Megazyme/极限右旋糖酶片/T-LDZ-1000T/1000片
商品编号：
T-LDZ-1000T
品牌：
Megazyme INC
市场价：
¥22056.00
美元价：
13233.60
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
HighpuritydyedandcrosslinkedLimit-Dextrizymetabletsforthemeasurementofenzymeactivity,forresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Fortheassayoflimit-dextrinaseandpullulanase.ContainingAZCL-Pullulan.
Newupdatedassayprotocolemployingamyloglucosidaseintosamplepreparation.
Colourimetricandfluorimetricsubstratesfortheassayoflimitdextrinase.
Mangan,D.,McCleary,B.V.,Cornaggia,C.,Ivory,R.,Rooney,E.&McKie,V.(2015).JournalofCerealScience,62,50-57.
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Themeasurementoflimit-dextrinase(LD)(EC3.2.1.142)ingrainsamplessuchasbarley,wheatorricecanbeproblematicforanumberofreasons.TheintrinsicLDactivityinthesesamplesisextremelylowandtheyoftencontainalimit-dextrinaseinhibitorand/orhighlevelsofreducingsugars.LDalsoexhibitstransglycosylationactivitythatcancomplicatethemeasurementofitshydrolyticactivity.AminormodificationtotheindustrialstandardLimit-Dextrizymetablettestissuggestedheretoovercomethistransglycosylationissue.Inaddition,twonewsubstratesaredescribedthatcanbeadoptedforuseinanauto-analyserformat.4,6-O-benzylidene-2-chloro-4-nitrophenyl-β-63-α-D-maltotriosyl-maltotrioside(BzCNPG3G3,Hexachrom)isnotsusceptIBLetotransglycosylationandservesamiablyasaroutinequantitativeassaytoolwiththepotentialtorunkineticassaysduetothelowpKa(∼5.5)ofthechromogenicmoietywhile4,6-O-benzylidene-4-methylumbelliferyl-β-63-α-D-maltotriosyl-maltotrioside(BzMUG3G3,Hexafluor)wasfoundtobesusceptibletotransglycosylationwithLD.ItisanticipatedthatHexafluormayfindextensiveuseinapplicationswherehighsensitivityisrequiredsuchashighthroughputscreeningstudies.
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).
Detectionofalimitdextrinaseinhibitorinbarley.
Macri,L.J.,MacGregor,A.W.,Schroeder,S.W.&Bazin,S.L.(1993).JournalofCerealScience,18(2),103-106.
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Twoproteinshavebeenisolatedfrombarley(Hordeumvulgarecv.Harrington)thatinhibitedlimitdextrinasefromgerminatedbarley.Theseinhibitorswerepurifiedbycarboxymethylcelluloseionexchangechromatographyandchromatofocusing.TheywereshowntohaveapproximateMrsof15kandisoelectricpointsofapproximately6•7and7•2(measuredbyisoelectricfocusing).
Purificationandcharacterisationoflimitdextrinaseinhibitorsfrombarley.
MacGregor,A.W.,Macri,L.J.,Schroeder,S.W.&Bazin,S.L.(1994).JournalofCerealScience,20(1),33-41.
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Twoinhibitorsofmaltlimitdextrinasewerepurifiedfromacrudebarleyextract(cv.Harrington)byCMcelluloseionexchangechromatographyandchromatofocusing.Theinhibitorswereheat-stableproteinsofMrapproximately15kandisoelectricpointsof6•7(lowpIinhibitor)and7•2(highpIinhibitor).BothinhibitorswereactiveoverawidepHrange,andweremosteffectiveatpH5•5to6•5,thepHoptimumofthelimitdextrinaseenzyme.Inactivationofthelimitdextrinaseenzymebyeitherinhibitorcouldbereversedbywarningthecomplexat40°Cinthepresenceofreducingagents.
Limitdextrinasefromgerminatingbarleyhasendotransglycosylaseactivity,whichexplainsitsactivationbymaltodextrins.
McDougall,G.J.,Ross,H.A.,Swanston,J.S.&Davies,H.V.(2004).Planta,218(4),542-551.
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Limitdextrinase(EC3.2.1.41)fromgerminatingbarley(HordeumvulgareL)canbeactivatedbymillimolarconcentrationsoflinearmaltodextrinswithadegreeofpolymerisation≥2.Theactivationwasassay-dependent;itwasdetectedusingassaysbasedonthesolubilisationofcross-linkeddyedpullulanbutnotinassaysthatdirectlymeasuredcleavageeventssuchastheformationofnewreducingtermini.Thisstronglysuggestedthatmaltodextrinsdidnotincreasethecatalyticrateoflimitdextrinasei.e.thisisnotatrueactivation.Ontheotherhand,considerableactivationwasnotedinassaysthatmeasuredpullulandegradationbyreductioninviscosity.Takentogether,thissuggestedthatmaltodextrinsalteredthemodeofactionoflimitdextrinase,causingmorerapiddecreasesinviscosityorgreatersolubilisationofdye-linkedpullulanfragmentspercleavageevent.Theproposedmechanismofactivationbyalterationinactionpatternwasreminiscentofinitialworkinthediscoveryofxyloglucanendotransglycosylase.Therefore,theABIlityoflimitdextrinasetocatalysetransglycosylationreactionsintopullulanwastestedandconfirmedbyanassaybasedontheincorporationofafluorescentlylabelledmaltotriosederivativeintohigher-molecular-weightproducts.Thetransglycosylationreactionwasdependentonlimitdextrinaseactivityandwasenhancedinmorehighlypurifiedpreparationsoflimitdextrinase.Transglycosylationwasinhibitedbyunlabelledmaltotriose.Howtransglycosylationaccountsfortheapparentactivationoflimitdextrinasebymaltodextrinsandthephysiologicalrelevanceofthisnovelreactionarediscussed.
Efficientsecretoryexpressionoffunctionalbarleylimitdextrinaseinhibitorbyhighcell-densityfermentationofPichiapastoris.
Jensen,J.M.,Vester-Christensen,M.B.,Møller,M.S.,Bønsager,B.C.,Christensen,H.E.M.,Hachem,M.A.&Svensson,B.(2011).ProteinExpressionandPurification,79(2),217-222.
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Thelimitdextrinaseinhibitor(LDI)frombarleyseedsactsspecificallyonlimitdextrinase(LD),anendogenousstarchdebranchingenzyme.LDIisa14kDahydrophobicproteincontainingfourdisulfidebondsandoneunpairedthiolgrouppreviouslyfoundtobeeitherglutathionylatedorcysteinylated.Itisamemberoftheso-calledCM-proteinfamilythatincludesα-amylaseandserineproteaseinhibitors,whichhavebeenextremelychallengingtoproducerecombinantlyinfunctionalformandingoodyields.Here,LDIisproducedinveryhighyieldsbysecretoryexpressionbyPichiapastorisapplyinghighcell-densityfermentationina5Lfed-batchbioreactor.Thusabout200mgofLDI,whichshowedtwofoldhigherinhibitoryactivitytowardsLDthanLDIfrombarleyseeds,waspurifiedfrom1LofculturesupernatantbyHis-tagaffinitychromatographyandgelfiltration.ElectrosprayionizationmassspectrometryverifiedtheidentityoftheproducedglutathionylatedLDI-His6.Ata1:1MratiotherecombinantLDIcompletelyinhibitedhydrolysisofpullulancatalyzedby5–10nMLD.LDIretainedstabilityinthepH2–12rangeandatpH6.5displayedahalf-lifeof53and33minat90and93°C,respectively.TheefficientheterologousproductionofLDIsuggestssecretoryexpressionbyP.pastoristobeapromisingstrategytoobtainotherrecombinantCM-proteins.
ThesurvivaloflimitdextrinaseduringfermentationintheproductionofScotchwhisky.
Walker,J.W.,Bringhurst,T.A.,Broadhead,A.L.,Brosnan,J.M.&Pearson,S.Y.(2001).JournaloftheInstituteofBrewing,107(2),99-106.
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Limitdextrinase,isanimportantenzymeinthehydrolysisofstarchfromcerealstofermentablesugars.WorkisdescribedwhichdemonstratestheimportanceofthisenzymeintheproductionofScotchwhisky.Thestudyconsiderstheoccurrence,survivalandactionoflimitdextrinase(totalandfree)duringfermentationinmaltandgraindistilleries.Theresultsofbothlaboratoryanddistillerystudiesrevealedthatlimitdextrinasecansurvivetheconditionsencounteredduringmashingandisnotonlypresentinthefermenterbutitsactivitycanincreaseduringfermentation.ThisobservationhasimportantimplicationsfortheproductionofScotchwhisky,sincethefermentationsubstrate(wash)isnotboiled,theenzymeisthereforeavailabletodegradedextrinsintofermentablesugars,andcanpotentiallyincreasetheyieldofalcohol.
Thioredoxininbarley:couldithavearoleinreleasinglimitdextrinaseinbrewerymashes?
Heisner,C.B.&Bamforth,C.W.(2008).JournaloftheInstituteofBrewing,114(2),122-126.
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Thereisnotastrongcorrelationbetweentheamountofthioredoxininbarleyandthetotalproteincontentofthegrain.Thelevelofdetectablethioredoxindecreasesduringgermination,whereastheamountoflimitdextrinaseincreases,forthemostpartinaboundform.Undernocircumstancescouldareleaseoflimitdextrinaseinanactiveformbedemonstratedthroughtheagencyofthethioredoxinsystem.Bycontrastthethiolagentdithiothreitol,especiallyinthepresenceofcalcium,didpromotetheactivationoflimitdextrinase.Ofmostpronouncedeffect,however,wastheloweringofpH.Three-foldhigherlimitdextrinaseactivitywasachievedwhenthepHwasloweredto4.0.
SecretoryexpressionoffunctionalbarleylimitdextrinasebyPichiapastorisusinghighcell-densityfermentation.
Vester-Christensen,M.B.,Hachem,M.A.,Naested,H.&Svensson,B.(2010).ProteinExpressionandPurification,69(1),112-119.
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Heterologousproductionoflargemultidomainproteinsfromhigherplantsisoftencumbersome.Barleylimitdextrinase(LD),a98kDamultidomainstarchandα-limitdextrindebranchingenzyme,playsamajorroleinstarchmobilizationduringseedgerminationandispossiblyinvolvedinstarchbiosynthesisbytrimmingofintermediatebranchedα-glucanstructures.HighlyactivebarleyLDisobtainedbysecretoryexpressionduringhighcell-densityfermentationofPichiapastoris.TheLDencodinggenefragmentwithoutsignalpeptidewassubclonedin-framewiththeSaccharomycescerevisiaeα-factorsecretionsignaloftheP.pastorisvectorpPIC9Kundercontrolofthealcoholoxidase1promoter.Optimizationofafed-batchfermentationprocedureenabledefficientproductionofLDina5-Lbioreactor,whichcombinedwithaffinitychromatographyonβ-cyclodextrin–SepharosefollowedbyHiloadSuperdex200gelfiltrationyielded34mghomogenousLD(84%recovery).TheidentityoftherecombinantLDwasverifiedbyN-terminalsequencingandbymassspectrometricpeptidemapping.Amolecularmassof98kDawasestimatedbySDS–PAGEinexcellentagreementwiththetheoreticalvalueof97419Da.KineticconstantsofLDcatalyzedpullulanhydrolysiswerefoundtoKm,app=0.16±0.02mg/mLandKcat,app=79±10s-1byfittingtheuncompetitivesubstrateinhibitionMichaelis–Mentenequation,whichreflectssignificantsubstrateinhibitionand/ortransglycosylation.Theresultingcatalyticcoefficient,Kcat,app/Km,app=488±23mL/(mgs)is3.5-foldhigherthanforbarleymaltLD.Surfaceplasmonresonanceanalysisshowedα-,β-,andγ-cyclodextrinbindingtoLDwithKdof27.2,0.70,and34.7µM,respectively.
Theadvantagesofusingnaturalsubstrate‐basedmethodsinassessingtherolesandsynergisticandcompetitiveinteractionsofbarleymaltstarch‐degrADIngenzymes.
Osman,A.M.(2002).JournaloftheInstituteofBrewing,108(2),204-214.
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Existingmethodsofassayofmaltstarch-degradingenzymeswerecriticallyappraised.Newmethodsbasedonnaturalsubstrates,namelystarchanditsnaturalintermediate-derivative,weredevelopedforalltheenzymes,exceptlimitdextrinaseforwhichpullulanwasused.Thermostability,optimaltemperaturesandpHswereestablished.α-Amylaseandlimitdextrinasewerethemostthermostableandβ-amylase,α-glucosidaseandmaltaseweretheleaststablewhilediastaseoccupiedanintermediateposition.Theoptimaltemperatureswerecongruentwiththermostability,β-amylasehavingthelowest(50°C)andα-amylasethehighest(65°C)withtheremainingenzymes,includingdiastase,fallinginbetween.Incontrast,α-amylasehasthelowestoptimalpH(pH4.5)andβamylasethehighest(pH5.5)whiletheothershavepHsinbetweenthetwovalues.Therolesoftheenzymeswereevaluatedtakingintoaccountthelevelofactivity,thermostability,optimumpH,thenatureoftheproduct(s),andtherelevancetobrewing.β-Amylaseproductionofmaltosewassynergisticallyenhanced,mostlybyα-amylasebutalsolimitdextrinase.α-Glucosidaseandmaltaseareunimportantforbrewing,becauseoftheirlowactivityandthenegativeimpactonβ-amylaseactivityandthenegativeeffectofglucoseonmaltoseuptakebyyeast.Thestarch-degradingenzymes(diastase)inagramofmaltwereabletodegrademorethan8gboiledstarchintoreducingsugarsin10minat65°C.Thelatter,suggeststhatitwillbepossibletogelatinisemostofthemaltstarchatahighertemperatureandensureitshydrolysistofermentablesugarsbymixingwithsmallerportionsofmaltandmashingatlowertemperaturese.g.50–60°C.
Oligosaccharideandsubstratebindinginthestarchdebranchingenzymebarleylimitdextrinase.
Møller,M.S.,Windahl,M.S.,Sim,L.,Bøjstrup,M.,Hachem,M.A.,Hindsgaul,O.,Palcic,M.,Svensson,B.&Henriksen,A.(2015).JournalofMolecularBIOLOGy,427(6),1263-1277.
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Completehydrolyticdegradationofstarchrequireshydrolysisofboththeα-1,4-andα-1,6-glucosidicbondsinamylopectin.Limitdextrinase(LD)istheonlyendogenousbarleyenzymecapableofhydrolyzingtheα-1,6-glucosidicbondduringseedgermination,andimpairedLDactivityinevitablyreducesthemaltoseandglucoseyieldsfromstarchdegradation.CrystalstructuresofbarleyLDandactive-sitemutantswithnaturalsubstrates,productsandsubstrateanaloguesweresoughttobetterunderstandthefacetsofLD–substrateinteractionsthatconfinehighactivityofLDtobranchedmaltooligosaccharides.Forthefirsttime,anintactα-1,6-glucosidicallylinkedsubstratespanningtheactivesiteofaLDorpullulanasehasbeentrappedandcharacterizedbycrystallography.Thecrystalstructurerevealsboththebranchandmain-chainbindingsitesandisusedtosuggestamechanismfornucleophilicityenhancementintheactivesite.Thesubstrate,productandanaloguecomplexeswerefurtherusedtooutlinesubstratebindingsubsitesandsubstratebindingrestraintsandtosuggestamechanismforavoidanceofdualα-1,6-andα-1,4-hydrolyticactivitylikelytobeabiologicalnecessityduringstarchsynthesis.
Achromogenicassaysuitableforhigh-throughputdeterminationoflimitdextrinaseactivityinbarleymaltextracts.
Bøjstrup,M.,Marri,L.,Lok,F.&Hindsgaul,O.(2015).JournalofagriculturalandFoodChemistry,63(50),10873-10878.
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Twenty-fourmaltsampleswereassayedforlimitdextrinaseactivityusingachromogenicassaydevelopedrecentlyinourgroup.Theassayutilizesasmallsolublechromogenicsubstratewhichishydrolyzedselectivelybylimitdextrinaseinacoupledassaytoreleasethechromophore2-chloro-4-nitrophenol.Thereleaseofthechromophore,correspondingtotheactivityoflimitdextrinase,canbefollowedbymeasuringtheUVabsorptionat405nm.The24maltsamplesrepresentedawidevariationoflimitdextrinaseactivities,andtheseactivitiescouldbeclearlydifferentiatedbytheassay.Theresultsobtainedwerecomparablewiththeresultsobtainedfromacommerciallyavailableassay,Limit-DextrizymefromMegazymeInternationalIreland.Furthermore,theimprovedassayusesasolublesubstrate.Thatmakesitwellsuitedforhigh-throughputscreeningasitcanbehandledina96-wellplateformat.
ValidationofMethods
RACIStandardMethod
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
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