,waspurifiedfromL.edodesfruitingbodiesafterharvesting.Thegeneencodingit,glu1,wasisolatedbyrapidamplificationofCDNAends(RACE)-PCRusingprimersdesignedfromtheN-terminalaminoacidsequenceofGLU1.Theputativeaminoacidsequenceofthematureproteincontained247aminoacidresidueswithamolecularmassof26kDaandapIof3.87,andrecombinantGLU1expressedinPichiapastorisexhibitedβ-1,3-glucanaseactivity.GLU1catalyzeddepolymerizationofglucanscomposedofβ-1,3-linkedmainchains,andreactionproductanalysisbythin-layerchromatography(TLC)clearlyindicatedthattheenzymehadanendolyticmode.However,theaminoacidsequenceofGLU1showednosignificantsimilaritytoknownglycosidehydrolases.GLU1hassimilaritytoseveralhypotheticalproteinsinfungi,andGLU1andhighlysimilarproteinsshouldbeclassifiedasanovelglycosidehydrolasefamily(GH128).
Modulationoftheimmuneresponseofporcineneutrophilsbydifferentβ-glucanpreparations.
Juul-Madsen,H.R.,Norup,L.&Lærke,H.N.(2010).Livestockscience,133(1),249-252.
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β-glucansofbacterialandfungaloriginareknownimmuno-modulators,butdataintheliteraturealsoindicatethatlichenandcereal-derivedβ-glucansmayhaveimmuno-modulatoryfunctions.Theaimofthecurrentstudywastotesttheeffectofdifferentsourcesofβ-glucansonneutrophilsinanex-vivowholebloodstimulationassay.Wholebloodsampleswereeithertreatedwithcurdlan,alinearβ-(1→3)-D-glucanfromthenon-pathogenicAlcaligenesfaecalis,lichenan,amixedlinkedβ-(1→3),(1→4)-D-glucanfromIslandicmoss(Cetrariaislandica)orzymosan,preparedfromyeastcellwallsandbeingrichinbranchedβ–(1→3),(1→6)–D-glucan.Thebloodcellwereeitherstimulatedaloneorincombinationwithlipopolysaccharide(LPS)andcomparedwithLPS-treatedanduntreatedcontrolsamples.PreliminaryresultsshowthatZymosan,hadadifferenteffectthanlichenanandcurdlan,onthesurfaceexpressionofToll-likeReceptor(TLR)2and4,butnotsignificantlyonthesignalregulatoryproteinSIRPαafterastimulationeitheraloneorincombinationwithLPS.Thus,branchingmayappeartobeimportantforthedifferenteffect,butaneffectofimpuritiesintheZymosanpreparationcannotberuledout.
Plantproductionofanti‐β‐glucanantibodiesforimmunotherapyoffungalinfectionsinhumans.
Capodicasa,C.,Chiani,P.,Bromuro,C.,DeBernardis,F.,Catellani,M.,Palma,A.S.,Liu,Y.,Feiz,T.,Cassone,A.,Benvenuto,E.&Torosantucci,A.(2011).PlantBiotechnologyJournal,9(7),776-787.
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Thereisanincreasinginterestinthedevelopmentoftherapeuticantibodies(Ab)toimprovethecontroloffungalpathogens,butnoneofthesereagentsisavailableforclinicaluse.Wepreviouslydescribedamurinemonoclonalantibody(mAb2G8)targetingβ-glucan,acellwallpolysaccharidecommontomostpathogenicfungi,whichconferredsignificantprotectionagainstCandidaalbicans,AspergillusfumigatusandCryptococcusneoformansinanimalmodels.Transferofthiswide-spectrum,antifungalmAbintotheclinicalsettingwouldallowthecontrolofmostfrequentfungalinfectionsinmanydifferentcategoriesofpatients.Tothisaim,twochimericmouse–humanAbderivativesfrommAb2G8,intheformatofcompleteIgGorscFv-Fc,weregenerated,transientlyexpressedinNicotianabenthamianaplantsandpurifiedfromleaveswithhighyields(approximately50mgAb/kgofplanttissues).BothrecombinantAbsfullyretainedtheβ-glucan-bindingspecificityandtheantifungalactivitiesofthecognatemurinemAbagainstC.albicans.Infact,theyrecognizedpreferentiallyβ1,3-linkedglucanmoleculespresentatthefungalcellsurfaceanddirectlyinhibitedthegrowthofC.albicansanditsadhesiontohumanepithelialcellsinvitro.Inaddition,boththeIgGandthescFv-FcpromotedC.albicanskillingbyisolated,humanpolymorphonuclearneutrophilsinexvivoassaysandconferredsignificantantifungalprotectioninanimalmodelsofsystemicorvulvovaginalC.albicansinfection.TheserecombinantAbsrepresentvaluablemoleculesfordevelopingnovel,plant-derivedimmunotherapeuticsagainstcandidiasisand,possIBLy,otherfungaldiseases.
Characterizationofabroad-specificityβ-glucanaseactingonβ-(1,3)-,β-(1,4)-,andβ-(1,6)-glucansthatdefinesanewglycosidehydrolasefamily.
Lafond,M.,Navarro,D.,Haon,M.,Couturier,M.&Berrin,J.G.(2012).AppliedandEnvironmentalMicrobiology,78(24),8540-8546.
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HerewereportthecloningofthePa_3_10940genefromthecoprophilicfungusPodosporaanserina,whichencodesaC-terminalfamily1carbohydratebindingmodule(CBM1)linkedtoadomainofunknownfunction.Thefunctionofthegenewasinvestigatedbyexpressionofthefull-lengthproteinandatruncatedderivativewithouttheCBM1domainintheyeastPichiapastoris.Usingalibraryofpolysaccharidesofdifferentorigins,wedemonstratedthatthefull-lengthenzymedisplaysactivitytowardabroadrangeofβ-glucanpolysaccharides,includinglaminarin,curdlan,pachyman,lichenan,pustulan,andcellulosicderivatives.Analysisoftheproductsreleasedfrompolysaccharidesrevealedthatthisβ-glucanaseisanexo-actingenzymeonβ-(1,3)-andβ-(1,6)-linkedglucansubstratesandanendo-actingenzymeonβ-(1,4)-linkedglucansubstrates.Hydrolysisofshortβ-(1,3),β-(1,4),andβ-(1,3)/β-(1,4)gluco-oligosaccharidesconfirmedthisstrikingfeatureandrevealedthattheenzymeperformsinanexo-typemodeonthenonreducingendofgluco-oligosaccharides.ExcisionoftheCBM1domainresultedinaninactiveenzymeonallsubstratestested.Toourknowledge,thisisthefirstreportofanenzymethatdisplaysbifunctionalexo-β-(1,3)/(1,6)andendo-β-(1,4)activitiestowardbeta-glucansandthereforecannotreADIlybeassignedtoexistingEnzymeCommissiongroups.Theaminoacidsequencehashighsequenceidentitytohypotheticalproteinswithinthefungaltaxaandthusdefinesanewfamilyofglycosidehydrolases,theGH131family.
Characterizationandthree-dimensionalstructuresoftwodistinctbacterialxyloglucanasesfromfamiliesGH5andGH12.
Gloster,T.M.,Ibatullin,F.M.,Macauley,K.,Eklöf,J.M.,Roberts,S.,Turkenburg,J.P.,Bjørnvad,M.E.,Jørgensen,P.L.,Danielsen,S.,Johansen,K.S.,Borchert,T.V.,Wilson,K.S.,Brumer,H.&Davies,G.J.(2007).JournalofBiologicalChemistry,282(26),19177-19189.
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Theplantcellwallisacomplexmaterialinwhichthecellulosemicrofibrilsareembeddedwithinameshofotherpolysaccharides,someofwhicharelooselytermed“hemicellulose.”Onesuchhemicelluloseisxyloglucan,whichdisplaysaβ-1,4-linkedD-glucosebackbonesubstitutedwithxylose,galactose,andoccasionallyfucosemoieties.Bothxyloglucanandtheenzymesresponsibleforitsmodificationanddegradationarefindingincreasingprominence,reflectingboththedriveforenzymaticbiomassconversion,theirroleindetergentapplications,andtheutilityofmodifiedxyloglucansforcellulosefibermodification.Herewepresenttheenzymaticcharacterizationandthree-dimensionalstructuresinligand-freeandxyloglucan-oligosaccharidecomplexedformsoftwodistinctxyloglucanasesfromglycosidehydrolasefamiliesGH5andGH12.Theenzymes,PaenibacilluspabuliXG5andBacilluslicheniformisXG12,bothdisplayopenactivecentergroovesgraftedupontheirrespective(β/α)8andβ-jellyrollfolds,inwhichthesidechaindecorationsofxyloglucanmaybeaccommodated.Fortheβ-jellyrollenzymetopologyofGH12,bindingofxylosylandpendantgalactosylmoietiesistolerated,buttheenzymeissimilarlycompetentinthedegradationofunbranchedglucans.Inthecaseofthe(β/α)8GH5enzyme,kineticallyproductiveinteractionsaremadewithbothxyloseandgalactosesubstituents,asreflectedinbothahighspecificactivityonxyloglucanandthekineticsofaseriesofarylglycosides.Thedifferentialstrategiesfortheaccommodationofthesidechainsofxyloglucanpresumablyfacilitatetheactionofthesemicrobialhydrolasesinmilieuswherediverseanddifferentlysubstitutedsubstratesmaybeencountered.
AnEndoglucanase,EglA,fromtheHyperThermophilicArchaeonPyrococcusfuriosusHydrolyzesβ-1,4BondsinMixed-Linkage(1→3),(1→4)-β-D-GlucansandCellulose.
Bauer,M.W.,Driskill,L.E.,Callen,W.,Snead,M.A.,Mathur,E.J.&Kelly,R.M.(1999).JournalofBacteriology,181(1),284-290.
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TheeglAgene,encodingathermostableendoglucanasefromthehyperthermophilicarchaeonPyrococcusfuriosus,wasclonedandexpressedinEscherichiacoli.Thenucleotidesequenceofthegenepredictsa319-amino-acidproteinwithacalculatedmolecularmassof35.9kDa.Theendoglucanasehasa19-amino-acidsignalpeptidebutnotcellulose-bindingdomain.TheP.furiosusendoglucanasehassignificantaminoacidsequencesimilarities,includingtheconservedcatalyticnucleophileandprotondonor,withendoglucanasesfromglucosylhydrolasefamily12.Thepurifiedrecombinantenzymehydrolyzedβ-1,4butnotβ-1,3glucosidiclinkagesandhadthehighestspecificactivityoncellopentaose(degreeofpolymerization[DP]=5)andcellohexaose(DP=6)oligosaccharides.Toalesserextent,EglAalsohydrolyzedshortercellodextrins(DP<5)=""as=""well=""as=""the=""amorphous=""portions=""of=""polysaccharides=""which=""contain=""only=""β-1,4=""bonds=""such=""as=""carboxymethyl=""cellulose,=""microcrystalline=""cellulose,=""whatman=""paper,=""and=""cotton=""linter.=""the=""highest=""specific=""activity=""toward=""polysaccharides=""occurred=""with=""mixed-linkage=""β-glucans=""such=""as=""barley=""β-glucan=""and=""lichenan.=""kinetics=""studies=""with=""cellooliogsaccharides=""and="">p-nitrophenyl-cellooligosaccharidesindicatedthattheenzymehadthreeglucosebindingsubsites(−I,−II,and−III)forthenonreducingendandtwoglucosebindingsubsites(+Iand+II)forthereducingendfromthescissileglycosidiclinkage.TheenzymehadtemperatureandpHoptimaof100°Cand6.0,respectively;ahalf-lifeof40hat95°C;andadenaturingtemperatureof112°Casdeterminedbydifferentialscanningcalorimetry.Thediscoveryofathermostableenzymewiththissubstratespecificityhasimplicationsforboththeevolutionofenzymesinvolvedinpolysaccharidehydrolysisandtheoccurrenceofgrowthsubstratesinhydrothermalventenvironments.
Ligandsfortheβ-glucanreceptor,Dectin-1,assignedusing“designer”microarraysofoligosaccharideprobes(neoglycolipids)generatedfromglucanpolysaccharides.
Palma,A.S.,Feizi,T.,Zhang,Y.,Stoll,M.S.,Lawson,A.M.,Díaz-Rodríguez,E.,Campanero-Rhodes,M.A.,Costa,J.L.,Gordon,S.,Brown,G.D.&Chai,W.(2006).JournalofBiologicalChemistry,281(9),5771-5779.
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Dectin-1isaC-typelectin-likereceptoronleukocytesthatmediatesphagocytosisandinflammatorymediatorproductionininnateimmunitytofungalpathogens.Dectin-1lacksresiduesinvolvedincalciumligationthatmediatescarbohydrate-bindingbyclassicalC-typelectins;nevertheless,itbindszymosan,aparticulateβ-glucan-richextractofSaccharomycescerevisiae,andbindingisinhibitedbypolysaccharidesrichinβ1,3-orbothβ1,3-andβ1,6-linkedglucose.TheoligosaccharideligandsonglucansrecognizedbyDectin-1havenotyetbeendelineatedprecisely.ItisalsonotknownwhetherDectin-1caninteractwithothertypesofcarbohydrates.Wehaveinvestigatedthis,sinceDectin-1showsglucan-independentbindingtoasubsetofT-lymphocytesandisinvolvedintriggeringtheirproliferation.HereweassignoligosaccharideligandsforDectin-1usingtheneoglycolipid-basedoligosaccharidemicroarraytechnology,auniqueapproachforconstructingmicroarraysoflipid-linkedoligosaccharideprobesfromdesiredsources.Wegenerate“designer”microarraysfromthreeglucanpolysaccharides,aneutralsolubleglucanisolatedfromS.cerevisiaeandtwobacterialglucans,curdlanfromAlcaligenesfaecalisandpustulanfromUmbilicariapapullosa,andusetheseinconjunctionwith187diverse,sequence-defined,predominantlymammalian-type,oligosaccharideprobes.Amongthese,Dectin-1bindingisdetectedexclusivelyto1,3-linkedglucoseoligomers,theminimumlengthrequiredfordetectablebindingbeinga10-or11-mer.Thus,theligandsassignedsofarareexogenousratherthanendogenous.WefurthershowthatDectin-1ligands,11-13gluco-oligomers,inclusteredform(displayedonliposomes),mimicthemacromolecularβ-glucansandcompetewithzymosanbindingandtriggeringoftumornecrosisfactor-αsecretionbyaDectin-1-expressingmacrophagecellline.
CharacterizationofanEndo-Processive-TypeXyloglucanaseHavingaβ-1,4-Glucan-BindingModuleandanEndo-TypeXyloglucanasefromStreptomycesavermitilis.
Ichinose,H.,Araki,Y.,Michikawa,M.,Harazono,K.,Yaoi,K.,Karita,S.&Kaneko,S.(2012).AppliedandEnvironmentalMicrobiology,78(22),7939-7945.
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Weclonedtwoglycosidehydrolasefamily74genes,thesav_1856geneandthesav_2574gene,fromStreptomycesavermitilisNBRC14893andcharacterizedtheresultantrecombinantproteins.Thesav_1856geneproduct(SaGH74A)consistedofacatalyticdomainandafamily2carbohydrate-bindingmoduleattheCterminus,whilethesav_2574geneproduct(SaGH74B)consistedofonlyacatalyticdomain.SaGH74AandSaGH74Bwereexpressedsuccessfullyandhadmolecularmassesof92and78kDa,respectively.Bothrecombinantproteinswerexyloglucanases.SaGH74Ahadoptimalactivityat60°CandpH5.5,whileSaGH74Bhadoptimalactivityat55°CandpH6.0.SaGH74AwasstableoverabroadpHrange(pH4.5to9.0),whereasSaGH74BwasstableoverarelativelynarrowpHrange(pH6.0to6.5).Analysisofthehydrolysisproductsoftamarindxyloglucanandxyloglucan-derivedoligosaccharidesindicatedthatSaGH74Awasendo-processive,whileSaGH74Bwasatypicalendo-enzyme.TheCterminusofSaGH74A,whichwasannotatedasacarbohydrate-bindingmodule,boundtoβ-1,4-linkedglucan-containingsolublepolysaccharidessuchashydroxyethylcellulose,barleyglucan,andxyloglucan.
Comparisonofβ-1,3-glucanaseproductionbyBotryosphaeriarhodinaMAMB-05andTrichodermaharzianumRifaianditsoptimizationusingastatisticalmixture-design.
Giese,E.C.,Dekker,R.F.H.,Scarminio,I.S.,Barbosa,A.M.&daSilva,R.(2011).BiochemicalEngineeringJournal,53(2),239-243.
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BotryosphaeriarhodinaMAMB-05producedβ-1,3-glucanasesandbotryosphaeranwhengrownonglucose,whileTrichodermaharzianumRifaionlyproducedtheenzyme.Acomparisonoflong-termcultivation(300h)byB.rhodinademonstratedacorrelationbetweentheformationofbotryosphaeran(48h)anditsconsumption(after108h),andde-repressionofβ-1,3-glucanasesynthesiswhenglucosewasdepletedfromthenutrientmedium,whereasforT.harzianumenzymeproductioncommencedduringexponentialgrowth.Growthprofilesandlevelsofβ-1,3-glucanasesproducedbybothfungionbotryosphaeranalsodiffered,aswellastheproductionofβ-1,3-glucanasesandβ-1,6-glucanasesonglucose,lactose,laminarin,botryosphaeran,lasiodiplodan,curdlan,Brewer"syeastpowderandlyophilizedfungalmycelium,whichweredependentuponthecarbonsourceused.Astatisticalmixture-designusedtooptimizeβ-1,3-glucanaseproductionbybothfungievaluatedbotryosphaeran,glucoseandlactoseconcentrationsasvariables.ForB.rhodina,glucoseandlactosepromotedenzymeproductionatthesamelevels(2.30UmL-1),whereasbotryosphaeranaddedtothesesubstratesexertedasynergiceffectfavorableforβ-glucanaseproductionbyT.harzianum(4.25UmL-1).
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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