Megazyme/D-甘露糖/D-果糖/D-葡萄糖分析试剂盒/K-MANGL/55每个试剂盒的分析
商品编号：
K-MANGL
品牌：
Megazyme INC
市场价：
¥3880.00
美元价：
2328.00
产品分类：
其它检测试剂盒
公司分类：
Other_kits
联系Q Q：
3392242852
电话号码：
4000-520-616
电子邮箱：
info@ebiomall.com
商品介绍
TheD-Mannose/D-Fructose/D-GlucosetestkitissuitableforthespecificmeasurementandanalysisofD-mannose,D-fructoseandD-glucoseinplantproductsandinacidhydrolysatesofpolysaccharides.
Alteredphysiologyandbiochemistryofimportedlitchifruitheldunderdifferentvaporpressuredeficits.
Somboonkaew,N.&Terry,L.A.(2010).JournalofAgriculturalandFoodChemistry,58(10),6209-6218.
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Theeffectsofvaporpressuredeficit(VPD)onlitchifruitqualityhavenotyetbeenfullydefined.Theaimofthisstudywastodetailthechangesinphysiology,sugars,organicacids,andindividualanthocyaninconcentrationsinimportedlitchifruitheldatvariouscontrolledrelativehumidity(RH)andVPDlevels.SO2-fumigated(butnotacid-treated)litchiimportedfromThailand(cv.Kom)andfromIsrael(cv.Mauritius)wereairfreightedtotheUnitedKingdomandthenstoredfor9daysateither5or13°Ctosimulateshelf-lifeconditions.FruitswerestoredunderaseriesofcontrolledRHconditionsforthedurationofthetrialusingdifferentconcentrationsofglycerolindeonizedwater.Respirationratesandweightlossesofbothfruitlotsweregreaterinlitchistoredat13°CandaVPDof0.274kPa.At5°CandaVPDof0or0.042kPa,sugarsandorganicacidsinarilandpericarptissueandindividualanthocyaninsinpericarpwerebettermaintained.ThisisthefirstpieceofworkthathassystematicallyevaluatedtheeffectofaseriesofVPDsonlitchifruitbiochemistrysuchthatimplicationsfordesigningsystemstobettermaintainthephysiologicalqualityofimportedlitchifruitarediscussed.
AnewbacterialhydrolasespecificforthecompatIBLesolutesα-D-mannopyranosyl-(1→2)-D-glycerateandα-D-glucopyranosyl-(1→2)-D-glycerate.
Alarico,S.,EmpADInhas,N.&daCosta,M.S.(2013).EnzymeandMicrobialTechnology,52(2),77-83.
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Theaccumulationpatternsandbiosynthesisofcompatiblesolutesinhyper/Thermophileshavebeenextensivelystudied.However,thereislittleinformationavailableontheirhydrolysis,leadingustosearchforenzymesforthisactivity.Fromtheanalysisofthegenomesofseveralmicroorganismsknowntoaccumulateα-D-mannopyranosyl-(1→2)-D-glycerate(mannosylglycerate,MG)orα-D-glucopyranosyl-(1→2)-D-glycerate(glucosylglycerate,GG)wewereabletoidentifyalikelycandidategeneforthehydrolysisofthesemolecules.TheThermusthermophilusHB27homologueencodedaputativeenzymewithmotifsoftheGH63andGH37familiesofglycosidehydrolases.WeexpressedthegenefromthisthermophilicbacteriumandfromRubrobacterradiotolerans,andconfirmedthattherecombinantenzymes,heredesignatedmannosylglyceratehydrolase(MgH),specificallyhydrolysedMG(orGG)tomannose(orglucose)andglycerate.Bothenzymeswerehighlystableandmaximallyactiveattemperaturesclosetoeachorganisms’optimalgrowthtemperatures(half-livesof15.4±0.5hat55°Cand16.1±0.4hat70°C)butatlowpH(4.0–4.5).CationswerenotrequiredfortheiractivityandeachenzymeexhibitedMichaelis–Mentenkineticsat50°Cand70°C,respectively,withcomparablecatalyticefficienciestowardsMGandGG.Herein,wepurifiedandcharacterizedanovelandhighlyspecificMG-andGG-hydrolyzingenzymethatrepresentanattractivetoolfordevelopmentofenzymaticassaysforquantificationofthesesolutes,whichseemtobemoreprevalentinmicroorganismsthaninitiallysUSPected.
ThemolecularcharacterizationofanovelGH38α-mannosidasefromthecrenarchaeonSulfolobussolfataricusrevealeditsABIlityinde-mannosylatingglycoproteins.
Cobucci-Ponzano,B.,Conte,F.,Strazzulli,A.,Capasso,C.,Fiume,I.,Pocsfalvi,G.,Rossi,M.&Moracci,M.(2010).Biochimie,92(12),1895-1907.
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α-Mannosidases,importantenzymesintheN-glycanprocessinganddegradationinEukaryotes,arefrequentlyfoundinthegenomeofBacteriaandArchaeainwhichtheirfunctionisstilllargelyunknown.Theα-mannosidasefromthehyperthermophilicCrenarchaeonSulfolobussolfataricushasbeenidentifiedandpurifiedfromcellularextractsanditsgenehasbeenclonedandexpressedinEscherichiacoli.Thegene,belongingtoretainingGH38mannosidasesofthecarbohydrateactiveenzymeclassification,isabundantlyexpressedinthisArchaeon.Thepurifiedα-mannosidaseactivitydependsonasingleZn2+ionpersubunitisinhibitedbyswainsoninewithanIC50of0.2mM.Themolecularcharacterizationofthenativeandrecombinantenzyme,namedSsα-man,showedthatitishighlyspecificforα-mannosidesandα(1,2),α(1,3),andα(1,6)-D-mannobioses.Inaddition,theenzymeisabletodemannosylateMan3GlcNAc2andMan7GlcNAc2oligosaccharidescommonlyfoundinN-glycosylatedproteins.Moreinterestingly,Ssα-manremovesmannoseresiduesfromtheglycosidicmoietyofthebovinepancreaticribonucleaseB,suggestingthatitcouldprocessmannosylatedproteinsalsoinvivo.Thisisthefirstevidencethatarchaealglycosidasesareinvolvedinthedirectmodificationofglycoproteins.
TheplantSelaginellamoellendorffiipossessesenzymesforsynthesisandhydrolysisofthecompatiblesolutesmannosylglycerateandglucosylglycerate.
Nobre,A.,Empadinhas,N.,Nobre,M.F.,Lourenço,E.C.,Maycock,C.,Ventura,M.R.,MingoteA.&daCosta,M.S.(2013).Planta,237(3),891-901.
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Amannosylglyceratesynthase(MgS)genedetectedinthegenomeofSelaginellamoellendorffiiwasexpressedinE.coliandtherecombinantenzymewaspurifiedandcharacterized.Aremarkableandunprecedentedfeatureofthisenzymewastheabilitytoefficientlysynthesizemannosylglycerate(MG)andglucosylglycerate(GG)alike,withmaximalactivityat50°C,pH8.0andwithMg2+asreactionenhancer.Wehavealsoidentifiedanovelglycosidehydrolasegeneinthisplant’sgenome,whichwasfunctionallyconfirmedtobehighlyspecificforthehydrolysisofMGandGGandnamedMGhydrolase(MgH),duetoitshomologywithbacterialMgHs.Therecombinantenzymewasmaximallyactiveat40°CandatpH6.0–6.5.Theactivitywasindependentofcations,butMn2+wasastrongstimulator.RegardlessoftheseefficientenzymaticresourceswecouldnotdetectMGorGGinS.moellendorffiiorintheextractsoffiveadditionalSelaginellaspecies.Herein,wedescribethepropertiesofthefirsteukaryoticenzymesforthesynthesisandhydrolysisofthecompatiblesolutes,MGandGG.
Celllysisinducedbymembrane-damagingdetergentsaponinsfromQuillajasaponaria.
Berlowska,J.,Dudkiewicz,M.,Kregiel,D.,Czyzowska,A.&Witonska,I.(2015).EnzymeandMicrobialTechnology,75,44-48.
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ThispaperpresentstheresultsofastudytodeterminetheeffectofQuillajasaponariasaponinsonthelysisofindustrialyeaststrains.CelllysisinducedbysaponinfromQ.saponariacombinedwiththeplasmolysingeffectof5%NaClforSaccharomycescerevisiae,Kluyveromycesmarxianusyeastsbiomasswasconductedat50°Cfor24–48 h.Membranepermeabilityandintegrityoftheyeastcellsweremonitoredusingfluorescenttechniquesandconcentrationsofproteins,freeaminonitrogen(FAN)andfreeaminoacidsinresultinglysateswereanalyzed.Proteinreleasewassignificantlyhigherinthecaseofyeastcelllysispromotedwith0.008%Q.saponariaand5%NaClincomparisontoplasmolysistriggeredbyNaClonly.
Strategicoptimizationofxylanase–mannanasecombi-CLEAsforsynergisticandefficienthydrolysisofcomplexlignocellulosicsubstrates.
Bhattacharya,A.&Pletschke,B.I.(2015).JournalofMolecularCatalysisB:Enzymatic,115,140-150.
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Cost-effectiveapplicationoflignocellulolyticenzymesholdsthekeytowardscommercializationofenzymatichydrolysisoflignocellulosicbiomass.Carrierfreeimmobilizationofenzyme(s)offersalucrativeProspect.Combined-crosslinkedenzymeaggregates(combi-CLEAs)areanovelprospectiveandthispresentstudyaddressesthepreparation,characterizationandapplicationofxylanase–mannanasecombi-CLEASonlime-preteatedsugarcanebagasseandmilledcornstover.X6-CLEAs,X7-CLEAs,L1-CLEAsandL7-CLEAswerepreparedafterelaborativeoptimizationoftheprecipitatingagentandglutaraldehydeconcentration.Thehighestactivityafterprecipitationwasobservedwithacetonebutfollowingcross-linkingwithglutaraldehydelessthan60%activitywasretained,whilemorethan60%activitywasretainedafterprecipitationwithammoniumsulphateandcross-linkingwithglutaraldehyde.Accessoryenzymeactivitiesincludingα-arabinofuranosidase,β-xylosidase,esterases,β-mannosidase,α-galactosidaseandβ-glucosidasewerealsodetermined.Morethanan1.5foldincreaseinthermostabilitycomparedtothefreeenzymewasobservedoverabroadtemperaturerange(50–70°C).Tri-synergystudiesandquadsynergystudieswereusedtogeneratecombi-CLEAswithdifferentproteinratios.Hydrolysisoflimepre-treatedbagassewithcombi-CLEAsatproteinratioscorrespondingtoX6(33.0%):X7(17.0%):L1(17.0%):L7(33.0%)resultedina1.68foldhighersugarreleasecomparedtothequadsynergymodelusingfreeenzymes.Similarly,hydrolysisofcornstoverwithcombi-CLEAsatproteinratioscorrespondingtoX6(40.0%):X7(10.0%):L1(10.0%):L7(40.0%)resultedinan1.58foldhighersugarreleasecomparedtothesugarreleaseobservedwiththequadsynergymodelusingfreeenzymes.Monomericsugarsconstituted70–75%ofreducingsugarsreleasedduringhydrolysis.Theroleofaccessoryenzymesinimprovingenzymesynergywasclearlyshown.Theefficiencyofcombi-CLEAscomparedtofreeenzymesmakesthemidealcandidatesfortheprudentandcost-effectivecommercializationoflignocellulolyticenzymes.
ABacteroideteslocusdedicatedtofungal1,6-β-glucandegradation:uniquesubstrateconformationdrivesspecificityofthekeyendo-1,6-β-glucanase.
Temple,M.J.,Cuskin,F.,Baslé,A.,Hickey,N.,Speciale,G.,Williams,S.J.,Gilbert,H.J.&Lowe,E.C.(2017).JournalofBIOLOGicalChemistry,jbc-M117.
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Glycansaremajornutrientsavailabletothehumangutmicrobiota(HGM).TheBacteroidesaregeneralistglycandegradersandthisfunctionismediatedlargelybypolysaccharideutilizationloci(PULs).ThegenomesofseveralBacteroidesspeciescontainaPUL,PUL1,6-beta;-glucan,thatwaspredictedtotargetmixedlinkedplant1,3;1,4-beta-glucans.TotestthishypothesiswecharacterizedtheproteinsencodedbythislocusinBacteroidesthetaiotaomicron,amemberoftheHGM.WeshowherethatPUL1,6-β-glucandoesnotorchestratethedegradationofaplantpolysaccharidebuttargetsafungalcellwallglycan,1,6-beta-glucan,whichisagrowthsubstrateforthebacterium.Thelocusisupregulatedby1,6-beta-glucan,andencodestwoenzymes,asurfaceendo-1,6-beta-glucanase,BT3312,andaperiplasmicbeta-glucosidasethattargetsprimarily1,6-beta-glucans.Thenon-catalyticproteinsencodedbyPUL1,6-beta-glucantarget1,6-beta-glucansandcompriseasurfaceglycanbindingproteinandaSusDhomologuethatdeliversglycanstotheoutermembranetransporter.Weidentifiedthecentralroleoftheendo-1,6-beta-glucanasein1,6-beta-glucandepolymerizationbydeletingbt3312,whichpreventedthegrowthofB.thetaiotaomicronon1,6-beta-glucan.ThecrystalstructureofBT3312incomplexwithβ-glucosyl-1,6-deoxynojirimycin,revealedaTIMbarrelcatalyticdomainthatcontainsadeepsubstratebindingclefttailoredtoaccommodatethehook-likestructureadoptedby1,6-beta-glucan.Specificityisdrivenbythecomplementarityoftheenzymeactivesitecleftandtheconformationofthesubstrate.WealsonotedthatPUL1,6-beta-glucanissyntenictomanyPULsfromotherBacteroidetessuggestingthatutilizationofyeastandfungalcellwall1,6-beta-glucansisawidespreadadaptationwithinthehumanmicrobiota.
Useofalmondshellasfoodingredient.
Kacem,I.,Martinez-Saez,N.,Kallel,F.,Khawla,J.B.,Claire,H.B.,Semia,C.E.&delCastillo,M.D.(2017).EuropeanFoodResearchandTechnology,1-12.
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Almondshellisamajorwastefromthealmondprocessingindustry.Itsfeasibilityasnaturalsourceofhealth-promotingcomponentswasexamined.Theby-productwasfractionatedunderbasicconditionsfollowinganeasyscale-upprocess.Thechemicalcompositionoftherecoveredfractionanditsantioxidantandantidiabeticpropertieswereevaluated.Novelinformationregardingthechemicalcompositionofthepolysaccharideswasalsoobtained.Almondshellisformedbylignin-carbohydratecomplexespossessingantioxidantpropertiesandcapacitytoinhibitα-glucosidase.Accordingtoourknowledge,thisisthefirsttimeα-glucosidaseinhibitoryactivityofalignin-carbohydratecomplexisreported.Biscuitscontainingnon-caloricsweetenersoluble(2.5%)andinsoluble(5.6%)dietaryfiber,naturalantioxidants(1.34mgofgallicacidequivalents/g)andα-glucosidaseinhibitors(1gofbiscuit–1mgofacarbose)achievedahighsensorialscore(7.2outof9)whenalmondshellwasincorporatedtothem.Theapplicationofafractionfromalmondshellcontaininglignin-polysaccharidescomplexesasfoodingredientinbiscuitformulationsforpeoplewithparticularnutritionalrequirementsisfeasibleandnew.
UV-methodforthedeterminationofD-Mannose,D-Fructose
andD-Glucoseinfoodstuffs,yeastcellpreparationsand
othermaterials
Principle:
(hexokinase)
(1)D-Mannose/D-fructose/D-glucose+ATP→
M-6-P/F-6-P/G-6-P+ADP
(glucose-6-phosphatedehydrogenase)
(2)G-6-P+NADP+→gluconate-6-phosphate+NADPH+H+
(phosphomannoseisomerase)(phosphoglucoseisomerase)
(3) M-6-P ↔ F-6-P ↔ G-6-P
Kitsize: *55assays
* Thenumberofmanualtestsperkitcanbedoubledifallvolumesarehalved.
ThiscanbereadilyaccommodatedusingtheMegaQuantTM Wave
Spectrophotometer(D-MQWAVE).Method: Spectrophotometricat340nm
Reactiontime: ~30min
Detectionlimit: 0.7mg/L
Applicationexamples:
Foodstuffs,yeastcellpreparations,enzymatichydrolysatesandother
materials(e.g.biologicalcultures,samples,etc.)
Methodrecognition: Novelmethod
Advantages
- Verycompetitiveprice(costpertest)
- Allreagentsstablefor>2yearsafterpreparation
- Onlyenzymatickitavailable
- Simpleformat
- Rapidreaction
- Mega-Calc™softwaretoolisavailablefromourwebsiteforhassle-freerawdataprocessing
- Standardincluded
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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