Abstract
AbstractThe effect of high salt concentration and pH on the binding of globular protein to polycation at different molar masses has been investigated by dynamic light scattering (DLS), turbidimetry and electrostatic modeling for the protein. In dilute concentration regime, DLS and pH titrations showed three remarkable pH transitions: pHc, the pH where soluble complexes of bovine serum albumin (BSA) and linear synthetic Polyethylenemine (PEI) are formed, pHc’ presents the end of primary soluble complex and pHφ presents the first appearance of microcoacervate droplets. All pH transitions increase with increasing NaCl concentration. The Adaptive Poisson-Boltzmann Solver (APBS) identify with precision the functional sites at the surface of BSA and shows that the strength of electrostatic interactions depends hugely on the variation of pH and ionic strength. At a very high concentration of salt, no remarkable effect on a mixture formed of a long chain of polycation and globular protein.
Highlights
In this part of work, we studied the electrostatic potential of protein (BSA)
We have investigated the interactions of Bovine Serum Albumin (BSA) with various molar masses of a linear polycation (PEI) versus pH and salt concentration using a dynamic light scattering, turbidimetry and computer simulations
These simulations were used to estimate the influence of pH and salt on the surface charge distributions and on the electrostatic potential of protein
Summary
DLS and pH protein/polyelectrolyte systems have been studied for their titrations showed three remarkable pH transitions: pHc, practical applications in food technology such as protein the pH where soluble complexes of bovine sLeertumF adlebnuomtiena seepldaraatniodn,leint cVreadseinngottheearmvaelcsttoarbisliptyacoer aocvideroFf pwroittehins,nite positive (BSA) and linear synthetic Polyethylenempianier A(P,EAI)∗ aorfediaagnodnastlaizbailbizlaetiFon-lionfefaorammaepmsuolsnioVn,s.eIanchfaoctf,wthheicahddaictitosnon an eigenb formed, pHc’ presents the end of primary soilrurebdleuccoimblpeletrxidiaogf opnoallyefaleschtrioolnyt.eSsuctoh aa psaoilruitsiocnalcleodmapoLseeodnaofrdmpianierr(aslee [13, De n adconrondpcpleeHnttsφr.paAtrielolsnpe.nHtTsthrtaehnesAifdtiiraospnt tsaivpienpcePraeoraiassnsecoweni-otBfhomilntsAizccwm,rroeaAaacpn∗ossniainsAcgSesaroNavnliavaddCeterltAo∗b.pfinoeIarnrsftodeitcoehlldfleii-vssdpeuccrrayoaa.ncsleTewashlsssheiuoneecgsnnh,teacwaavbphneilserizaurteeulhatttethohiroemeensseoeepxrlparpiotashtcrteetisrisdcamoulernrseieassnaucuraetarnopepimsqrauoulolstaereotpi,enuhastsnih.esedAfmumncloaflltehdetehneddou (APBS) identify with precision the functional sTithese alittethraeturaebcuonndtaanitnlsitemraatnuyreepxraomveps ltehsatotfhseeclfh-adruacatleLreoof nthaerpdrpotaeiirns/. For instanc surface of BSA and shows that the strength aotfeedlewctirtohstaanticirrepdoulcyeiblelcetrmoloydteulientfeorracthtioenTseriws iallfifgecetredalgbeybreanvoifrothnme henytpael rcube (see [ interactions depends hugely on the variatLioenonoaf rpdHpaanirdof Kfarcatwortsc,hinoupkarttyicpuela(sr epeH[1a0n,dDieonnicitsitorenn6g.t1h])(;9(-i1i2i)).tIhnedeLeedo,nard pair as ionic strength. Let {θi}di= denotIenatshtiasnpdaapredr,ortdherionbgjeocftitvheeiesigteonvchaaluraecsteorfizAe. Tthheen A, A∗ is s is a standard ordinetreinragctoiof nths ebeetiwgeeennvparlouteesinosfaAnd∗ c(saetieon[7ic, pPorloypeloescittrioolnyte8s.7])
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