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A hyperglycosylated recombinant human interferon-β (rhIFN-β) R27T mutant was established to improve relapsing-remitting multiple sclerosis (RRMS) in our previous study. We focused on the stability of the R27T mutant throughout its production lifetime, including culture, purification, and storage before formulation prior to clinical use. Herein, we address the stability of this protein during optimized culture and purification processes. Additionally, we employed artificial stress conditions during culture and purification to characterize R27T instability. Although, among total R27T, relative native R27T ratio displayed transiently low even under optimized production process, the ratio was recovered by the end of the overall production process, suggesting that culture and purification processes are optimized. Artificial stress during culture and purification processes resulted in degradation of R27T acidic and basic variants, and mismatched disulfide bonds in no-aggregated forms as well as in the aggregated form. The presence of disulfide bond exchange without aggregation in the unfolded/misfolded state could be a novel finding for rhIFN-β products. The results provide meaningful information for the comprehensive evaluation of the stability of the R27T variant.

Stability and Activity of the Hyperglycosylated Human Interferon-β R27T Variant