In some studies, the concept of antiplasticization to independently manipulate the α and β relaxations is employed, thus allowing us to differentiate their respective contributions to the stability of freeze-dried proteins. Antiplasticizers refer to molecular or nanoparticulate substances that lead to the increased rate of α relaxation (resulting in a lower glass transition temperature, Tg), negative deviations from volume additivity upon mixing, and an increase in elastic moduli, while concurrently slow down the higher frequency β relaxation process. This contrasts with regular plasticization, where both the α and β relaxations are accelerated upon the addition of a diluent. Antiplasticization has been observed in several polysaccharide mixtures, 145 particularly enriched by water and glycerol. Multiple research studies have demonstrated the antiplasticization of trehalose when combined with glycerol at different concentrations. DES has been used to study the antiplasticization effect of melt-quenched trehalose-glycerol glasses. The dielectric relaxation times with varying amounts of glycerol were measured covering a broad frequency range between 40Hz to 18GHz. A linear proportionality between the relaxation time of a relatively fast dielectric relaxation process and mass fraction of glycerol up to 0.2 below a certain antiplasticization temperature which is 297K in the study. In addition, a linear relationship between protein degradation rates (log𝜏d) and activation energy (Ea) of the βJG relaxation process was derived in more than 100 antiplasticized sugar glass formulations at 23°C. In contrast, no evident correlation was found between protein degradation and (T-Tg), suggesting that faster dynamic processes may be linked directly to the degradation rates. Further, a more quantitative characterization using DES was established and an antiplasticization factor as a ratio of JG relaxation time for the mixture and pure trehalose was used to measure the extent of antiplasticization. 141 This factor is temperature sensitive which is about 1.6 at 293K but less than 1 above 323K. Though most of these DES studies investigated the correlation between the protein stability and antiplasticization effort, they mainly studied the additive-induced sugar antiparticipation and limited studies focused on the protein itself. There are some limitations of DES in protein dynamic characterization. DES serves as a technique with an extremely wide frequency range, but it is often challenging to interpret the data obtained. Moreover, dielectric measurements cannot offer microscopic insights, and distinguishing between relaxation modes associated with proteins and solvents is not straightforward. Sometimes, the correct assignment of spectra in DES is required but challenging to differentiate the relaxation process of water and protein overlap in hydrated lyophilized solids.