巨酶/木聚糖（罗望子）/P-XYGLN/3克
商品编号：
P-XYGLN
品牌：
Megazyme INC
市场价：
¥2976.00
美元价：
1785.60
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
HighpurityXyloglucan(Tamarind)foruseinresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Purity~95%.Highviscosity.Ara:Gal:Xyl:Glc=3:18:34:45
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.
ArsenalofplantcellwalldegrADIngenzymesreflectshostpreferenceamongplantpathogenicfungi.
King,B.C.,Waxman,K.D.,Nenni,N.V.,Walker,L.P.,Bergstrom,G.C.&Gibson,D.M.(2011).BiotechnolBiofuels,4(4).
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Background:Thediscoveryanddevelopmentofnovelplantcellwalldegradingenzymesisakeysteptowardsmoreefficientdepolymerizationofpolysaccharidestofermentablesugarsfortheproductionofliquidtransportationbiofuelsandotherbioproducts.TheindustrialfungusTrichodermareeseiisknowntobehighlycellulolyticandisamajorindustrialmicrobialsourceforcommercialcellulases,xylanasesandothercellwalldegradingenzymes.However,enzyme-ProspectingresearchcontinuestoidentifyopportunitiestoenhancetheactivityofT.reeseienzymepreparationsbysupplementingwithenzymaticdiversityfromothermicrobes.Thegoalofthisstudywastoevaluatetheenzymaticpotentialofabroadrangeofplantpathogenicandnon-pathogenicfungifortheirabilitytodegradeplantbiomassandisolatedpolysaccharides.Results:Large-scalescreeningidentifiedarangeofhydrolyticactivitiesamong348uniqueisolatesrepresenting156speciesofplantpathogenicandnon-pathogenicfungi.Hierarchicalclusteringwasusedtoidentifygroupsofspecieswithsimilarhydrolyticprofiles.Amongmoderatelyandhighlyactivespecies,plantpathogenicspecieswerefoundtobemoreactivethannon-pathogensonsixofeightsubstratestested,withnosignificantdifferenceseenontheothertwosubstrates.Amongthepathogenicfungi,greaterhydrolysiswasseenwhentheyweretestedonbiomassandhemicellulosederivedfromtheirhostplants(commelinoidmonocotordicot).AlthoughT.reeseihasahydrolyticprofilethatishighlyactiveoncelluloseandpretreatedbiomass,itwaslessactivethansomenaturalisolatesoffungiwhentestedonxylansanduntreatedbiomass.Conclusions:Severalhighlyactiveisolatesofplantpathogenicfungiwereidentified,particularlywhentestedonxylansanduntreatedbiomass.Therewerestatisticallysignificantpreferencesforbiomasstypereflectingthemonocotordicothostpreferenceofthepathogentested.Thesehighlyactivefungiarepromisingtargetsforidentificationandcharacterizationofnovelcellwalldegradingenzymesforindustrialapplications.
CompletegenomeofanewFirmicutesspeciesbelongingtothedominanthumancolonicmicrobiota(‘Ruminococcusbicirculans’)revealstwochromosomesandaselectivecapacitytoutilizeplantglucans.
Wegmann,U.,Louis,P.,Goesmann,A.,Henrissat,B.,Duncan,S.H.&Flint,H.J.(2014).EnvironmentalMicroBIOLOGy,16(9),2879–2890.
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Therecentlyisolatedbacterialstrain80/3representsoneofthemostabundant16SrRNAphylotypesdetectedinthehealthyhumanlargeintestineandbelongstotheRuminococcaceaefamilyofFirmicutes.Thecompletedgenomesequencereportedhereisthefirstforamemberofthisimportantfamilyofbacteriafromthehumancolon.Thegenomecomprisestwolargechromosomesof2.24and0.73Mbp,leadingustoproposethenameRuminococcusbicirculansforthisnewspecies.Analysisofthecarbohydrateactiveenzymecomplementsuggestsanabilitytoutilizecertainhemicelluloses,especiallyβ-glucansandxyloglucan,forgrowththatwasconfirmedexperimentally.Theenzymaticmachineryenablingthedegradationofcelluloseandxylanbyrelatedcellulolyticruminococciishoweverlackinginthisspecies.Whilethegenomeindicatedthecapacitytosynthesizepurines,pyrimidinesandall20aminoacids,onlygenesforthesynthesisofnicotinate,NAD+,NADP+andcoenzymeAweredetectedamongtheessentialvitaminsandco-factors,resultinginmultiplegrowthrequirements.Invivo,thesegrowthfactorsmustbesuppliedfromthediet,hostorothergutmicroorganisms.OtherfeaturesofecologicalinterestincludetwotypeIVpilins,multipleextracytoplasmicfunction-sigmafactors,aureaseandabilesalthydrolase.
Synergismbetweencucumberα-expansin,fungalendoglucanaseandpectinlyase.
Wei,W.,Yang,C.,Luo,J.,Lu,C.,Wu,Y.&Yuan,S.(2010).JournalofPlantPhysiology,167(14),1204-1210.
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Severalrecombinantfungalenzymes(endoglucanaseandpectinase)werestudiedfortheirinteractionswithα-expansinincellwallextensionandpolysaccharidedegradation.BothCel12AandCel5AwereabletohydrolyzecelluloseCMC-Naandmixed-linkageβ-glucan.IncontrasttoCel5A,Cel12Acouldalsohydrolyzexyloglucanandinducewallextensionofcucumberhypocotylsinaninvitroassay.Combiningα-expansin,evenathighconcentrations,withCel12Adidnotenhancethemaximum/finalwallextensionrateinducedbyCel12Aalone.Theseresultsstronglysuggestthatmodification/degradationofthexyloglucanmolecule/networkisthekeyforcellwallextension,andα-expansinandCel12Amaysharethesameactingsiteinthesubstrate.Pectinase(Pel1,apectinlyase)enhancedα-expansin-inducedwallextensioninaconcentration-dependentmanner,suggestingthatthepectinnetworkmaynormallyregulateaccessibilityofexpansintothexyloglucan–cellulosecomplex.α-ExpansinenhancedCel12A"shydrolyticactivityoncelluloseCMC-Nabutnotonxyloglucanandβ-glucan.ExpansindidnotaffectCel5A"shydrolyticactivity.Interestingly,expansinalsoenhancedPel1"sactivityondegradinghighesterifiedpectin.Apotentialexplanationforwhyexpansincouldsynergisticallyinteractwithonlycertainenzymesonspecificpolysaccharidesisdiscussed.Additionalresultsalsosuggestedthatcellwallswellingmaynotbeasignificanteventduringtheactionofexpansinandhydrolases.
Arevisedarchitectureofprimarycellwallsbasedonbiomechanicalchangesinducedbysubstrate-specificendoglucanases.
Park,Y.B.&Cosgrove,D.J.(2012).PlantPhysiology,158(4),1933-1943.
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Xyloglucaniswidelybelievedtofunctionasatetherbetweencellulosemicrofibrilsintheprimarycellwall,limitingcellenlargementbyrestrictingtheabilityofmicrofibrilstoseparatelaterally.Totestthebiomechanicalpredictionsofthis“tetherednetwork”model,weassessedtheabilityofcucumber(Cucumissativus)hypocotylwallstoundergocreep(long-term,irreversibleextension)inresponsetothreefamily-12endo-β-1,4-glucanasesthatcanspecificallyhydrolyzexyloglucan,cellulose,orboth.Xyloglucan-specificendoglucanase(XEGfromAspergillusaculeatus)failedtoinducecellwallcreep,whereasanendoglucanasethathydrolyzesbothxyloglucanandcellulose(Cel12AfromHypocreajecorina)inducedahighcreeprate.Acellulose-specificendoglucanase(CEGfromAspergillusniger)didnotcausecellwallcreep,eitherbyitselforincombinationwithXEG.Testswithadditionalenzymes,includingafamily-5endoglucanase,confirmedtheconclusionthattocausecreep,endoglucanasesmustcutbothxyloglucanandcellulose.Similarresultswereobtainedwithmeasurementsofelasticandplasticcompliance.BothXEGandCel12Ahydrolyzedxyloglucaninintactwalls,butCel12AcouldhydrolyzeaminorxyloglucancompartmentrecalcitranttoXEGdigestion.XyloglucaninvolvementintheseenzymeresponseswasconfirmedbyexperimentswithArabidopsis(Arabidopsisthaliana)hypocotyls,whereCel12Ainducedcreepinwild-typebutnotinxyloglucan-deficient(xxt1/xxt2)walls.Ourresultsareincompatiblewiththecommondepictionofxyloglucanasaload-bearingtetherspanningthe20-to40-nmspacingbetweencellulosemicrofibrils,buttheydoimplicateaminorxyloglucancomponentinwallmechanics.Thestructurallyimportantxyloglucanmaybelocatedinlimitedregionsoftightcontactbetweenmicrofibrils.
Structuralbasisforentropy-drivencellulosebindingbyatype-Acellulose-bindingmodule(CBM)andbacterialexpansin.
Georgelis,N.,Yennawar,N.H.&Cosgrove,D.J.(2012).ProceedingsoftheNationalAcademyofSciences,109(37),14830-14835.
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Componentsofmodularcellulases,type-Acellulose-bindingmodules(CBMs)bindtocrystallinecelluloseandenhanceenzymeeffectiveness,butstructuraldetailsoftheinteractionareuncertain.WeanalyzedcellulosebindingbyEXLX1,abacterialexpansinwithabilitytoloosenplantcellwallsandwhosedomainD2hastype-ACBMcharacteristics.EXLX1stronglybindstocrystallinecelluloseviaD2,whereasitsaffinityforsolublecellooligosaccharidesisweak.Calorimetryindicatedcellulosebindingwaslargelyentropicallydriven.WesolvedthecrystalstructuresofEXLX1complexedwithcellulose-likeoligosaccharidestofindthatEXLX1bindstheligandsthroughhydrophobicinteractionsofthreelinearlyarrangedaromaticresiduesinD2.Thecrystalstructuresrevealedauniqueformofligand-mediateddimerization,withtheoligosaccharidesandwichedbetweentwoD2domainsinoppositepolarity.Thisreportclarifiesthemoleculartargetofexpansinandthespecificmolecularinteractionsofatype-ACBMwithcellulose.
Biochemicalandmolecularcharacterizationofsecretedα-xylosidasefromAspergillusniger.
Scott-Craig,J.S.,Borrusch,M.S.,Banerjee,G.,Harvey,C.M.&Walton,J.D.(2011).JournalofBiologicalChemistry,286(50),42848-42854.
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α-Linkedxyloseisamajorcomponentofxyloglucansinthecellwallsofhigherplants.Anα-xylosidase(AxlA)waspurifiedfromacommercialenzymepreparationfromAspergillusniger,andtheencodinggenewasidentified.Theproteinisamemberofglycosylhydrolasefamily31.Itwasactiveonp-nitrophenyl-α-D-xyloside,isoprimeverose,xyloglucanheptasaccharide(XXXG),andtamarindxyloglucan.WhenexpressedinPichiapastoris,AxlAhadactivitycomparabletothenativeenzymeonpNPα-XandIPdespiteapparenthyperglycosylation.ThepHoptimumofAxlAwasbetween3.0and4.0.AxlAtogetherwithβ-glucosidasedepolymerizedxyloglucanheptasaccharide.AcombinationofAxlA,β-glucosidase,xyloglucanase,andβ-glucosidaseintheoptimalproportionsof51:5:19:25or59:5:11:25couldcompletelydepolymerizetamarindXGtofreeGlcorXyl,respectively.Tothebestofourknowledge,thisisthefirstcharacterizationofasecretedmicrobialα-xylosidase.Secretedα-xylosidasesappeartoberareinnature,beingabsentfromothertestedcommercialenzymemixturesandfromthegenomesofmostfilamentousfungi.
RestorationofmatureetiolatedcucumberhypocotylcellwallsusceptibilitytoexpansinbypretreatmentwithfungalpectinasesandEGTAinvitro.
Zhao,Q.,Yuan,S.,Wang,X.,Zhang,Y.,Zhu,H.&Lu,C.(2008).PlantPhysiology,147(4),1874-1885.
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Matureplantcellwallslosetheirabilitytoexpandandbecomeunresponsivetoexpansin.Thisphenomenonisbelievedtobeduetocross-linkingofhemicellulose,pectin,orphenolicgroupsinthewall.Byscreeningvarioushydrolyticenzymes,wefoundthatpretreatmentofnongrowing,heat-inactivated,basalcucumber(Cucumissativus)hypocotylswithpectinlyase(Pel1)fromAspergillusjaponicuscouldrestorereconstitutedexogenousexpansin-inducedextensioninmaturecellwallsinvitro.RecombinantpectatelyaseA(PelA)andpolygalacturonase(PG)fromAspergillusspp.exhibitedsimilarcapacitytoPel1.Pel1,PelA,andPGalsoenhancedthereconstitutedexpansin-inducedextensionoftheapical(elongating)segmentsofcucumberhypocotyls.However,theeffectiveconcentrationsofPelAandPGforenhancingthereconstitutedexpansin-inducedextensionweregreaterintheapicalsegmentsthaninthebasalsegments,whereasPel1behavedintheoppositemanner.Thesedataareconsistentwithdistributionofmoremethyl-esterifiedpectinincellwallsoftheapicalsegmentsandlessesterifiedpectininthebasalsegments.Associatedwiththedegreeofesterificationofpectin,morecalciumwasfoundincellwallsofbasalsegmentscomparedtoapicalsegments.PretreatmentofthecalciumchelatorEGTAcouldalsorestorematurecellwalls"susceptibilitytoexpansinbyremovingcalciumfrommaturecellwalls.Becauserecombinantpectinasesdonothydrolyzeotherwallpolysaccharides,andendoglucanase,xylanase,andproteasecannotrestorethematurewall"sextensibility,wecanconcludethatthepectinnetwork,especiallycalcium-pectatebridges,maybetheprimaryfactorthatdeterminescucumberhypocotylmaturecellwalls"unresponsivenesstoexpansin.
CottonfibercellwallsofGossypiumhirsutumandGossypiumbarbadensehavedifferencesrelatedtoloosely-boundxyloglucan.
Avci,U.,Pattathil,S.,Singh,B.,Brown,V.L.,Hahn,M.G.&Haigler,C.H.(2013).PloSone,8(2),e56315.
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Cottonfiberisanimportantnaturaltextilefiberduetoitsexceptionallengthandthickness.Thesepropertiesariselargelythroughprimaryandsecondarycellwallsynthesis.Thecottonfiberofcommerceisacellulosicsecondarywallsurroundedbyathincuticulatedprimarywall,buttherewereonlysparsedetailsavailableaboutthepolysaccharidesinthefibercellwallofanycottonspecies.Inaddition,Gossypiumhirsutum(Gh)fiberwasknowntohaveanadhesivecottonfibermiddlelamella(CFML)thatjoinsadjacentfibersintotissue-likebundles,butitwasunknownwhetheraCFMLexistedinothercommerciallyimportantcottonfibers.WecomparedthecellwallchemistryoverthetimecourseoffiberdevelopmentinGhandGossypiumbarbadense(Gb),thetwomostimportantcommercialcottonspecies,whenplantsweregrowninparallelinahighlycontrolledgreenhouse.Underthesegrowingconditions,therateofearlyfiberelongationandthetimeofonsetofsecondarywalldepositionweresimilarinfibersofthetwospecies,butasexpectedtheGbfiberhadaprolongedelongationperiodanddevelopedhigherqualitycomparedtoGhfiber.TheGbfibershadaCFML,butitwasnotdirectlyrequiredforfiberelongationbecauseGbfibercontinuedtoelongaterapidlyafterCFMLhydrolysis.Forbothspecies,fiberatsevenageswasextractedwithfourincreasinglystrongsolvents,followedbyanalysisofcellwallmatrixpolysaccharideepitopesusingantibody-basedGlycomeProfiling.Togetherwithimmunohistochemistryoffibercross-sections,thedatashowthattheCFMLofGbfibercontainedlowerlevelsofxyloglucancomparedtoGhfiber.Xyloglucanendo-hydrolaseactivitywasalsohigherinGbfiber.Ingeneral,thedataprovidearichpictureofthesimilaritiesanddifferencesinthecellwallstructureofthetwomostimportantcommercialcottonspecies.
Roleof(1,3)(1,4)β-glucanincellwalls:Interactionwithcellulose.
Kiemle,S.N.,Zhang,X.,Esker,A.R.,Toriz,G.,Gatenholm,P.&Cosgrove,D.J.(2014).Biomacromolecules,15(5),1727-1736.
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(1,3)(1,4)-β-D-Glucan(mixed-linkageglucanorMLG),acharacteristichemicelluloseinprimarycellwallsofgrasses,wasinvestigatedtodeterminebothitsroleincellwallsanditsinteractionwithcelluloseandothercellwallpolysaccharidesinvitro.BindingisothermsshowedthatMLGadsorptionontomicrocrystallinecelluloseisslow,irreversible,andtemperature-dependent.MeasurementsusingquartzcrystalmicrobalancewithdissipationmonitoringshowedthatMLGadsorbedirreversiblyontoamorphousregeneratedcellulose,formingathickhydrogel.Oligosaccharideprofilingusingendo-(1,3)(1,4)-β-glucanaseindicatedthattherewasnodifferenceinthefrequencyanddistributionof(1,3)and(1,4)linksinboundandunboundMLG.ThebindingofMLGtocellulosewasreducedifthecellulosesampleswerefirsttreatedwithcertaincellwallpolysaccharides,suchasxyloglucanandglucuronoarabinoxylan.ThetetheringfunctionofMLGincellwallswastestedbyapplyingendo-(1,3)(1,4)-β-glucanasetowallsamplesinaconstantforceextensometer.Cellwallextensionwasnotinduced,whichindicatesthatenzyme-accessibleMLGdoesnottethercellulosefibrilsintoaload-bearingnetwork.
Cellseparationinkiwifruitwithoutdevelopmentofaspecialiseddetachmentzone.
Prakash,R.,Hallett,I.C.,Wong,S.F.,Johnston,S.L.,O’Donoghue,E.M.,McAtee,P.A.,Seal,A.G.,Atkinson,R.G.&Schröder,R.(2017).BMCPlantBiology,17(1),86.
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Background:Unlikeinabscissionordehiscence,fruitofkiwifruitActinidiaerianthadeveloptheabilityforpeeldetachmentwhentheyareripeandsoftintheabsenceofamorphologicallyidentifiableabscissionzone.Twoclosely-relatedgenotypeswithcontrastingdetachmentbehaviourhavebeenidentified.The‘good-peeling’genotypehasdetachmentwithcleandebondingofcells,andapeeltissuethatdoesnottear.The‘poor-peeling’genotypehaspoordetachability,withcellsthatruptureupondebonding,andpeeltissuethatfragmentseasily.Results:Structuralstudiesindicatedthatpeeldetachabilityinbothgenotypesoccurredintheouterpericarpbeneaththehypodermis.Immunolabellingshoweddifferencesinmethylesterificationofpectin,wheretheinterfaceoflabellingcoincidedwiththelocationofdetachmentinthegood-peelinggenotype,whereasinthepoor-peelinggenotype,nosuchinterfaceexisted.Thiszoneofdifferenceinmethylesterificationwasenhancedbydifferentialcellwallchangesbetweenthepeelandouterpericarptissue.Althoughbothgenotypesexpressedtwopolygalacturonasegenes,noenzymeactivitywasdetectedinthegood-peelinggenotype,suggestinglimitedpectinbreakdown,keepingcellwallsstrongwithouttearingorfragmentationofthepeelandfleshupondetachment.Differencesinlocationandamountsofwall-stiffeninggalactaninthepeelofthegood-peelinggenotypepossiblycontributedtothisphenotype.Hemicellulose-actingtransglycosylasesweremoreactiveinthegood-peelinggenotype,suggestinganinfluenceonpeelflexibilitybyremodellingtheirsubstratesduringdevelopmentofdetachability.Highxyloglucanaseactivityinthepeelofthegood-peelinggenotypemaycontributebyhavingastrengtheningeffectonthecellulose-xyloglucannetwork.Conclusions:InfruitofA.eriantha, peeldetachabilityisduetotheestablishmentofazoneofdiscontinuitycreatedbydifferentialcellwallchangesinpeelandouterpericarptissuesthatleadtochangesinmechanicalpropertiesofthepeel.Duringripening,thepeelbecomesflexibleandthecellscontinuetoadherestronglytoeachother,preventingbreakage,whereastheunderlyingouterpericarplosescellwallstrengthassofteningproceeds.Togethertheseresultsrevealanovelandinterestingmechanismforenablingcellseparation.
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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