Megazyme/红色普鲁兰多糖/S-RPUL/3克
商品编号：
S-RPUL
品牌：
Megazyme INC
市场价：
¥4296.00
美元价：
2577.60
产品分类：
反应底物
公司分类：
Reaction_substrate
联系Q Q：
3392242852
电话号码：
4000-520-616
电子邮箱：
info@ebiomall.com
商品介绍
Highpuritydyed,solubleRedPullulanforthemeasurementofenzymeactivity,forresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Substrateformeasurementofpullulanaseincommercialenzymepreparationsandforthemeasurementoflimit-dextrinaseinmaltflours.
Measurementofthecontentoflimit-dextrinaseincerealflours.
McCleary,B.V.(1992).CarbohydrateResearch,227,257-268.
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Proceduresforthequantitativeextraction,activation,andassayoflimit-dextrinaseincerealflourshavebeendeveloped.Extractionandactivationrequireincubationinbuffercontaining20mmcysteineforatleast16horwith25mMdithiothreitolfor5h.Activityisassayedwithasoluble,dyedsubstrate(Red-Pullulan)oraninsoluble,dyed,andcross-linkedsubstrate(Azurine-CL-Pullulan)whichisdispensedintabletform(Limit-DextriZymetablets).
Overexpressionofthioredoxinhleadstoenhancedactivityofstarchdebranchingenzyme(pullulanase)inbarleygrain.
Cho,M.J.,Wong,J.H.,Marx,C.,Jiang,W.,Lemaux,P.G.&Buchanan,B.B.(1999).ProceedingsoftheNationalAcademyofSciences,96(25),14641-14646.
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Biochemicallyactivewheatthioredoxinhhasbeenoverexpressedintheendospermoftransgenicbarleygrain.TwoDNAconstructscontainingthewheatthioredoxinhgene(wtrxh)wereusedfortransformation;eachcontainedwtrxhfusedtoanendosperm-specificB1-hordeinpromotereitherwithorwithoutasignalpeptidesequencefortargetingtotheproteinbody.Twenty-twostable,independentlytransformedregenerablelineswereobtainedbyselectingwiththeherbicidebialaphostotestforthepresenceofthebarherbicideresistancegeneonacotransformedplasmid;allwerepositiveforthisgene.Thepresenceofwtrxhwasconfirmedin20linesbyPCRanalysis,andtheidentityandlevelofexpressionofwheatthioredoxinhwasassessedbyimmunoblots.Althoughlevelsvariedamongthedifferenttransgenicevents,wheatthioredoxinhwasconsistentlyhighlyexpressed(upto30-fold)inthetransgenicgrain.TransgeniclinestransformedwiththeB1-hordeinpromoterwithasignalpeptidesequenceproducedahigherlevelofwheatthioredoxinhonaveragethanthosewithoutasignalsequence.Theoverexpressionofthioredoxinhintheendospermofgerminatedgraineffecteduptoa4-foldincreaseintheactivityofthestarchdebranchingenzyme,pullulanase(limitdextrinase),theenzymethatspecificallycleavesα-1,6linkagesinstarch.Theseresultsraisethequestionofhowthioredoxinhenhancestheactivityofpullulanasebecauseitwasfoundthattheinhibitorhadbecomeinactivebeforetheenzymeshowedappreciableactivity.
Astarch‐accumulatingmutantofArABIdopsisthalianadeficientinachloroplasticstarch‐hydrolysingenzyme.
Zeeman,S.C.,Northrop,F.,Smith,A.M.&Rees,T.A.(1998).ThePlantJournal,15(3),357-365.
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TheaimofthisworkwastoidentifyenzymesthatparticipateinthedegradationoftransitorystarchinArabidopsis.Amutantlinewasisolatedbyscreeningleavesattheendofthenightforthepresenceofstarch.Themutanthadahigherstarchcontentthanthewild-typethroughoutthediurnalcycle.Thisaccumulationwasduetoareductioninstarchbreakdown,leADIngtoanimbalancebetweentheratesofsynthesisanddegradation.Noreductionintheactivityofendo-amylase(α-amylase),β-amylase,starchphosphorylase,maltase,pullulanaseorD-enzymecouldbedetectedincrudeextractsofleavesofthemutant.However,nativePAGEingelscontainingamylopectinrevealedthatastarch-hydrolysingactivity,putativelyidentifiedasanendo-amylaseandpresentinwild-typechloroplasts,wasabsentorappreciablyreducedinthemutant.Thisisthefirsttimethataspecificenzymerequiredforstarchdegradationhasbeenidentifiedinleaves.
Thestarch-debranchingenzymesisoamylaseandpullulanasearebothinvolvedinamylopectinbiosynthesisinriceendosperm.
Kubo,A.,Fujita,N.,Harada,K.,Matsuda,T.,Satoh,H.&Nakamura,Y.(1999).PlantPhysiology,121(2),399-410.
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Theactivitiesofthetwotypesofstarchdebranchingenzymes,isoamylaseandpullulanase,weregreatlyreducedinendospermsofallelicsugary-1mutantsofrice(Oryzasativa),withthedecreasemorepronouncedforisoamylasethanforpullulanase.However,thedecreaseinisoamylaseactivitywasnotrelatedtothemagnitudeofthesugaryphenotype(theproportionofthephytoglycogenregionoftheendosperm),asobservedwithpullulanase.InthemoderatelymutatedlineEM-5,thepullulanaseactivitywasmarkedlylowerinthephytoglycogenregionthaninthestarchregion,andisoamylaseactivitywasextremelyloworcompletelylostinthewholeendospermtissue.Theseresultssuggestthatbothdebranchingenzymesareinvolvedinamylopectinbiosynthesisinriceendosperm.Wepresumethatisoamylaseplaysapredominantroleinamylopectinsynthesis,butpullulanaseisalsoessentialorcancompensatefortheroleofisoamylaseintheconstructionoftheamylopectinmultiple-clusterstructure.ItishighlypossIBLethatisoamylasewasmodifiedinsomesugary-1mutantssuchasEM-273andEM-5,sinceitwaspresentinsignificantandtraceamounts,respectively,inthesemutantsbutwasapparentlyinactive.TheresultsshowthattheSugary-1geneencodestheisoamylasegeneofthericegenome.
EnzymaticpropertiesandregulationofZPU1,themaizepullulanase-typestarchdebranchingenzyme.
Wu,C.,Colleoni,C.,Myers,A.M.&James,M.G.(2002).ArchivesofBiochemistryandBiophysics,406(1),21-32.
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Starchdebranchingenzymes(DBE)arerequiredformobilizationofcarbohydratereservesandforthenormalstructuralorganizationofstorageglucanpolymers.Twoisoforms,thepullulanase-typeDBEsandtheisoamylase-typeDBEs,arebothhighlyconservedinplants.ToaddressDBEfunctionsinstarchassemblyandbreakdown,thisstudycharacterizedthebiochemicalactivityofZPU1,apullulanase-typeDBEthatistheproductofthemaizeZpu1gene.AssaysshoweddirectlythatrecombinantZPU1(ZPU1r)expressedinEscherichiacolifunctionsasapullulanase-typeenzyme,and1H-NMRspectroscopydemonstratedthatZPU1rspecificallyhydrolyzesα-(1→6)branchlinkages.PreferredsubstratesforZPU1rhydrolyticactivityweredetermined,aswerepH,temperature,andthermalstabilityoptima.KineticpropertiesofZPU1rwithrespecttotwosubstrates,β-limitdextrinandpullulan,weredetermined.ZPU1activitywasincreasedbyincubationwiththioredoxinh,andnativeactivitywasdecreasedinmutantsthataccumulatesolublesugars,suggestingpotentialregulatorymechanisms.
Theeffectofstoragetemperatureonreducingsugarconcentrationandtheactivitiesofthreeamylolyticenzymesintubersofthecultivatedpotato,SolanumtuberosumL.
Cottrell,J.E.,Duffus,C.M.,Paterson,L.,Mackay,G.R.,Allison,M.J.&Bain,H.(1993).PotatoResearch,36(2),107-117.
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Reducingsugarcontent,andactivitiesofthreestarchhydrolysingenzymes,alpha-amylase,beta-amylaseanddebranchingenzymeweremeasuredoverseveralmonthsintubersoffivecultivarsstoredat4°Cor10°C.Cultivarsdifferedintheirsensitivitytostoragetemperature.Reducingsugarcontentoftubersandtheactivitiesofthreestarchhydrolysingenzymesincreasedsharplyduringthefirstweeksofstorageat4°C.At10°C,reducingsugarcontent,andtheactivityofthethreeenzymesremainedconstantorincreasedonlyslightly.
Invitropullulanaseactivityofwheat(TriticumaestivumL.)limit-dextrinasetypestarchdebranchingenzymeismodulatedbyredoxconditions.
Repellin,A.,Båga,M.&Chibbar,R.N.(2008).JournalofCerealScience,47(2),302-309.
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Expressionofalimit-dextrinase(LD)typestarchdebranchingenzyme(EC3.2.1.41)wasobservedindevelopingwheat(TriticumaestivumL.)endospermandgerminatinggrains,indicatingarolefortheenzymeinbothbiosynthesisanddegradationofstarch.Afull-lengthCDNA,TaLD1,encodingLDinwheatdevelopingkernelswasisolatedandpredictedtoencodea98.6kDamatureproteinactiveinamyloplasts.IsolatedcDNAwasexpressedinEscherichiacolitoproducearecombinantHis-taggedLD,whichmainlyaccumulatedininclusionbodiesasaninactiveenzyme.ExtractionofHis-taggedLDfromtheinclusionbodiesfollowedbydialysisunderthiol/disulphideredoxconditionsallowedpartialrefoldingoftheproteinanddetectionofpullulanasespecificactivitiesbyzymogramanalysisandenzymeassays.SeveralactiveconformationsweredemonstratedbytherecombinantTaLD1andpullulanaseactivitycouldbemodulatedbyredoxconditionsinvitro.TheresultssuggestthatcellularredoxconditionsmayregulatethelevelofLDactivityinwheattissues.
Flavobacteriumfrigidariumsp.nov.,anaerobic,psychrophilic,xylanolyticandlaminarinolyticbacteriumfromAntarctica.
Humphry,D.R.,George,A.,Black,G.W.&Cummings,S.P.(2001).InternationalJournalofSystematicandEvolutionaryMicroBIOLOGy,51(4),1235-1243.
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Apsychrophilic,aerobicbacteriumdesignatedA2iTwasisolatedfrommarinesedimentrecoveredfromshallowwaterssurroundingAdelaideIsland,Antarctica(67°34"S,68°07"W).Theorganismexhibitedxylanolyticandlaminarinolyticactivityandwashalotolerant.Basiccharacterizationshowedthatitwasgram-negative,non-motile,yellow-pigmented(β,β-carotene-3,3"-diol)andpositiveforoxidaseandcatalasesynthesis.Analysisofthe16SrDNAsequencesuggeststhattheorganismbelongstotheFlexibacter-Cytophaga-Bacteroidesphylum.Onthebasisofits16SrDNAsequence,thebacteriumis96.8%similartoFlavobacteriumcolumnareATCC43622-itsclosestrelation.ThegenomicDNAG+Ccontentwas35mol%.Growthonxylanoccursoptimallyat15°C,thoughgrowthalsooccursat0°C,andthedoublingtimesare9.6and34.8h,respectively.Themaximumgrowthtemperatureonxylanisat24°C.Thebacteriumisaneutrophile,growingacrossthepHrange5.6-8.4andhavinganoptimumatpH7.5.Analysisofthe16SrDNAsequence,togetherwithphenotypiccharacterization,suggeststhattheorganismisamemberofthegenusFlavobacterium.DNA-DNAhybridizationexperimentshaveshownthatitisanovelspecies;itisproposed,therefore,thattheorganismbedesignatedasthetypestrainofFlavobacteriumfrigidariumsp.nov.(=ATCC700810T=NCIMB13737T).
ExpressionandsecretionofBacilluspolymyxaneopullulanaseinSaccharomycescerevisiae.
Yebra,M.J.,Blasco,A.&Sanz,P.(1999).FEMSMicrobiologyLetters,170(1),41-49.
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WehaveisolatedthegeneencodingtheneopullulanaseenzymefromBacilluspolymyxaCECT155.Itconsistsofanopenreadingframeof1545bpthatcouldcodeforaproteinof515aminoacids.ThisopenreadingframewasexpressedinBacillussubtilisandthecorrespondingtransformantsproducedextracellularneopullulanase.TheneopullulanasegenewasalsoexpressedinSaccharomycescerevisiaeplacingitunderthecontroloftheyeastactingene(ACT1)promoter.Clonescontainingtheintactneopullulanasegene,includingitsownbacterialsignalsequence,gaverisetothesynthesisofactive,butintracellular,enzymebyS.cerevisiaetransformants.Whensequencesspecifyingthesignalsequenceandleaderregionoftheyeastmatingpheromoneα-factor(MFα1)werefusedupstreamofthegeneencodingtheneopullulanaseenzyme,theenzymewassecretedbyS.cerevisiae.ThesecretedproteinpresentedthesamebiochemicalpropertiesandthesameapparentmolecularmassastheBacilluspolymyxaoriginalenzyme.Thepredictedaminoacidsequenceoftheneopullulanaseproteincontainedsequencemotifsconservedamongamylolyticenzymes.NorthernblotanalysisindicatedthatthetranscriptionoftheneopullulanasegeneinB.polymyxawasinducedbythepresenceofthesubstrate,pullulan,intheculture,andwasrepressedbyglucose.
Proteinheterogeneityofspinachpullulanaseresultsfromthecoexistenceofinterconvertibleisomericformsofthemonomericenzyme.
Henker,A.,Schindler,I.,Renz,A.&Beck,E.(1998).Biochem.J,331,929-935.
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Purifiedpullulanase(starch-debranchingenzyme,R-enzyme,EC3.2.1.41)fromspinach(SpinaciaoleraceaL.)chloroplastsseparatedintoatleastsevenindividualenzymicallyactiveproteins(isomers,numbered1–7)onisoelectricfocusingorcolumnchromatofocusing.Attheirisoelectricpoints(betweenpH4.7and5.2)theseformswereratherstable.AtslightlyalkalinepH,eachconvertedintothewholesetofisomers.PAGEofthepurifiedenzymeunderdenaturingornon-denaturingconditionsresultedinoneproteinband.Whensubstrate(amylopectinorpullulan)wasincludedinthegel,thenativeenzymeaswellasanyoftheindividualisomersseparatedintotwo(sometimesthree)bands("substrate-inducedforms",numberedI–III)withdifferentspecificactivities,dissociationconstantsoftheenzyme–substratecomplexesandactivationenergies.Eachsubstrate-inducedformproducedthewholesetofsevenisomersonisoelectricfocusing.Thespecificactivityofthetotalenzymereflectedtherelativeproportionsofthesubstrate-inducedforms.Tosomeextenttherelativeproportions,asdeterminedbycrossedimmunoelectrophoresis,couldbeshiftedinfavourofthemoreorthelessactiveformsbyreductionwithdithiothreitol,andgentleoxidationrespectively.ActivationbydithiothreitoldidnotalterthemodeofactionoftheenzymebutonlyincreasedthevelocityofsubstratedegradationandextendeditsactivityintothepHrangeofthechloroplast.Asaconsequenceofisomerinterconversion,microheterogeneitycouldservetoregulatepullulanaseactivityinabiochemicalmannerthatsharessomefeatureswithallostericregulation.
CharacterizationofnovelneopullulanasefromBacilluspolymyxa.
Yebra,M.J.,Arroyo,J.,Sanz,P.&Prieto,J.A.(1997).AppliedBiochemistryandBiotechnology,68(1),113-120.
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BacilluspolymyxaCECT155producesanextracellularneopullulanaseactivitythatdegradespullulantopanose.Thisactivitywasstimulatedbythepresenceofpullulanintheculture,andrepressedbyglucose.Theapparentmolwtdeterminedfortheenzymewas58kDa.TheoptimumpHandtemperatureforneopullulanaseactivitywerepH6.0and50°C,respectively.TheenzymewasstableinapHrangeof4.0–8.0,andtemperaturesupto60°C.Thesepropertiesmakeitsuitableforthesaccharificationprocessesinthestarchindustries.
Cloning,expressionandcharacterizationoftherecombinantcold-activetype-IpullulanasefromShewanellaarctica.
Elleuche,S.,Qoura,F.M.,Lorenz,U.,Rehn,T.,Brueck,T.&Antranikian,G.(2015).JournalofMolecularCatalysisB:Enzymatic,116,70-77.
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Anactivity-basedscreeningapproachledtotheidentificationofanovelglycosidehydrolasefamily-13pullulanasegene(pul13A)fromapsychrophilicbacterium.Therecombinantenzymeexhibitedadeducedpeptidesequenceof1440aminoacidresiduesandwasproducedinaheterologoushostinEscherichiacoli.Purificationfrominclusionbodieswasachievedbyasix-stepdialysisprotocolenablingmildrefoldingoftheurea-denaturatedproteinfollowedbyaffinity-andsize-exclusionchromatographyundernativeconditions.Pul13Aisatype-Ipullulanase,whichiscapableofhydrolysingα-1,6-glycosidicbondsinpullulantoproducemaltotriose,whilemaltoseandintermediateoligosaccharidesareproducedfromsolublestarchandamylopectin.Therecombinantenzymeexhibitedtypicalpropertiesofcold-adaptedproteinsincludinglowThermostabilityatelevatedtemperatures.Itshowedatemperatureoptimumat35°C,whileat10°Cresidualactivity(25%)remained.TheoptimalpHwasintherangeof6.0-7.0,withPul13AbeingstableatneutralandbasicpH,butnotintheacidicrange.CatalyticactivitywasincreasedinthepresenceofdivalentcationscalciumandcobaltandbothmetalionswerealsoabletorestorecatalyticactivityofEDTA-chelatedenzymesamples.Pul13Arepresentsthefirsttype-Ipullulanasefromapsychrophilethathasbeenproducedinrecombinantform.Moreover,itsfavourableenzymaticpropertiesmakethisenzymeapotentialcandidateforindustrialapplicationssuchasstarchdegradationforethanolbasedbiofuelproduction.
CharacterizationofatypeIpullulanasefromAnoxybacillussp.SK3-4revealsanunusualsubstratehydrolysis.
Kahar,U.M.,Ng,C.L.,Chan,K.G.&Goh,K.M.(2016).AppliedMicrobiologyandBiotechnology,100(14),6291–6307.
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TypeIpullulanasesareenzymesthatspecificallyhydrolyseα-1,6linkagesinpolysaccharides.ThisstudyreportstheanalysesofanoveltypeIpullulanase(PulASK)fromAnoxybacillussp.SK3-4.PurifiedPulASK(molecularmassof80 kDa)wasstableatpH 5.0-6.0andwasmostactiveatpH 6.0.TheoptimumtemperatureforPulASKwas60°C,andtheenzymewasreasonablystableatthistemperature.PullulanwasthepreferredsubstrateforPulASK,with89.90 %adsorbanceefficiency(variousotherstarches,56.26–72.93 %efficiency).SimilartoothertypeIpullulanases,maltotriosewasformedondigestionofpullulanbyPulASK.PulASKalsoreactedwithβ-limitdextrin,asugarrichinshortbranches,andformedmaltotriose,maltotetraoseandmaltopentaose.Nevertheless,PulASKwasfoundtopreferablydebranchlongbranchesatα-1,6glycosidicbondsofstarch,producingamylose,linearorbranchedoligosaccharides,butwasnonreactiveagainstshortbranches;thus,noreducingsugarsweredetected.ThisissurprisingasallcurrentlyknowntypeIpullulanasesproducereducingsugars(predominantlymaltotriose)ondigestingstarch.TheclosesthomologueofPulASK(95 %identity)isatypeIpullulanasefromAnoxybacillussp.LM14-2(Pul-LM14-2),whichiscapableofformingreducingsugarsfromstarch.Withrationaldesign,aminoacids362-370ofPulASKwerereplacedwiththecorrespondingsequenceofPul-LM14-2.Themutantenzymeformedreducingsugarsondigestingstarch.Thus,weidentifiedanovelmotifinvolvedinsubstratespecificityintypeIpullulanases.Ourcharacterizationmaypavethewayfortheindustrialapplicationofthisuniqueenzyme.
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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