We have recently described a non-chromatographic, ligand-free approach for antibody (Ab) purification based on specially designed: [Tween-20:bathophenanthroline:Fe2+] aggregates. To assess the potential generality of this approach, a variety of detergents belonging to four nonionic detergent families (Tween, Brij, Triton and Pluronic) have now been studied. All surfactant aggregates lead to high purity of the recovered Abs (>95%, by gel densitometry). Good overall Ab recovery yields were observed with: Tween-20 (80-83%), Brij-O20 (85-87%) and Triton X-100 (87-90%), while Pluronic F-127 was less efficient (42-53%). Of additional importance is the finding that the process can depend on filtration (rather than centrifugation), thereby allowing a continuous purification mode that leads to the recovery of monomeric IgG’s (by DLS) and preservation of Ab specificity (by ELISA). The amphiphilic chelator, bathophenanthroline (batho) is recycled almost quantitatively (95%) by crystallization. Good IgG recovery yields (~80%) are also observed when Ab concentrations are increased from 1 mg/ml to 3-5 mg/mL. Potential advantages of the purification platform for industrial downstream processing of therapeutic monoclonal antibodies (mAbs), are discussed.