Megazyme/Azo-Casein (Sulphanilamide Dyed)/S-AZCAS/10 grams
商品编号:
S-AZCAS
品牌:
Megazyme INC
市场价:
¥3576.00
美元价:
2145.60
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,solubleAzo-Casein(SulphanilamideDyed)forthemeasurementofenzymeactivity,forresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Ahighlysensitive,solublesubstratefortheassayofendo-proteaseactivity.Thissubstratehasa5-foldgreatersensitivitythansimilarproductssuppliedbyothercompanies.
Harvestedbroccoli(Brassicaoleracea)respondstohighcarbondioxideandlowoxygenatmospherebyinducingstress-responsegenes.
Eason,J.R.,Ryan,D.,Page,B.,Watson,L.&Coupe,S.A.(2007).PostharvestBIOLOGyandTechnology,43(3),358-365.
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Broccoli(BrassicaoleraceaL.)tissueheldinacontrolledatmosphere(CA;10%carbondioxideand5%oxygen)senescesmoreslowlythantissueheldinair.CA-treatedbroccolitissuesloselesswaterandsolublesugars,havelowerproteaseactivity,andhavenosignificantlossofcolor(hueangle,chlorophyllcontent)for96hafterharvest(20°C,dark)comparedtotissueheldinairthatstartstosenesceandyellowafter48h.ThecurrentstudyexamineddifferentialgeneexpressioninbroccolitissuesinresponsetopostharvestCAtreatment.ThisgeneticanalysiswasundertakentoidentifyCA-responsivegenesthatmayactassignalingelementsandrepresspostharvestsenescenceprocesses.CA-responsivegeneswithup-anddown-regulatedexpression(comparedtoaircontrols)wereisolatedaftera6hCAtreatmentbydifferentialdisplay-polymerasechainreaction.ThecandidateCA-responsivegenesincludedanumberofnovelgeneswithoutpreviouslyassignedfunctions,andgenesofknownfunctionpreviouslyfoundtoberegulatedbystress(e.g.dehydration,saltstress,lowtemperature,andsugarstarvation).
Programmedcelldeathduringflowersenescence:isolationandcharacterizationofcysteineproteinasesfromSandersoniaaurantiaca.
Eason,J.R.,Ryan,D.J.,Pinkney,T.T.&O"Donoghue,E.M.(2002).FunctionalPlantBiology,29(9),1055-1064.
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CysteineproteaseinhibitorsdelayedthesenescenceofSandersoniaaurantiacaHook.flowers.TepalfADIngandwiltingoccurredlaterinthe2,2´-dipyridyl-treatedflowers,andtheseflowershadagreatersolubleproteincontentandlessactiveendoproteasescomparedwithcontrolflowersthatwereheldinwater.Biochemicalanalysisrevealedthepresenceofseveralprotease-activebandsinthesolubleproteinfractionSandersoniatepals.Activityofthepolypeptidesincreasedasflowersenescenceprogressed.WesternanalysiswithanantibodyraisedagainstthecastorbeancysteineproteinaseidentifiedhomologousproteinsinSandersoniaflowers(ca46,41and31kDa).ThreeCDNAsencodingcysteineproteinaseswereisolatedfromSandersoniatepals(PRT5,PRT15andPRT22).Expressionofallthreeincreasedintepalsassenescenceprogressed.mRNAsforPRT5weredetectedonlyinsenescingflowertissue,whereasPRT15andPRT22wereexpressedinleaf,stemandroottissue.PRT5hassignificanthomologytoC-terminusKDELproteins,whichhavearoleinthedegradationofplantcellcontentsduringprogrammedcelldeath.PRT15ismostsimilartocysteineproteinaseswithalongC-terminalextension,whereasPRT22ishomologoustostress-inducedcysteineproteinases.
EffectofpHonthesolubilizationofbrewers’spentgrainbymicrobialcarbohydrasesandproteases.
Faulds,C.B.,Robertson,J.A.&Waldron,K.W.(2008).JournalofAgriculturalandFoodChemistry,56(16),7038-7043.
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Thepotentialforenzymaticsolubilizationofbrewers’spentgrainbycarbohydrasesandproteaseswasexaminedoverabroadpHrange(pH3.2−11.2).EnzymesfromTrichoderma(Depol686)weremostefficientatalowerpH,whileenzymesfromtheHumicolapreparation(Depol740)werethebestperformeroverthewholerange.Profilingofkeyglycosidehydrolase,esteraseandproteaseactivitiesacrossthepHrangedemonstratedthatsolubilizationofspentgrainbytheTrichodermenzymescorrespondedtotherangeofmaximumactivities.ThiswasnotthecasewiththeHumicolaenzymes,wheremaximumsolubilizationofthesubstrateoccurredatpH9.1,atwhichpHthedeterminedactivitieswerelow.ProteaseactivityinDepol740wasassociatedwithahighsolubilization,butinhibitionofproteolyticactivityresultedinonlya5%decreaseinspentgrainsolubilization.Theseresultssuggestthatwhileenzymescanbeusedtoexploitagro-industrialsbyproduct,theuseofhighpHincreasestheextentofhydrolysisandanunidentifiedfactorproducedbyHumicolaimprovestheenzyme-catalyzedsolubilizationoflignocellulosicmaterial.
Protease-inducedsolubilisationofcarbohydratesfrombrewers"spentgrain.
Faulds,C.B.,Collins,S.,Robertson,J.A.,Treimo,J.,Eijsink,V.G.H.,Hinz,S.W.A.Schols,H.A.,Buchert,J.&Waldron,K.W.(2009).JournalofCerealScience,50(3),332-336.
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TheimpactofmicrobialproteasesonthereleaseofcarbohydratesfromBSGwasstudied.Theproteaseswereabletoreleasethenon-cellulosicglucose,aportionofferuloylatedarABInoxylanandover50%oftheproteinfrombrewers"spentgrain(BSG)after24hhydrolysis.Thenon-cellulosicglucosewasderivedfromresidualstarch-derivedproductspersistinginBSGaftermashing.Theproteasesdidnotcleavethehydroxycinnamateesterlinkagespresentonthearabinoxylanbackbone,andthusdonotbehaveasferuloylesterases.However,thematerialsolubilisedfromspentgrainbytheproteasescontainedupto198µgboundferulicacid/gextract,whichrepresented8.6%ofthetotalferulicacidpresentinBSG.Theseresultssuggestthataportionofwater-extractableferuloylatedarabinoxylanandstarchistrappedwithintheBSGmatrixbyaproteinaceousbarrier.
IsolationandcharacterizationofaBacilluslicheniformisstraincapableofdegradingzearalenone.
Yi,P.J.,Pai,C.K.&Liu,J.R.(2011).WorldJournalofMicrobiologyandBiotechnology,27(5),1035-1043.
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Theworldwidecontaminationofcereals,oilseeds,andothercropsbymycotoxin-producingmouldsisasignificantproblem.Mycotoxinshaveadverseeffectsonhumansandanimalsthatresultinillnessesandeconomiclosses.Reductionoreliminationofmycotoxincontaminationinfoodandfeedisanimportantissue.Thisstudyaimedtoscreensoilbacteriafordegradationofzearalenone(ZEN).ApurecultureofstrainCK1isolatedfromsoilsamplesshowedmostcapableofdegradationofZEN.Usingphysiological,biochemical,and16SrRNAgenesequenceanalysismethods,CK1wasidentifiedasBacilluslicheniformis.Additionof2ppmofZENinLuria–Bertani(LB)medium,B.licheniformisCK1decreased95.8%ofZENafter36hofincubation.InZEN-contaminatedcornmealmedium,B.licheniformisCK1decreasedmorethan98%ofZENafter36hofincubation.Inaddition,B.licheniformisCK1wasnon-hemolytic,non-enterotoxinproducing,anddisplayedhighlevelsofextracellularxylanase,cellulase,andproteaseactivities.ThesefindingssuggestthatB.licheniformisCK1couldbeusedtoreducetheconcentrationsofZENandimprovethedigestibilityofnutrientsinfeedstuffssimultaneously.
Suppressionofthecysteineprotease,aleurain,delaysfloretsenescenceinBrassicaoleracea.
Eason,J.R.,Ryan,D.J.,Watson,L.M.,Hedderley,D.,Christey,M.C.,Braun,R.H.&Coupe,S.A.(2005).PlantMolecularBiology,57(5),645-657.
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Analeurain-likeprotein,BoCP5,isup-regulatedduringharvest-inducedsenescenceinbroccolifloretandleaftissue.BoCP5ismostcloselyrelatedtoanArabidopsisprotein(91%,AAF43041)andhas71%identitytobarleyaleurain(P05167).ThemRNAforthisgeneaccumulateswithin6hafterharvestinbroccoliflorets,anditsexpressionisreducedintissuethathasbeenheldinsenescence-delayingtreatments(e.g.water,sucrosefeeding,controlledatmosphere).Thegeneisalsoexpressedinleavesduringaging-relatedandharvest-inducedsenescence.Analysisofproteinbandsthatcross-reactwithantibodiesraisedtothebacterialBoCP5fusionprotein,revealedprominentimmunoreactivebandsatca.26,28,31,and38kDinflorettissue.The31kDbandwasabsentinproteinextractsfromleaftissue.Agrobacterium-mediatedtransformationwasusedtoproducetransgenicbroccoliplantswithdown-regulatedBoCP5.AreductioninthepostharvestexpressionofBoCP5inflorettissuewasachievedforfourtransgeniclinesinthecurrentstudy.Inthreeoftheselinespostharvestfloretsenescence(yellowing)wasdelayed,andfloretscontainedsignificantlygreaterchlorophylllevelsduringpostharveststorageat20°Cthanwild-typeplants.Line4showedthegreatestdown-regulationofBoCP5,andinthislinepostharvestproteaseactivityremainedatpre-harvestlevels,andtheyieldofsolubleproteinsextractedfromfloretsafterharvestwassignificantlygreaterthanthatofwild-typetissue.
Hydrolysisofrawhideusingproteolyticenzymeextractedfrompapayalatex.
Pitpreecha,S.&Damrongsakkul,S.(2006).KoreanJournalofChemicalEngineering,23(6),972-976.
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Crudeproteolyticenzymewasextractedfrompapayalatexusingtwosolvents,waterandphosphatebufferpH6.Theyieldofextractedenzymeusingwaterasasolventwassimilartothatusingphosphatebuffer.Followingthesolventextraction,theextractedenzymewasprecipitatedin45wt%saturatedammoniumsulfatesolution.Theyieldandactivityofprecipitatedenzymeconsiderablydecreased.Crudeproteolyticenzymeextractedusingwaterasanextractingliquidwas,therefore,selectedtouseingelatinproductionfromrawhidehydrolysis,comparingtotheuseofcommercialpapain.Theeffectsofhydrolysisconditionsongelatinrecoveryandpropertiesofobtainedgelatinwereinvestigated.Theoptimumconditionsfortheactivitiesofbothcrudeextractedenzymeandcommercialpapainwereat75°CandpH7.Atthiscondition,thehighestpercentagesofgelatinrecoverywereobtainedfromrawhidehydrolysisreactions.Thegelatinrecoveryandgelstrengthofgelatinobtainedfromcrudeextractedenzymeandcommercialpapainhydrolysisweresimilar.Thisprovedthatcrudeextractedenzymefrompapayalatexcouldbeeffectivelyusedingelatinproduction,insteadoftheuseofcommercialpapain,withacomparativelylowcost.
Identificationofdehydration‐responsivecysteineproteasesduringpost‐harvestsenescenceofbroccoliflorets.
Coupe,S.A.,Sinclair,B.K.,Watson,L.M.,Heyes,J.A.&Eason,J.R.(2003).JournalofExperimentalBotany,54(384),1045-1056.
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Harvest‐inducedsenescenceofbroccoliresultsintissuewiltingandsepalchlorosis.Assenescenceprogresses,chlorophyllandproteinlevelsinflorettissuesdeclineandendo‐proteaseactivity(measuredwithazo‐casein)increases.Proteaseactivityincreasedfrom24hafterharvestfortissuesheldinairat20°C.Activitywaslowerinflorettissuesfrombranchletsthathadbeenheldinsolutionsofsucrose(2%w/v)orunderhighcarbondioxide,lowoxygen(10%CO2,5%O2)conditions.Fourprotease‐activeproteinbandswereidentifiedinsenescingflorettissuebyzymography,andtheuseofchemicalinhibitorsofproteaseactionsuggeststhatsome44%ofproteaseactivityinsenescingflorettissue72hafterharvestisduetotheactionofcysteineandserineproteases.FourputativecysteineproteasecDNAshavebeenisolatedfrombroccoliflorettissue(BoCP1,BoCP2,BoCP3,BoCP4).ThecDNAsaremostsimilar(73–89%attheaminoacidlevel)todehydration‐responsivecysteineproteasespreviouslyisolatedfromArabidopsisthaliana(RD19,RD21).ThemRNAsencodedbythebroccolicDNAsareexpressedinflorettissueduringharvest‐inducedsenescencewithmRNAaccumulatingwithin6hofharvestforBoCP1,12hofharvestforBoCP4andwithin24hofharvestforBoCP2andBoCP3.InductionofthecDNAsisdifferentiallydelayedwhenbroccolibranchletsareheldinsolutionsofwaterorsucrose.Inaddition,theexpressionofBoCP1andBoCP3isinhibitedintissueheldinatmospheresofhighcarbondioxide/lowoxygen(10%CO2,5%O2).TheputativecysteineproteasemRNAsareexpressedbeforemeasurableincreasesinendo‐proteaseactivity,lossofprotein,chlorophyllortissuechlorosis.
Suppressingexpressionofasolubleacidinvertase(BoINV2)inbroccoli(Brassicaoleracea)delayspostharvestfloretsenescenceanddownregulatescysteineprotease(BoCP5)transcription.
Eason,J.R.,Ryan,D.J.,Watson,L.M.,Pinkney,T.,Hedderley,D.,Christey,M.C.,Braun,R.H.&Coupe,S.A.(2007).PhysiologiaPlantarum,130(1),46-57.
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WereportontheproductionandselectionoftransgenicBrassicaoleraceavar.Italicalineswithadownregulatedsolubleacidinvertase(BoINV2).Explantsofbroccoli(cv.Triathlon)weretransformedwithanantisenseconstructofBoINV2underthecontrolofanAsparagusofficinalis-derivedharvest-inducedpromoterusingAgrobacteriumtumefaciens-mediatedtransformation.BoINV2isupregulatedinwild-typebroccoliflorettissueafterharvest.TransgenicbroccolilinesshowedreducedBoINV2mRNAaccumulationimmediatelyafterharvestcomparedwithwild-type.DownregulationofBoINV2hadnosignificantimpactontheexpressionofasecondbroccoliacidinvertasegene(BoINV1),butplantswithdownregulatedBoINV2alsohadlowerexpressionofasenescence-associatedcysteineprotease(BoCP5)comparedwithwild-type.ThetotalsolublesugarlevelsinflorettissueofantisenseBoINV2linesweregreaterthanwild-typetissueafterharvest(upto1.5timeshigher).Solubleproteincontentofwild-typetissuedecreasedfrom48hafterharvestwithanincreaseinproteaseactivity.Incomparison,twoantisenseBoINV2linesretainedat-harvestlevelsofsolubleproteinuntil72and96hafterharvestandhadlowerpostharvestendoproteaseactivitycomparedwithwild-type.AntisenseBoINV2linesalsohadaslowerrateoffloretsepalchlorosisafterharvestcomparedwithwild-type.
Effectsofsolubledietarycelluloseonspecificgrowthrate,survivalanddigestiveenzymeactivitiesinthreefreshwatercrayfish(Cherax)species.
Dammannagoda,L.K.,Pavasovic,A.,Hurwood,D.A.&Mather,P.B.(2015).AquacultureResearch,46(3),626-636.
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Thecurrentstudyevaluatedtheeffectofsolubledietarycelluloseongrowth,survivalanddigestiveenzymeactivityinthreeendemic,Australianfreshwatercrayfishspecies(redclaw:Cheraxquadricarinatus,marron:C.tenuimanus,yabby:C.destructor).Separateindividualfeedingtrialswereconductedforlate-stagejuvenilesfromeachspeciesinanautomatedrecirculatingfreshwater,culturesystem.Animalswerefedeitheratestdiet(TD)thatcontained20%solublecelluloseorareferencediet(RD)substitutedwiththesameamountofcornstarch,overa12-weekperiod.RedclawfedwithRDshowedsignificantlyhigher(P<0.05)=""specific=""growth=""rates=""(sgr)=""compared=""with=""animals=""fed=""the=""td,=""while=""sgr=""of=""marron=""and=""yabby=""fed=""the=""two=""diets=""were=""not=""significantly=""different.=""expressed=""cellulase=""activity=""levels=""in=""redclaw=""were=""not=""significantly=""different=""between=""diets.=""marron=""and=""yabby=""showed=""significantly=""higher=""cellulase=""activity=""when=""fed=""the=""rd="">P<0.05).=""amylase=""and=""protease=""activity=""in=""all=""three=""species=""were=""significantly=""higher=""in=""the=""animals=""fed=""with=""rd="">P<0.05).=""these=""results=""indicate=""that=""test=""animals=""of=""all=""three=""species=""appear=""to=""utilize=""starch=""more=""efficiently=""than=""soluble=""dietary=""cellulose=""in=""their=""diet.=""the=""inclusion=""of=""20%=""soluble=""cellulose=""in=""diets=""did=""not=""appear,=""however,=""to=""have=""a=""significant=""negative=""effect=""on=""growth=""rates.="">
CharacterisationoftheenzymaticpropertiesofMpAPr1,anasparticproteasesecretedbythewineyeastMetschnikowiapulcherrima.
Theron,L.W.,Bely,M.&Divol,B.(2017).JournaloftheScienceofFoodandAgriculture.
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BACKGROUND:MpAPr1,encodinganacidproteasefromthewineyeastMetschnikowiapulcherrimaIWBTY1123,waspreviouslyisolatedandshowntodisplaypotentialactivityagainstcaseinandgrapeproteins.However,itscharacterisationremainedpartial.RESULTS:MpAPr1wasclonedintothepGAPZαAvectorandtransformedintoKomagataellapastorisX33forheterologousexpression.Afterverificationofactivity,theenzymepropertieswerecharacterised.ProteaseactivitywithintheconcentratedsupernatantwasretainedoverapHrangeof3.0to5.0andbetween10°Cto50°C.Optimalconditionsforproteaseactivitywerefoundat40°CandpH4.5.ActivitywasmostlyunaffectedbythepresenceofmetalionswiththeexceptionofCu2+andNi2+.FurThermore,proteolyticactivitywasretainedinthepresenceofsugarandethanol.pHandtemperatureconditionsforMpAPr1expressioninK.pastoriswereoptimised.Purificationwasachievedbymeansofcationexchangechromatographyandkineticparameters(KmandVmaxweredetermined.MpAPr1activityagainstgrapeproteinswasconfirmed,buttheextentofthedegradationwasdependentonthenatureoftheseproteinsandtheenvironmentalconditions.CONCLUSION::Overall,theresultssuggestthatMpAPr1couldbeappliedinfoodbiotechnologyprocessessuchaswinemaking.
Batch-to-batchvariationandstoragestabilityofthecommercialpeptidasepreparationFlavourzymeinrespectofkeyenzymeactivitiesanditsinfluenceonprocessreproducibility.
Merz,M.,Appel,D.,Berends,P.,Rabe,S.,Blank,I.,Stressler,T.&Fischer,L.(2016).EuropeanFoodResearchandTechnology,242(7),1005-1012.
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Thesynergyofendopeptidasesandexopeptidasesisthekeyforanefficienthydrolysisofproteins.FlavourzymeissoldasacommercialpeptidasepreparationfromAspergillusoryzaethatexhibitsvariousendo-andexopeptidaseactivitiesand,therefore,generatesproteinhydrolysateswithhighdegreesofhydrolysis.Themanufacturer(Novozymes)standardizestheenzymepreparationforonepeptidaseactivity,determinedwiththeMarkersubstrateH-Leu-pNA.However,sevenpeptidasesofFlavourzymewererecentlyidentifiedandpurified,andthesignificantcontributionofsixofthemtowheatglutenhydrolysiswasdemonstrated.Theknowledgeaboutthebatch-to-batchvariationandstoragestabilityoftheFlavourzymepreparationregardingtheotherpeptidaseactivitiesarestillunclear,andthisisimportantinformationfortheusageoftheenzymepreparationtogainreproducIBLeproteinhydrolysisprocesses.Inthepresentstudy,wetested12Flavourzymebatchesfortheactivityofthesevenpeptidases.Theimpactofthestoragetimeonthepeptidaseactivitiesandthemagnitudeofthebatch-to-batchvariationwereinvestigated.IncontrasttotheactivitydeterminedwithH-Leu-pNAasasubstrate,thevariationsoftheotherpeptidaseactivitieswerenoticeable.Thevariationoftheendopeptidaseactivitywasmostdistinctandtheactivitydecreasedduringthestoragetimeofthepreparation.ThevariationoftheFlavourzymecompositionalsoaffectedthereproducibilityofacaseinbatchhydrolysisprocess,whichshouldbetakenintoaccountforanyfutureresearchandindustrialapplication.
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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