简介:Whenaproteinisencapsulatedintopoly(DL-lactide-co-glycolide)(PLGA)microspheresbymeansofthedouble-emulsionmethod,theharshmicrospheresformationprocessincludingultrasonification,exposuretoanorganicsolventandapolymermaycausethedenaturationoftheprotein.Inthisstudy,weinvestigatedtheenzymaticactivitychangeandtheeffectoftheexcipientsonthestabilityofrecombinanthumanCu,Zn-superoxidedismutase(rhCu,Zn-SOD)duringtheemulsification.ThespecificactivityrecoverywasfoundtobeconcentrationdependentandtheexcipientsinvolvedsuchasPEG600andTween20,andtrehalosewereshowntoincreasethestabilityofrhCu,Zn-SOD.TheproteinstructuralintegritywithinthemicrosphereswasanalyzedbyFTIR.ThestructureofrhCu,Zn-SODwithinPLGAmicrospherescontainingtrehalosewasfoundtobesimilartothatofthenativesolidstate,whereastheproteinencapsulatedduringthepreparationintheabsenceofanyexcipientchangedduetothepossiblehydrophobicinteractionwiththepolymer.Theresultssuggestthatarationalstabilitystrategyforproteintobeencapsulatedintomicrospheresshouldaimatdifferentprocesses.