Optimal formulation of peptide and protein pharmaceuticals into efficacious dosage forms to ensure sufficient stability and provide acceptable shelf life is critical. To achieve a stable pharmaceutical drug product, excipients are often added to the protein drug substance. In this study, we investigate recombinant human albumin (rAlbumin) for its ability to prevent or minimize physical and chemical degradation of two allelic variants of the recombinant malaria vaccine candidate, merozoite surface protein 2 (MSP2), in various test formulations. The studies establish that rAlbumin provides protection against MSP-2 losses by: reducing non-specific adsorption, acting as an anti-oxidant, and significantly reducing amyloid-like aggregate formation of the malarial antigen proteins. In all three case models, excipients commonly used for the purpose were also examined. Results indicate rAlbumin performs as well as and often better than the comparators and demonstrates that rAlbumin as an excipient has the capacity to improve: (1) physical stability, including protection against surface adsorption and aggregation; (2) chemical stability, in preventing oxidation.