I have modified an affinity chromatography column coated with Protein G to efficiently separate IgGs. Is it possible to elute the bound IgGs by adjusting temperature instead of utilizing elution solvent?
I'd say that to disrupt the affinity interaction you would have to -at least partially- unfold/denature the protein structure, so I think that your suggestion is not possible..
In theory yes if mainly hydrogen bonds exist between protein G and IgG. The problem as you say is that protein structure can be also perturbed. Moreover do not forget that hydrophobic interactions are favored as temperature increases, thus you got to be careful. Do the experiments and share the outcome.