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HighpuritydyedandcrosslinkedCellazymeCtabletsforthemeasurementofenzymeactivity,forresearch,biochemicalenzymeassaysandinvitrodiagnosticanalysis.
Fortheassayofendo-cellulase.ContainingAZCL-HE-Cellulose.Recommendedsubstratefortheassayofendo-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.
Comparisonofendolytichydrolasesthatdepolymerise1,4-β-D-mannan,1,5-α-L-arABInanand1,4-β-D-galactan.
McCleary,B.V.(1991).“EnzymesinBiomassConversion”,(M.E.HimmelandG.F.Leatham,Eds.),ACSSymposiumSeries460,Chapter34,pp.437-449.AmericanChemicalSociety,Washington.
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Hydrolysisofmannan-typepolysaccharidesbyβ-mannanaseisdependentonsubstitutiononandwithinthemain-chainaswellasthesourceoftheβ-mannanaseemployed.Characterisationofreactionproductscanbeusedtodefinethesub-sitebindingrequirementsoftheenzymesaswellasthefine-structuresofthepolysaccharides.Actionofendo-arabinanaseandendo-galactanaseonarabinansandarabinogalactansisdescribed.Specificassaysforendo-arabinanaseandarabinan(infruit-juiceconcentrates)arereported.
Measurementofpolysaccharidedegradingenzymesusingchromogenicandcolorimetricsubstrates.
McCleary,B.V.(1991).ChemistryinAustralia,58,398-401.
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Enzymicdegradationofcarbohydratesisofmajorsignificanceintheindustrialprocessingofcerealsandfruits.Intheproductionofbeer,barleyisgerminatedunderwelldefinedconditions(malting)toinducemaximumenzymesynthesiswithminimumrespirationofreservecarbohydrates.Thegrainsaredriedandthenextractedwithwaterundercontrolledconditions.Theamylolyticenzymessynthesizedduringmalting,aswellasthosepresentintheoriginalbarley,convertthestarchreservestofermentablesugars.Otherenzymesactonthecellwallpolysaccharides,mixed-linkageβ-glucanandarabinoxylan,reducingtheviscosityandthusaidingfiltration,andreducingthepossibilityofsubsequentprecipitationofpolymericmaterial.Inbaking,β-amylaseandα-amylasegivecontrolleddegradationofstarchtofermentablesugarssoastosustainyeastgrowthandgasproduction.Excessquantitiesofα-amylaseintheflourresultinexcessivedegradationofstarchduringbakingwhichinturngivesastickycrumbtextureandsubsequentproblemswithbreadslicing.Juiceyieldfromfruitpulpissignificantlyimprovedifcell-walldegradingenzymesareusedtodestroythethree-dimensionalstructureandwaterbindingcapacityofthepecticpolysaccharidecomponentsofthecellwalls.Problemsofroutineandreliableassayofcarbohydratedegradingenzymesinthepresenceofhighlevelsofsugarcompoundsareexperiencedwithsuchindustrialprocess.
Optimisingtheresponse.
Acamovic,T.&McCleary,B.V.(1996).FeedMix,4,14-19.
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Afinebalanceexistsbetweenenzymeactivityandtheadverseeffectsassociatedwithfeedprocessing.Accurateestimationofenzymeactivityinthefeedisapre-requisitetooptimisingtheresponse.
Xyr1receivesthelactoseinductionsignalandregulateslactosemetabolisminHypocreajecorina.
Stricker,A.,R.,Steiger,M.,G.&Mach,R.,L.(2007).FEBSLetters,581(21),3915-3920.
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ThisstudyreportsthevitalregulatoryinfluenceofXyr1(xylanaseregulator1)onthetranscriptionofhydrolyticenzyme-encodinggenesandhydrolaseformationonlactoseinHypocreajecorina.Whilethetranscriptionofthexyr1geneitselfisachievedbyreleaseofcarboncataboliterepression,thetranscriptformationofxyr1(xylanase1)isregulatedbyanadditionalinductionmechanismmediatedbylactose.Xyr1hasanimportantimpactonlactosemetabolismbydirectlyactivatingxyr1(xylosereductase1)transcriptionandindirectlyinfluencingtranscriptionofbga1(β-galactosidase1).ThelatterisachievedbyregulatingtheconversionofD-galactosetotheinducingcarbonsourcegalactitol.
Scouringofflaxrovewiththeaidofenzymes.
Ossola,M.&Galante,Y.M.(2004).EnzymeandMicrobialTechnology,34(2),177-186.
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Linenistheyarnorthefabricsmadefromfibresoftheflaxplant(Linumusitatissumum),which,likeotherbastfibrecrops,canbegrowninmoderateclimatesandneedslowinputofagrochemicalstogivehighyields.Beforecottontookoverasthemainplant-derivedtextilematerial,linenwasoneofthemostimportantsourceoftextilefibres.Followingafewdecadesofalmostabandonment,flaxfibresarebeingre-evaluatedthankstotheuniquefeaturesoffreshness,comfortandeleganceoflinenapparels,sheets,towelsandotherhouseholdtextileitems.However,flaxprocessingintoyarnessentiallystillfollowstraditionalmethodologies.Wehavereinvestigatedtheeffectsofseveralwellcharacterized,mostlyrecombinant,industrialenzymesonrawflaxrove(onapilotscalefromfourtimes1kgspoolsupto130kgofmaterial)asanalternativetochemicalscouring,followedbyasinglebleachingstepandbyyarnwetmechanicalspinning.Afterspinning,allrelevantyarnparametersweremeasuredandevaluated(e.g.,resistance,stretching,percentageofneps,etc.).Inthepresentwork,wedemonstratetheadvantagesofscouringwiththeenzymestested,usedundermildreactionconditions,incomparisonwithtraditionalchemicalscouring.Thedecreasingorderofeffectivenesswas:pectinase>xylanase=galactomannanase=protease>lipase>or=laccase.Asimpleandstraightforwardschemeofrovebiopreparationandbleachingisproposed,followedbywetspinningtoyieldahighqualitylinenyarn.
Efficientyeastcell-surfacedisplayofexo-andendo-cellulaseusingtheSED1anchoringregionanditsoriginalpromoter.
Inokuma,K.,Hasunuma,T.&Kondo,A.(2014).BiotechnologyforBiofuels,7(1):8.
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Background:Therecombinantyeaststrainsdisplayingtheheterologouscellulolyticenzymesonthecellsurfaceusingtheglycosylphosphatidylinositol(GPI)anchoringsystemareconsideredpromisingbiocatalystsfordirectconversionoflignocellulosicmaterialstoethanol.However,thecellulolyticactivitiesoftheconventionalcellulase-displayingyeaststrainsareinsufficientforthehydrolysisofcellulose.Inthisstudy,weconstructednovelgenecassettesfortheefficientcelluloseutilizationbycellulase-displayingyeaststrains.Results:Thenovelgenecassettesforthecell-surfacedisplayofAspergillusaculeatusβ-glucosidase(BGL1)andTrichodermareeseiiendoglucanaseII(EGII)wereconstructedusingthepromoterandtheGPIanchoringregionderivedfromSaccharomycescerevisiaeSED1.ThegenecassetteswereintegratedintotheS.cerevisiaegenome,thentheβ-glucosidaseactivityoftheserecombinantstrainswasevaluated.WerevealedthatsimultaneousutilizationoftheSED1promoterandSed1anchoringdomaininagenecassetteenabledhighly-efficientenzymeintegrationintothecellwall.Theβ-glucosidaseactivityofrecombinantyeastcellstransducedwiththenovelgenecassettewas8.4-foldhigherthanthatofaconventionalstrain.ThenovelEGII-displayingstrainalsoachieved106-foldhigherhydrolysisactivityagainstthewater-insolublecellulosethanaconventionalstrain.FurThermore,directethanolproductionfromhydrothermallyprocessedricestrawwasimprovedbythedisplayofT.reeseiiEGIIusingthenovelgenecassette.Conclusions:Wehavedevelopednovelgenecassettesfortheefficientcell-surfacedisplayofexo-andendo-typecellulolyticenzymes.Theresultssuggestthatthisgenecassettehasthewideapplicabilityforcell-surfacedisplayandthatcellulase-displayingyeastshavesignificantpotentialforcost-effectivebioethanolproductionfromlignocellulosicbiomass.
