Megazyme/羧甲基纤维素4M/P-CMC4M/40克
商品编号：
P-CMC4M
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
HighpurityCarboxymethylCellulose4Mforuseinresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Carboxymethylated(DS~0.4),mediumviscositycellulose.Recommendedsubstratefortheassayofcellulasesbyreducingsugarmethods.Formostendo-cellulases,thisisamuchmoresensitivesubstratethanCMC-7M(DS=0.7).
Afibrolyticpotentialinthehumanileummucosalmicrobiotarevealedbyfunctionalmetagenomics.
Patrascu,O.,Béguet-Crespel,F.,Marinelli,L.,LeChatelier,E.,Abraham,A.,Leclerc,M.,Klopp,C.,Terrapon,N.,Henrissat,B.,Blottière,H.M.,Doré,J.&ChristelBéra-Maillet.(2017).ScientificReports,7,40248.
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Thedigestionofdietaryfibersisamajorfunctionofthehumanintestinalmicrobiota.SofarthisfunctionhasbeenattributedtothemicroorganismsinhABItingthecolon,andmanystudieshavefocusedonthisdistalpartofthegastrointestinaltractusingeasilyaccessIBLefecalmaterial.However,microbialfermentations,supportedbythepresenceofshort-chainfattyacids,aresUSPectedtooccurintheuppersmallintestine,particularlyintheileum.Usingafosmidlibraryfromthehumanilealmucosa,wescreened20,000clonesfortheiractivitiesagainstcarboxymethylcelluloseandxylanschosenasmodelsofthemajorplantcellwall(PCW)polysaccharidesfromdietaryfibres.ElevenpositiveclonesrevealedabroadrangeofCAZymeencodinggenesfromBacteroidesandClostridialesspecies,aswellasPolysaccharideUtilizationLoci(PULs).Thefunctionalglycosidehydrolasegeneswereidentified,andoligosaccharidebreak-downproductsexaminedfromdifferentpolysaccharidesincludingmixed-linkageβ-glucans.CAZymesandPULswerealsoexaminedfortheirprevalenceinhumangutmicrobiome.Severalclustersofgenesoflowprevalenceinfecalmicrobiomesuggestedtheybelongtounidentifiedstrainsratherspecificallyestablishedupstreamthecolon,intheileum.Thus,theilealmucosa-associatedmicrobiotaencompassestheenzymaticpotentialforPCWpolysaccharidedegradationinthesmallintestine.
PurificationandCharacterizationofaThermostableβ-mannanasefromBacillussubtilisBE-91:PotentialApplicationinInflammatoryDiseases.
Cheng,L.,Duan,S.,Feng,X.,Zheng,K.,Yang,Q.,&Liu,Z.(2016).BioMedResearchInternational,ID6380147.
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β-mannanasehasshowncompellingBIOLOGicalfunctionsbecauseofitsregulatoryrolesinmetabolism,inflammation,andoxidation.Thisstudyseparatedandpurifiedtheβ-mannanasefromBacillussubtilisBE-91,whichisapowerfulhemicellulose-degrADIngbacteriumusinga“two-step”methodcomprisingultrafiltrationandgelchromatography.Thepurifiedβ-mannanase(about28.2 kDa)showedhighspecificactivity(79,859.2 IU/mg).TheoptimumtemperatureandpHwere65°Cand6.0,respectively.Moreover,theenzymewashighlystableattemperaturesupto70°CandpH4.5–7.0.Theβ-mannanaseactivitywassignificantlyenhancedinthepresenceofMn2+,Cu2+,Zn2+,Ca2+,Mg2+,andAl3+andstronglyinhibitedbyBa2+andPb2+.KmandVmaxvaluesforlocustbeangumwere7.14 mg/mLand107.5 µmol/min/mLversus1.749 mg/mLand33.45 µmol/min/mLforKonjacglucomannan,respectively.Therefore,β-mannanasepurifiedbythisworkshowsstabilityathightemperaturesandinweaklyacidicorneutralenvironments.Basedonsuchdata,theβ-mannanasewillhavepotentialapplicationsasadietarysupplementintreatmentofinflammatoryprocesses.
Enzymaticpreparationofmushroomdietaryfibre:Acomparisonbetweenanalyticalandindustrialenzymes.
Wong,K.H.&Cheung,P.C.K.(2009).FoodChemistry,115(3),795-800.
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Acomparativestudyonpreparingdietaryfibres(DFs)fromthreemushroomsclerotia,namely,Pleurotustuber-regium(PTR),Polyporusrhinocerus(PR)andWolfiporiacocos(WC),usinganalyticalorindustrialenzymes(includingα-amylase,proteaseandamyloglucosidase),wasconducted.Apartfromenzymeactivityandpurity,theireffectsontheyieldofsclerotialDFaswellasitsmajorcomponents,suchasβ-glucans,chitinandresistantglycogen(RG),wereinvestigatedandcompared.Theactivitiesofallindustrialenzymesweresignificantlylowerthanthoseoftheircorrespondinganalyticalones,exceptfortheFungamyl®SuperMA,whichhadthehighestα-amylaseactivity(6395U/g).However,thisfungalα-amylasewaslessabletodigestthethreesclerotialglycogenswhencomparedwiththebacterialalternatives.Amongstalltestedenzymes,onlyanalyticalandindustrialamyloglucosidaseswerefoundtohavesignificantamountofcontaminatingcellulase(7.05–7.07U/ml)andlichenase(4.62–4.67U/ml)activities,whichwouldcauseendo-depolymerizationoftheβ-glucan-typecellwallcomponents(3.39%reductioninglucoseresidueafterRGcorrection)ofthePTR,leadingtoamarkedα-amylasehydrolysisofitsotherwisephysically-inaccessiblecytoplasmicglycogen(20.3%reductioninRGcontent).CommercialproductionofthethreenovelsclerotialDFs,usingtheindustrialenzymes,wouldbefeasiblesince,inadditiontotheireconomicadvantage,boththeyield(PTR:81.2%;PR:86.5%;WC:96.2%ofsampleDM)andtotalnon-starchpolysaccharidecontents(PTR:88.0%;PR:92.5%;WC:91.1%DF-richmaterialsofDM)oftheirresultingsclerotialDFswerecomparabletothelevelsofthosepreparedusinganalyticalenzymes.
CharacterizationofafunctionalsolubleformofaBrassicanapusmembrane-anchoredendo-1,4-β-glucanaseheterologouslyexpressedinPichiapastoris.
Mølhøj,M.,Ulvskov,P.&DalDegan,F.(2001).PlantPhysiology,127(2),674-684.
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TheBrassicanapusgene,Cel16,encodesamembrane-anchoredendo-1,4-β-glucanasewithadeducedmolecularmassof69kD.Asforothermembrane-anchoredendo-1,4-β-glucanases,Cel16consistsofapredictedintracellular,chargedNterminus(methionine1-lysine70),ahydrophobictransmembranedomain(isoleucine71-valine93),andaperiplasmiccatalyticcore(lysine94-proline621).Here,wereportthefunctionalanalysisofΔ1-90Cel16,theNterminallytruncatedCel16,missingresidues1through90andcomprisingthecatalyticdomainofCel16expressedrecombinantlyinthemethylotrophicyeastPichiapastorisasasolubleprotein.Atwo-steppurificationprotocolyieldedΔ1-90Cel16inapureform.ThemolecularmassofΔ1-90Cel16,whendeterminedbysodiumdodecylsulfate-polyacrylamidegelelectrophoresis,wasabout130kDandabout60kDafterenzymaticremovalofN-glycans,fittingtheexpectedmolecularmassof59kD.Δ1-90Cel16washighlyNglycosylatedascomparedwiththenativeB.napusCel16protein.Δ1-90Cel16hadapHoptimumof6.0.TheactivityofΔ1-90Cel16wasinhibitedbyEDTAandexhibitedastrongdependenceoncalcium.Δ1-90Cel16showedsubstratespecificityforlowsubstitutedcarboxymethyl-celluloseandamorphouscellulose.Itdidnothydrolyzecrystallinecellulose,xyloglycan,xylan,(1→3),(1→4)-β-D-glucan,thehighlysubstitutedhydroxyethylcellulose,ortheoligosaccharidescellotriose,cellotetraose,cellopentaose,orxylopentaose.SizeexclusionanalysisofΔ1-90Cel16-hydrolyzedcarboxymethylcelluloseshowedthatΔ1-90Cel16isatrueendo-actingglucanase.
Propertiesoffamily79β-glucuronidasesthathydrolyzeβ-glucuronosyland4-O-methyl-β-glucuronosylresiduesofarabinogalactan-protein.
Konishi,T.,Kotake,T.,Soraya,D.,Matsuoka,K.,Koyama,T.,Kaneko,S.,Igarashi,K.,Samejima,M.&Tsumuraya,Y.(2008).CarbohydrateResearch,343(7),1191-1201.
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Thecarbohydratemoietiesofarabinogalactan-proteins(AGPs),whicharemainlycomposedofGal,L-Ara,GlcA,and4-Me-GlcAresidues,areessentialforthephysiologicalfunctionsoftheseproteoglycansinhigherplants.Forthisstudy,wehaveidentifiedtwogenesencodingfamily79β-glucuronidases,designatedAnGlcAaseandNcGlcAase,inAspergillusnigerandNeurosporacrassa,respectively,basedontheaminoacidsequenceofanativeβ-glucuronidasepurifiedfromacommercialpectolyticenzymepreparationfromA.niger.AlthoughthededucedproteinsequencesofAnGlcAaseandNcGlcAasewerehighlysimilar,therecombinantenzymesexpressedinPichiapastorisexhibiteddistinctsubstratespecificitytoward4-Me-GlcAresiduesofAGPs:recombinantAnGlcAase(rAnGlcAase)substantiallyliberatedbothGlcAand4-Me-GlcAresiduesfromradishAGPs,whereasrecombinantNcGlcAase(rNcGlcAase)activityonthe4-Me-GlcAresiduesofAGPswasverylow.MaximumactivityofrAnGlcAasehydrolyzingPNPβ-GlcAoccurredatpH3.0–4.0,whereasthemaximumrNcGlcAaseactivitywasatpH6.0.TheapparentKmvaluesofrAnGlcAasewere30.4µMforPNPβ-GlcAand422µMforβ-GlcA-(1→6)-Gal,andthoseofrNcGlcAasewere38.3µMand378µM,respectively.Similartothenativeenzyme,rAnGlcAasewasabletocatalyzethetransglycosylationofGlcAresiduesfromPNPβ-GlcAtovariousmonosaccharideacceptorssuchasGlc,Gal,andXyl.WeproposethatbothAnGlcAaseandNcGlcAaseareinstancesofanoveltypeofβ-glucuronidasewiththecapacitytohydrolyzeβ-GlcAand4-Me-β-GlcAresiduesofAGPs,althoughtheydiffersignificantlyintheirpreferences.
Axyloglucan-specificfamily12glycosylhydrolasefromAspergillusniger:recombinantexpression,purificationandcharacterization.
Master,E.R.,Zheng,Y.,Storms,R.,Tsang,A.&Powlowski,J.(2008).Biochem.J,411,161-170.
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AnewGH12(glycosylhydrolase12)familyXEG[xyloglucan-specificendo-β-1,4-glucanase(EC3.2.1.151)]fromAspergillusniger,AnXEG12A,wasoverexpressed,purifiedandcharacterized.WhereassevenxyloglucanasesfromGH74andtwoxyloglucanasesfromGH5havebeencharacterizedpreviously,thisisonlythethirdcharacterizedexampleofaGH12familyxyloglucanase.GH12enzymesarestructurallyandmechaNISTicallydistinctfromGH74enzymes.Althoughover100GH12sequencesarenowavailable,littleisknownaboutthestructuralandbiochemicalbasesofxyloglucanbindingandhydrolysisbyGH12enzymes.ComparisonoftheAnXEG12ACDNAsequencewiththegenomesequenceofA.nigershowedthepresenceoftwointrons,oneinthecodingregionandthesecondoneinthe333-nt-long3´-untranslatedregionofthetranscript.TheenzymewasexpressedrecombinantlyinA.nigerandwasreadilypurifiedfromtheculturesupernatant.Theisolatedenzymeappearedtohavebeenprocessedbyakexin-typeprotease,whichremovedashortprosequence.Thesubstratespecificitywasrestrictedtoxyloglucan,withcleavageatunbranchedglucoseinthebackbone.Theapparentkineticparametersweresimilartothosereportedforotherxyloglucan-degradingendoglucanases.ThepHoptimum(5.0)andtemperatureresultinginhighestenzymeactivity(50–60°C)werehigherthanthosereportedforaGH12familyxyloglucanasefromAspergillusaculeatus,butsimilartothoseofcellulose-specificendoglucanasesfromtheGH12family.Phylogenetic,sequenceandstructuralcomparisonsofGH12familyendoglucanaseshelpedtodelineatefeaturesthatappeartobecorrelatedtoxyloglucanspecificity.
Degradationofcarbohydratemoietiesofarabinogalactan-proteinsbyglycosidehydrolasesfromNeurosporacrassa.
Takata,R.,Tokita,K.,Mori,S.,Shimoda,R.,Harada,N.,Ichinose,H.,Kaneko,A.,Igarashi,k.,Samejima,M.,Tsumuraya,Y.&Kotake,T.(2010).CarbohydrateResearch,345(17),2516-2522.
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Arabinogalactan-proteins(AGPs)areafamilyofplantproteoglycanshavinglargecarbohydratemoietiesattachedtocore-proteins.ThecarbohydratemoietiesofAGPscommonlyhaveβ-(1→3)(1→6)-galactanasthebackbone,towhichotherauxiliarysugarssuchasL-AraandGlcAareattached.Forthepresentstudy,anα-L-arabinofuranosidasebelongingtoglycosidehydrolasefamily(GHF)54,NcAraf1,andanendo-β-(1→6)-galactanaseofGHF5,Nc6GAL,wereidentifiedinNeurosporacrassa.RecombinantNcAraf1(rNcAraf1)expressedinPichiapastorishydrolyzedradishAGPsaswellasarabinanandarabinoxylan,showingrelativelybroadsubstratespecificitytowardpolysaccharidescontainingα-L-arabinofuranosylresidues.RecombinantNc6GAL(rNc6GAL)expressedinP.pastorisspecificallyactedonβ-(1→6)-galactosylresidues.WhereasAGPfromradishrootswashardlyhydrolyzedbyrNc6GALalone,β-(1→6)-galactansidechainswerereducedtooneortwogalactanresiduesbyacombinationofrNcAraf1andrNc6GAL.TheseresultssuggestthatthecarbohydratemoietiesofAGPsaredegradedbytheconcertedactionofNcAraf1andNc6GALsecretedfromN.crassa.
MolecularcloningandexpressioninEscherichiacoliofaTrichodermavirideendo-beta-(1→6)-galactanasegene.
Kotake,T.,Kaneko,S.,Kubomoto,A.,Haque,M.,Kobayashi,H.&Tsumuraya,Y.(2004).Biochem.J,377(3),749-755.
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Ageneencodingendo-β-(1→6)-galactanasefromTrichodermaviridewasclonedbyreversetranscriptase–PCRandexpressedinEscherichiacoli.Thegenecontainedanopenreadingframeconsistingof1437bp(479aminoacids).Thededucedaminoacidsequenceoftheproteinshowedlittlesimilaritywithotherknownglycosidehydrolases.Asignalsequence(20aminoacids)wasfoundattheN-terminalregionoftheproteinandthemolecularmassofthematureformwascalculatedtobe50.488kDa.ThegeneproductexpressedinE.coliasarecombinantproteinfusedwiththioredoxinandHis6tagshadalmostthesamesubstratespecificityandmodeofactionasnativeenzymepurifiedfromacommercialcellulasepreparationofT.viride,i.e.recombinantenzymeendo-hydrolysedβ-(1→6)-galacto-oligomerswithaDP(degreeofpolymerization)higherthan3,anditcouldalsohydrolyseα-L-arabinofuranosidase-treatedarabinogalactanproteinfromradish.Itproducedβ-(1→6)-galacto-oligomersrangingfromDP2toatleast8attheinitialhydrolysisstageandgalactoseandβ-(1→6)-galactobioseasthemajorproductsatthefinalreactionstage.Theseresultsindicatethattheclonedgeneencodesanendo-β-(1→6)-galactanase.Asfarasweknow,thisisthefirsttimeanendo-β-(1→6)-galactanasehasbeencloned.
CrystalstructuresofClostridiumthermocellumxyloglucanase,XGH74A,revealthestructuralbasisforxyloglucanrecognitionanddegradation.
Martinez-Fleites,C.,Guerreiro,C.I.P.D.,Baumann,M.J.,Taylor,E.J.,Prates,J.A.,Ferreira,L.M.A.,CarlosM.G.A.,Fontes,C.M.G.A.,Brumer,H.&Davies,G.J.(2006).JournalofBiologicalChemistry,281(34),24922-24933.
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Theenzymaticdegradationoftheplantcellwalliscentralbothtothenaturalcarboncycleand,increasingly,toenvironmentallyfriendlyroutestobiomassconversion,includingtheproductionofbiofuels.Theplantcellwallisacomplexcompositeofcellulosemicrofibrilsembeddedindiversepolysaccharidescollectivelytermedhemicelluloses.Xyloglucanisonesuchpolysaccharidewhosehydrolysisiscatalyzedbydiversexyloglucanases.HerewepresentthestructureoftheClostridiumthermocellumxyloglucanaseXgh74Ainbothapoandligand-complexedforms.Thestructures,incombinationwithmutagenesisdataonthecatalyticresiduesandthekineticsandspecificityofxyloglucanhydrolysisrevealacomplexsubsitespecificityaccommodatingseventeenmonosaccharidemoietiesofthemultibranchedsubstrateinanopensubstratebindingterrain.
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
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