Megazyme/Azo-CM-Cellulose (Powder)/S-ACMC/4 grams
商品编号：
S-ACMC
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Megazyme INC
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¥3864.00
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2318.40
产品分类：
反应底物
公司分类：
Reaction_substrate
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3392242852
电话号码：
4000-520-616
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info@ebiomall.com
商品介绍
Highpuritydyed,solubleAzo-CM-Celluloseforthemeasurementofenzymeactivity,forresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Substrateforthespecificmeasurementofendo-1,4-β-D-glucanase(cellulase).
Newchromogenicsubstratesfortheassayofalpha-amylaseand(1→4)-β-D-glucanase.
McCleary,B.V.(1980).CarbohydrateResearch,86(1),97-104.
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Newchromogenicsubstrateshavebeendevelopedforthequantitativeassayofalpha-amylaseand(1→4)-β-D-glucanase.Thesewerepreparedbychemicallymodifyingamyloseorcellulosebeforedyeing,toincreasesolubility.Afterdyeing,thesubstrateswereeithersolubleorcouldbereADIlydispersedtoformfine,gelatinoussUSPensions.Assaysbasedontheuseofthesesubstratesaresensitiveandhighlyspecificforeitheralpha-amylaseor(1→4)-β-D-glucanase.Themethodofpreparationcanalsobeappliedtoobtainsubstratesforotherendo-hydrolases.
Evaluationofsubstratecompositionforlignocellulolyticenzymesproductionbysolidstatefermentationfromwastesofoliveoilandwineindustries.
Salgado,J.M.,Moreira,C.,Abrunhosa,L.,Venâncio,A.,Domínguez,J.M.&Belo,I.(2012).AmericanprogrammeforScience,TechnologyandDevelopment,95-101.
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Wastesfromoliveoilandwineindustries(asexhaustedgrapemark,vineshoottrimmings,two-phaseolivemillwaste,vinassesandolivemillwastewaterwereevaluatedforlignocellulolyticenzymesproduction(ascellulases,xylanasesandferuloylesterases)bysolidstatefermentationwithAspergillusniger,AspergillusibericusandAspergillusjaponicus.TostudytheeffectofdifferentsubstratesinenzymesproductionaPlackett-Burmanexperimentaldesignwaspresented.Thevariablesthathadahigherpositiveeffectinlignocellulolyticenzymeswereurea,timeandexhaustedgrapemark.Themixtureoftwo-phaseolivemillwastewithexhaustedgrapemarkandvineshoottrimmingshadmaximaactivityofcellulases,xylanasesandferuloylesterases.
CellulolyticpotentialofThermophilicspeciesfromfourfungalorders.
Busk,P.K.&Lange.L.(2013).AMBExpress,3(1),47.
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ElucidationoffungalbiomassdegradationisimportantforunderstandingtheturnoverofBIOLOGicalmaterialsinnatureandhasimportantimplicationsforindustrialbiomassconversion.Inrecentyearstherehasbeenanincreasinginterestinelucidatingthebiologicalroleofthermophilicfungiandincharacterizationoftheirindustriallyusefulenzymes.Inthepresentstudyweinvestigatedthecellulolyticpotentialof16thermophilicfungifromthethreeascomyceteordersSordariales,EurotialesandOnygenalesandfromthezygomyceteorderMucoralesthuscoveringallfungalordersthatincludethermophiles.Thermophilicfungiaretheonlydescribedeukaryotesthatcangrowattemperaturesabove45°C.All16fungiwereabletogrowoncrystallinecellulosebuttheirsecretedenzymesshowedwidelydifferentcellulolyticactivities,pHoptimaandthermostABIlities.Interestingly,incontrasttopreviousreports,wefoundthatsomefungisuchasMelanocarpusalbomycesreadilygrewoncrystallinecelluloseandproducedcellulases.Theseresultsindicatethattherearelargedifferencesinthecellulolyticpotentialofdifferentisolatesofthesamespecies.Furthermore,alltheselectedspecieswereabletodegradecellulosebutthedifferencesincellulolyticpotentialandthermostabilityofthesecretomedidnotcorrelatetothetaxonomicposition.PCRamplificationandsequencingof22cellulasegenesfromthefungishowedthatthelevelofthermostabilityofthecellulose-degradingactivitycouldnotbeinferredfromthephylogeneticrelationshipofthecellulases.
TranscriptionalcomparisonofthefilamentousfungusNeurosporacrassagrowingonthreemajormonosaccharidesD-glucose,D-xyloseandandL-arabinose.
Li,J.,Lin,L.,Li.H.,Tian,C.&Ma,Y.(2014).BiotechnologyforBiofuels,7(1),31.
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Background:D-glucose,D-xyloseandL-arabinosearethethreemajormonosaccharidesinplantcellwalls.Completeutilizationofallthreesugarsisstillabottleneckforsecond-generationcellulolyticbioethanolproduction,especiallyforL-arabinose.However,littleisknownaboutgeneexpressionprofilesduringL-arabinoseutilizationinfungiandacomparisonofthegenome-widefungalresponsetothesethreemajormonosaccharideshasnotyetbeenreported.Results:Usingnext-generationsequencingtechnology,wehaveanalyzedthetranscriptomeofN.crassagrownonL-arabinoseversusD-xylose,withD-glucoseasthereference.WefoundthatthegeneexpressionprofilesonL-arabinoseweredramaticallydifferentfromthoseonD-xylose.ItappearsthatL-arabinosecanrewirethefungalcellmetabolicpathwaywidelyandprovoketheexpressionofmanykindsofsugartransporters,hemicellulasegenesandtranscriptionfactors.Incontrast,manyfewergenes,mainlyrelatedtothepentosemetabolicpathway,wereupregulatedonD-xylose.TherewiredmetabolicresponsetoL-arabinosewassignificantlydifferentandwiderthanthatundernocarbonconditions,althoughthecarbonstarvationresponsewasinitiatedonL-arabinose.Threenovelsugartransporterswereidentifiedandcharacterizedfortheirsubstrateshere,includingoneglucosetransporterGLT-1(NCU01633)andtwonovelpentosetransporters,XAT-1(NCU01132),XYT-1(NCU05627).Onetranscriptionfactorassociatedwiththeregulationofhemicellulasegenes,HCR-1(NCU05064)wasalsocharacterizedinthepresentstudy.Conclusions:WeconductedthefirsttranscriptomeanalysisofNeurosporacrassagrownonL-arabinoseandperformedacomparativeanalysiswithcellsgrownonD-xyloseandD-glucose,whichdeepenstheunderstandingoftheutilizationofL-arabinoseandD-xyloseinfilamentousfungi.ThedatasetgeneratedbythisresearchwillbeusefulforminingtargetgenesforD-xyloseandL-arabinoseutilizationengineeringandthenovelsugartransportesidentifiedaregoodtargetsforpentoseuntilizationandbiofuelsproduction.Moreover,hemicellulaseproductionbyfungicouldbeimprovedbymodifyingthehemicellulaseregulatordiscoveredhere.
Relevanceofthelightsignalingmachineryforcellulaseexpressionintrichodermareesei(hypocreajecorina).
Gyalai-Korpos,M.,Nagy,G.,Mareczky,Z.,Schuster,A.,Réczey,K.&Schmoll,M.(2010).BMCResearchNotes,3,330.
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Background:Innature,lightisoneofthemostimportantenvironmentalcuesthatfungiperceiveandinterpret.Itisknownnotonlytoinfluencegrowthandconidiation,butalsocellulasegeneexpression.WethereforestudiedtherelevanceofthemaincomponentsofthelightperceptionmachineryofTrichodermareesei(Hypocreajecorina),ENV1,BLR1andBLR2,forproductionofplantcellwalldegradingenzymesinfermentationsaimedatefficientbiosynthesisofenzymemixturesforbiofuelproduction.Findings:Ourresultsindicatethatdespitecultivationinmostlydarkconditions,allthreecomponentsshowaninfluenceoncellulaseexpression.Whilewefoundtheperformanceoftheenzymemixturesecretedbyadeletionmutantinenv1tobeenhanced,thehighercellulolyticactivityobservedforΔblr2ismainlyduetoanincreasedsecretioncapacityofthisstrain.Δblr1showedenhancedbiomassaccumulation,butduetoitsobviouslylowersecretioncapacitystillwastheleastefficientstraininthisstudy.Conclusions:Weconcludethatwithrespecttoregulationofplantcellwalldegradingenzymes,thebluelightregulatorproteinsareunlikelytoactasacomplex.Theirregulatoryinfluenceoncellulasebiosynthesisinvolvesanalterationofproteinsecretion,whichmaybeduetoadjustmentoftranscriptionorposttranscriptionalregulationofupstreamfactors.Incontrast,theregulatoryfunctionofENV1seemstoinvolveadjustmentofenzymeproportionstoenvironmentalconditions.
DehydrogenaseGRD1RepresentsaNovelComponentoftheCellulaseReguloninTrichodermareesei(Hypocreajecorina).
Schuster,A.,Kubicek,C.P.&Schmoll,M.(2011).AppliedandEnvironmentalMicrobiology,77(13),4553-4563.
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Trichodermareesei(Hypocreajecorina)isnowadaysthemostimportantindustrialproducerofcellulaseandhemicellulaseenzymes,whichareusedforpretreatmentofcellulosicbiomassforbiofuelproduction.Inthisstudy,weintroduceanovelcomponent,GRD1(glucose-ribitoldehydrogenase1),whichshowsenzymaticactivityoncellobioseandpositivelyinfluencescellulasegenetranscription,expression,andextracellularendo-1,4-β-D-glucanaseactivity.grd1isdifferentiallytranscribedupongrowthoncelluloseandtheinductionofcellulasegeneexpressionbysophorose.Thetranscriptionofgrd1iscoregulatedwiththatofcel7a(cbh1)underinducingconditions.GRD1isfurtherinvolvedincarbonsourceutilizationonseveralcarbonsources,suchasthoseinvolvedinlactoseandD-galactosecatabolism,inseveralcasesinalight-dependentmanner.WeconcludethatGRD1representsanovelenhancerofcellulasegeneexpression,whichbycoregulationwiththemajorcellulasemayactviaoptimizationofinducingmechanisms.
Influenceofthecarbonsourceonproductionofcellulases,hemicellulasesandpectinasesbyTrichodermareeseiRutC-30.
Olsson,L.,Christensen,T.M.I.E.,Hansen,K.P.&Palmqvist,E.A.(2003).EnzymeandMicrobialTechnology,33(5),612-619.
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ThegrowthandenzymeproductionbyTrichodermareeseiRutC-30usingdifferentlignocellulosicmaterialsascarbonsourcewereinvestigated.Cellulose,sugarbeetpulpandalkalineextractedsugarbeetpulp(resultinginpartialremovalofhemicellulose,ligninandpectin)ormixturesthereofwereusedascarbonsources.Itwasfoundthatendoglucanaseandendoxylanseactivitieswereproducedthroughoutthecultivations,whereasα-arabinosidasewasinducedlateduringthecultivation.Thehighestamountsofendoglucanse,couldbemeasuredwhenT.reeseiRutC-30wasgrownoncelluloseorcellulosecontainingmixtures.Endoxylanasewasproducedonallsubstrates,butthepresenceofcellulosewasfavourablefortheproduction.Polygalacturonaseactivitycouldbemeasuredathighvaryinglevelsthroughoutthecultivations,exceptduringgrowthoncellulose.Thevaryinglevelsmightoriginatefromtheproductionofdifferentisoenzymesofpolygalacturonase.
Jeongeupianaejangsanensisgen.nov.,sp.nov.,acellulose-degradingbacteriumisolatedfromforestsoilfromNaejangMountaininKorea.
Yoon,J.H.,Choi,J.H.,Kang,S.J.,Choi,N.S.,Lee,J.S.&Song,J.J.(2010).InternationalJournalofSystematicandEvolutionaryMicrobiology,60(3),615-619.
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AGram-stain-negative,motile,rod-shaped,cellulose-degradingbacterialstrain,BIO-TAS4-2T,whichbelongstotheBetaproteobacteria,wasisolatedfromforestsoilfromNaejangMountain,Korea,anditstaxonomicpositionwasinvestigatedbyusingapolyphasicstudy.StrainBIO-TAS4-2TgrewoptimallyatpH7.0–8.0,at30°Candinthepresenceof0–1.0 %(w/v)NaCl.Phylogenetictreesbasedon16SrRNAgenesequencesshowedthatstrainBIO-TAS4-2TclusteredwithmembersofthegeneraAndreprevotia,SilvimonasandDeefgeaofthefamilyNeisseriaceae,withwhichitexhibited16SrRNAgenesequencesimilaritiesof93.5–94.2 %.StrainBIO-TAS4-2TcontainedQ-8asthepredominantubiquinoneandsummedfeature3(C16:1ϖ7cand/oriso-C15:02-OH)andC16:0asthemajorfattyacids.TheDNAG+Ccontentwas63.8mol%.StrainBIO-TAS4-2Tcouldbedifferentiatedfrommembersofphylogeneticallyrelatedgenerabydifferencesinfattyacidcomposition,DNAG+Ccontentandsomephenotypicproperties.Onthebasisofphenotypic,chemotaxonomicandphylogeneticdata,strainBIO-TAS4-2Tisconsideredtorepresentanovelspeciesinanewgenus,forwhichthenameJeongeupianaejangsanensisgen.nov.,sp.nov.isproposed,withBIO-TAS4-2T(=KCTC22633T=CCUG57610T)asthetypestrain.
Regulationofendo-actingglycosylhydrolasesinthehyperthermophilicbacteriumThermotogamaritimagrownonglucan-andmannan-basedpolysaccharides.
Chhabra,S.R.,Shockley,K.R.,Ward,D.E.&Kelly,R.M.(2002).AppliedandEnvironmentalMicrobiology,68(2),545-554.
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ThegenomesequenceofthehyperthermophilicbacteriumThermotogamaritimaencodesanumberofglycosylhydrolases.Manyoftheseenzymeshavebeenshowninvitrotodegradespecificglycosidesthatpresumablyserveascarbonandenergysourcesfortheorganism.However,becauseofthebroadsubstratespecificityofmanyglycosylhydrolases,itisdifficulttodeterminethephysiologicalsubstratepreferencesforspecificenzymesfrombiochemicalinformation.Inthisstudy,T.maritimawasgrownonarangeofpolysaccharides,includingbarleyβ-glucan,carboxymethylcellulose,carobgalactomannan,konjacglucomannan,andpotatostarch.Inallcases,significantgrowthwasobserved,andcelldensitiesreached109cells/ml.Northernblotanalysesrevealeddifferentsubstrate-dependentexpressionpatternsforgenesencodingthevariousendo-actingβ-glycosidases;thesepatternsrangedfromstrongexpressiontonoexpressionundertheconditionstested.Forexample,cel74(TM0305),ageneencodingaputativeβ-specificendoglucananse,wasstronglyexpressedonallsubstratestested,includingstarch,whilenoevidenceofexpressionwasobservedonanysubstrateforlam16(TM0024),xyl10A(TM0061),xyl10B(TM0070),andcel12A(TM1524),whicharegenesthatencodealaminarinase,twoxylanases,andanendoglucanase,respectively.Thecel12B(TM1525)gene,whichencodesanendoglucanase,wasexpressedonlyoncarboxymethylcellulose.Anextracellularmannanaseencodedbyman5(TM1227)wasexpressedoncarobgalactomannanandkonjacglucomannanandtoalesserextentoncarboxymethylcellulose.Anunexpectedresultwasthefindingthatthecel5A(TM1751)andcel5B(TM1752)genes,whichencodeputativeintracellular,β-specificendoglucanases,wereinducedonlywhenT.maritimawasgrownonkonjacglucomannan.Toinvestigatethebiochemicalbasisofthisfinding,therecombinantformsofMan5(Mr,76,900)andCel5A(Mr,37,400)wereexpressedinEscherichiacoliandcharacterized.Man5,aT.maritimaextracellularenzyme,hadameltingtemperatureof99°Candanoptimuntemperatureof90°C,comparedto90and80°C,respectively,fortheintracellularenzymeCel5A.WhileMan5hydrolyzedbothgalactomannanandglucomannan,noactivitywasdetectedonglucansorxylans.Cel5A,however,notonlyhydrolyzedbarleyβ-glucan,carboxymethylcellulose,xyloglucan,andlicheninbutalsohadactivitycomparabletothatofMan5ongalactomannanandhigheractivitythanMan5onglucomannan.ThebiochemicalcharacteristicsofCel5A,thefactthatCel5AwasinducedonlywhenT.maritimawasgrownonglucomannan,andtheintracellularlocalizationofCel5Asuggestthatthephysiologicalroleofthisenzymeincludeshydrolysisofglucomannanoligosaccharidesthataretransportedfollowinginitialhydrolysisbyextracellularglycosidases,suchasMan5.
CellulosedegradationbySulfolobussolfataricusrequiresacell-anchoredendo-β-1-4-glucanase.
Girfoglio,M.,Rossi,M.&Cannio,R.(2012).JournalofBacteriology,194(18),5091–5100.
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Asequenceencodingaputativeextracellularendoglucanase(sso1354)wasidentifiedinthecompletegenomesequenceofSulfolobussolfataricus.Theencodedproteinsharessignaturemotifswithmembersofglycosidehydrolasesfamily12.Afteranunsuccessfulfirstattemptatcloningthefull-lengthcodingsequencesinEscherichiacoli,anactivebutunstablerecombinantenzymelackinga27-residueN-terminalsequencewasgenerated.This27-amino-acidsequenceshowssignificantsimilaritywithcorrespondingregionsinthesugarbindingproteinsAraS,GlcS,andTreSofS.solfataricusthatareresponsIBLeforanchoringthemtotheplasmamembrane.Astrategybasedonaneffectivevector/hostgeneticsystemforSulfolobusandonexpressioncontrolbythepromoteroftheS.solfataricusgenewhichencodestheglucosebindingproteinallowedproductionoftheenzymeinsufficientquantitiesforstudy.Infact,theenzymeexpressedinS.solfataricuswasstableandhighlythermoresistantandshowedoptimalactivityatlowpHandhightemperature.Theproteinwasdetectedmainlyintheplasmamembranefraction,confirmingthestructuralsimilaritytothesugarbindingproteins.TheresultsoftheproteinexpressioninthetwodifferenthostsshowedthattheSSO1354enzymeisendowedwithanendo-β-1-4-glucanaseactivityandspecificallyhydrolyzescellulose.Moreover,italsoshowssignificantbutdistinguishablespecificitytowardseveralothersugarpolymers,suchaslichenan,xylan,debranchedarabinan,pachyman,andcurdlan.
Unravellingthemolecularbasisforlightmodulatedcellulasegeneexpression-theroleofphotoreceptorsinNeurosporacrassa.
Schmoll,M.,Tian,C.,Sun,J.,Tisch,D.&Glass,N.L.(2012).BMCgenomics,13(1),127.
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Background:Lightrepresentsanimportantenvironmentalcue,whichexertsconsiderableinfluenceonthemetabolismoffungi.StudieswiththebiotechnologicalfungalworkhorseTrichodermareesei(Hypocreajecorina)haverevealedaninterconnectionbetweentranscriptionalregulationofcellulolyticenzymesandthelightresponse.Neurosporacrassahasbeenusedasamodelorganismtostudylightandcircadianrhythmbiology.WethereforeinvestigatedwhetherlightalsoregulatestranscriptionalregulationofcellulolyticenzymesinN.crassa.Results:WeshowthattheN.crassaphotoreceptorgeneswc-1,wc-2andvvdareinvolvedinregulationofcellulasegeneexpression,indicatingthatthisphenomenonisconservedamongfilamentousfungi.ThenegativeeffectofVVDonproductionofcellulolyticenzymesistherebyaccomplishedbyitsroleinphotoadaptationandhenceitsfunctioninWhitecollarcomplex(WCC)formation.Incontrast,theinductionofvvdexpressionbytheWCCdoesnotseemtobecrucialinthisprocess.Additionally,wefoundthatWC-1andWC-2notonlyactasacomplex,butalsohaveindividualfunctionsupongrowthoncellulose.Conclusions:Genomewidetranscriptomeanalysisofphotoreceptormutantsandevaluationofresultsbyanalysisofmutantstrainsidentifiedseveralcandidategeneslikelytoplayaroleinlightmodulatedcellulasegeneexpression.Geneswithfunctionsinaminoacidmetabolism,glycogenmetabolism,energysupplyandproteinfoldingareenrichedamonggeneswithdecreasedexpressionlevelsinthewc-1andwc-2mutants.Theabilitytoproperlyrespondtoaminoacidstarvation,i.e.up-regulationofthecrosspathwaycontrolproteincpc-1,wasfoundtobebeneficialforcellulasegeneexpression.OurresultsfurthersuggestacontributionofoxidativedepolymerizationofcellulosetoplantcellwalldegradationinN.crassa.
Characterisationofcellulaseactivityinthedigestivesystemoftheredclawcrayfish(Cheraxquadricarinatus).
Xue,X.M.,Anderson,A.J.,Richardson,N.A.,Anderson,A.J.,Xue,G.P.&Mather,P.B.(1999).Aquaculture,180(3),373-386.
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Endogenouscellulaseactivitywasidentifiedinthegastricfluidanddigestiveglandoftheredclawcrayfish.CellulaseshowedmaximalactivityfrompH4to5andwasstableforupto2hat40°C.Cellulaseactivityinthedigestiveglandwasunaffectedbyantibiotictreatment.Takentogetherthesefindingssuggestasignificantendogenouscomponentforredclawcellulaseactivity.Partialpurificationofcellulaseactivitywasperformedusinganionexchangeandgelfiltrationchromatography.OnemajorandoneminorbandofactivitywereidentifiedsubsequentlybySDS-PAGEandzymography.Themolecularweightofthemajorbandwasestimatedat40kDawhiletheminorbandwasestimatedat30kDa.Redclawcellulaseenzymesdemonstratedbroadsubstratespecificity,hydrolysingpolysaccharidescontainingβ-1,4andmixedβ-1,4andβ-1,3glycosidicbondsbutshowedapreferenceforsolublesubstrates.Hydrolysisproductsofcellodextrinsofvariouslengthsalsoshowedthattheenzymesliberatedfreeglucose.Exposureofredclawtoantibioticsresultedinadramaticdeclineinbacterialpopulationsinthegastriccontents(>90%)butonlya40%declineincellulaseactivity.
Identificationofthermostableβ-xylosidaseactivitiesproducedbyAspergillusbrasiliensisandAspergillusniger.
Pedersen,M.,Lauritzen,H.K.,Frisvad,J.C.&Meyer,A.S.(2007).BiotechnologyLetters,29(5),743-748.
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TwentyAspergillusstrainswereevaluatedforproductionofextracellularcellulolyticandxylanolyticactivities.Aspergillusbrasiliensis,A.nigerandA.japonicasproducedthehighestxylanaseactivitieswiththeA.brasiliensisandA.nigerstrainsproducingthermostableβ-xylosidases.Theβ-xylosidaseactivitiesoftheA.brasiliensisandA.nigerstrainshadsimilartemperatureandpHoptimaat75°CandpH5andretained62%and99%,respectively,oftheseactivitiesover1hat60°C.At75°C,thesevalueswere38and44%,respectively.WhereasA.nigerisawellknownenzymeproducer,thisisthefirstreportofxylanaseandthermostableβ-xylosidaseproductionfromthenewlyidentified,non-ochratoxin-producingspeciesA.brasiliensis.
TheeffectofPleurotusostreatusarabinofuranosidaseanditsevolvedvariantinlignocellulosicbiomassesconversion.
Marcolongo,L.,Ionata,E.,Cara,F.L.,Amore,A.,Giacobbe,S.,Pepe,O.&Faraco,V.(2014).FungalGeneticsandBiology,72,162-167.
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ThefungalarabinofuranosidasefromPleurotusostreatusPoAbfrecombinantlyexpressedinPichiapastorisrPoAbfanditsevolvedvariantrPoAbfF435Y/Y446Fweretestedfortheireffectivenesstoenhancetheenzymaticsaccharificationofthreelignocellulosicbiomasses,namelyArundodonax,corncobsandbrewer’sspentgrains(BSG),afterchemicalorchemical–physicalpretreatment.AlltherawmaterialsweresubjectedtoanalkalinepretreatmentbysoakinginaqueousammoniasolutionwhilstthebiomassfromA.donaxwasalsopretreatedbysteamexplosion.Thecapabilityofthewild-typeandmutantrPoAbftoincreasethefermentablesugarsrecoverywasassessedbyusingtheseenzymesincombinationwithdifferent(hemi)cellulolyticactivities.TheseenzymaticmixtureswereeitherentirelyofcommercialoriginorcontainedthecellulasefromStreptomycessp.G12CelStreprecombinantlyexpressedinEscherichiacoliinsubstitutiontothecommercialcounterparts.TheadditionofthearabinofuranosidasesfromP.ostreatusimprovedthehydrolyticefficiencyofthecommercialenzymaticcocktailsonallthepretreatedbiomasses.ThebestresultswereobtainedusingtherPoAbfevolvedvariantandarerepresentedbyincreasesofthexyloserecoveryupto56.4%.Thesedataclearlyhighlighttheimportantroleoftheaccessoryhemicellulolyticactivitiestooptimizethexylanbioconversionyields.
GrowthandEnzymeProductioninBlueCrabs(Callinectessapidus)FedCelluloseandChitinSupplementedDiets.
Allman,A.L.,Williams,E.P.&Place,A.R.(2017).JournalofShellfishResearch,36(1),283-291.
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Thebluecrab[Callinectessapidus(Rathbun,1896)]isabenthicdecapodwithavarieddiet.Thedietincludesinvertebratesanddetritalmaterialthatcanhaverelativelylargeamountsofchitinandcellulose,bothofwhichcanbedifficulttodigestformanyorganismsandoftenrequiretheaidofspecificbacteriainthegutmicrobiome.Inthisstudy,juvenilebluecrabswerefedanoptimizeddefinedpelleteddietwitha20%replacementofwheatflourfillerwitheitherchitin,cellulose,ora14%/6%mixofboth,followedbyadietswitchtotheopposingingredient.Crabshadincreasinggrowthperformancewithincreasingamountsofcelluloseinthedietversuschitinandhadanadditionalmoltinmostcases.Thisoccurredduringtheinitialphaseandfollowingtheswitch,indicatingthatperformancecanberecovered.Subsequently,celluloseandchitindigestionassayswereusedtoshowthattheforegut,midgut,andhindgutwereallabletosignificantlydigestmorecellulosethanchitinwiththemajorityofactivityintheforegutandmidgut.Implicationsforrearinganddietformulationsaswellastheroleofcelluloseandchitindigestioninthenaturaldietarediscussed.
Conferringcellulose-degradingabilitytoYarrowialipolyticatofacilitateaconsolidatedbioprocessingapproach.
Guo,Z.P.,Duquesne,S.,Bozonnet,S.,Cioci,G.,Nicaud,J.M.,Marty,A.&O’Donohue,M.J.(2017).BiotechnologyforBiofuels,10(1),132.
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Background:Yarrowialipolytica,oneofthemostwidelystudied“nonconventional”oleaginousyeastspecies,isunabletogrowoncellulose.Recently,weidentifiedandoverexpressedtwoendogenousβ-glucosidasesinY.lipolytica,thusenablingthisyeasttousecello-oligosaccharidesasacarbonsourceforgrowth.Usingthisengineeredyeastplatform,wehavenowgonefurthertowardbuildingafullycellulolyticY.lipolyticaforuseinconsolidatedbioprocessingofcellulose.Results:Initially,differentessentialenzymecomponentsofacellulasecocktail(i.e,.cellobiohydrolasesandendoglucanases)wereindividuallyexpressedinY.lipolyticainordertoascertaintheviabilityofthestrategy.Accordingly,theTrichodermareeseiendoglucanaseI(TrEGI)andII(TrEGII)weresecretedasactiveproteinsin Y.lipolytica,withthesecretionyieldofEGIIbeingtwicethatofEGI.CharacterizationofthepurifiedHis-taggedrecombinantEGproteins(rhTrEGs)revealedthatrhTrEGIdisplayedhigherspecificactivitythanrhTrEGIIonbothcellotrioseandinsolublecellulosicsubstrates,suchasAvicel,β-1,3glucan,β-1,4glucan,andPASC.Similarly,cellobiohydrolases,suchasT.reeseiCBHIandII(TrCBHIandII),andtheCBHIfromNeurosporacrassa(NcCBHI)weresuccessfullyexpressedinY.lipolytica. However,theyieldoftheexpressed TrCBHIwaslow,soworkonthiswasnotpursued.Contrastingly,rhNcCBHIwasnotonlywellexpressed,butalsohighlyactiveonPASCandmoreactiveonAvicel(0.11 U/mg)thanwild-type TrCBHI(0.065 U/mg).Therefore,workwaspursuedusingacombinationof NcCBHIand TrCBHII.ThequantificationofenzymelevelsinculturesupernatantsrevealedthattheuseofahybridpromoterinsteadoftheprimarilyusedTEFpromoterprocuredfourandeighttimesmore NcCBHIand TrCBHIIexpressions,respectively.Finally,thecoexpressionofthepreviouslydescribed Y.lipolyticaβ-glucosidases,theCBHII,andEGIandIIfromT.reesei,andtheN.crassaCBHIprocuredanengineered Y.lipolyticastrainthatwasabletogrowbothonmodelcellulosesubstrates,suchashighlycrystallineAvicel,andonindustrialcellulosepulp,suchasthatobtainedusinganorganosolvprocess.Conclusions:A Y.lipolyticastraincoexpressingsixcellulolyticenzymecomponentshasbeensuccessfullydeveloped.Inaddition,theresultspresentedshowhowtherecombinantstraincanbeoptimized,forexample,usingartificialpromoterstotailorexpressionlevels.Mostsignificantly,thisstudyhasprovidedademonstrationofhowthestraincangrowonasampleofindustrialcelluloseassolecarbonsource,thusrevealingthefeasibilityofYarrowia-basedconsolidatedbioprocessfortheproductionoffuelandchemicalprecursors.Further,enzymeandstrainoptimization,coupledtoappropriateprocessdesign,willundoubtedlyleadtomuchbetterperformancesinthefuture.
Immobilizationoftwoendoglucanasesfromdifferentsources.
Sarcina,R.,Giosafatto,C.V.L.,Faraco,V.,Lama,L.,Esposito,M.&Mariniello,L.(2017).InternationalJournalofEnvironment,AgricultureandBiotechnology,2(4),1809-1813.
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Cellulasesareaimportantfamilyofhydrolyticenzymeswhichcatalyzethebondofcelluloseandotherrelatedcello-oligosaccharidederivates.Industrialapplicationsrequireenzymeshighlystableandeconomicallyviableintermsofreusability.Thesecostscanbereducedbyimmobilizingthecellulases,offeringapotentialsolutionthroughenzymerecyclingandeasyrecovery.Thecovalentimmobilizationofenzymesisreportedhere:oneiscommercialcellulasefromAspergillusnigerandotheroneisrecombinantenzyme,namedCelStrepitbecausewasisolatedfromanewcellulolyticstrain,Streptomycessp.G12,.TheoptimalpHforbindingis4.6forbothcellulasesandtheoptimalenzymeconcentrationsare1mg/mLand5mg/mLrespectively.Thesupportforimmobilizationisapoliacrylicmatrix.Experimentscarriedoutinthisworkshowpositiveresultsofenzymeimmobilizationintermsofefficiencyandstabilityandconfirmtheeconomicandbiotechnicaladvantagesofenzymeimmobilizationforawiderangeofindustrialapplications.
ChemicalcharacterizationandimmunomodulatoryactivityofacetylatedpolysaccharidesfromDendrobiumdevonianum.
Deng,Y.,Li,M.,Chen,L.X.,Chen,X.Q.,Lu,J.H.,Zhao,J.&Li,S.P.(2017).CarbohydratePolymers,180,238-245.
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Thechainconformation,chemicalcharactersandimmunomodulatoryactivityofpolysaccharidefromDendrobiumdevonianum(DDP)wereinvestigated.Resultsshowedthatmolecularweights,polydispersityindex,radiusofgyrationsofDDPwere3.99×105 Da,1.27,74.1nm,respectively.Byapplyingthepolymersolutiontheory,theexponent(v)valuesof<>2>z1/2=kMwvwascalculatedas0.38,whichrevealedthatDDPexistedasaglobularshapeinaqueoussolution,andfurtherconfirmedbyAFManalysis.Furthermore,themainmonosaccharidecompositionswereManandGlcwiththeratioof29.61:1.00.Indeed,themainglycosidiclinkageswereβ-1,4-Manp,andsubstitutedwithacetylgroupsatO-2andO-3position.Notably,DDPcouldpromotetheimmunefunctionsofmacrophagesincludingNOreleaseandphagocytosis.Thus,DDPcouldbeexploredasanaturalimmune-stimulatingagentinthehealthandfunctionalfoodareaaswellaspharmaceuticalindustries.
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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