d-氨基葡萄糖苷酶的失活动力学研究

d-氨基葡萄糖苷酶的失活动力学研究

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时间:2018-07-31

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1、D-氨基葡萄糖苷酶的失活动力学研究,b1.8No.1MarineScienceBulletinMay2006InactivationKineticsof-N-Acetyi-D-GiucosaminidasefromPrawn(Penaeusvannamei)byFormaldehydeXIEXiaolan(谢晓兰)?2SHIYan(~艳),HUANGQiansheng(黄乾生),CHENq~ngrJ(陈清西)1.KeyLaboratoryofMinistryofEducationfo,CellBiologyandTumorCell

2、Engineering,SchoolofLireSciences.XiamenUniversity,Xiamen361005.Fujian,China2,DepartmentofChemistry,QuanzhouNormalUniversity,Quanzhou36201l,Fujian,ChinaAbstract:B-N-Acetyl-D-glucosaminidase(NAGase,EC.3.2.1.52)isacompositionofchitinolyticenzymesanddisintegratedimmerandt

3、rimeroligomersofN-acetyl-B-D-glucosamine(NAG)intomonomer.Prawnvannamei)NAGaseisinvolvedindigestionandmoltingprocesses.Somepollutantsinseawateraffecttheenzymeactivitycausinglossofthebiologicalfunctionoftheenzyme,whichaffectstheexuviatingshellandthreatensthesurvivalofth

4、eanima1.Theeffectofformaldehydeonprawn(vannamei)B,N.acety1.D-glucosaminidaseactivityforthehydrolysisofpNP-NAGhasbeenstudied.Theresultsshowthatformaldehyde,atappropriateconcentrations,CanleadtOreversibleinactivationoftheenzyme,andtheIG0isestimatedtObe1.05mol.L'..Theina

5、ctivationmechanismobtainedfromLineweaver-BurkplotsshowsthattheinactivationoftheenzymebyformaldehydebelongstOthecompetitivetype.Theinactivationkineticsoftheenzymebyformaldehydehasbeenstudiedusingtheprogress?-of-substrate?—reactionmethoddescribedbyTsou.andtherateconstan

6、tshavebeendetermined.Theresultsshowthatk+0ismuchlargerthan,indicatingthefreeenzymemoleculeisfragileintheformaldehydesolution.Keywords:vannamei;B-N-acetyl-D-glucosaminidase;inactivation;kinetics;formaldehydeIntroductionChitin.oneofthemostabundantorganiccompoundsinnatur

7、e,iSastructuralpolysaccharidecomposedofN.acetyl—B—D—glucosamine(NAG)residues.Thepolysaccharide,sometimereferredtoas"animalcellulose".iSamajorcomponentofthecrustaceanexoskeleton.Crustaceangrowthanddevelopmentaleachievedbyecdysis,theperiodicsheddingoftherigidexoskeleton

8、il1.Threechitinolyticenzymes,exo.chitinase,endo—chitinaseandN—acetyl—p—D—glucosaminidase(NAGase,EC3.2.1.52).arenecessaryford

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