During formulation development, proteins are commonly lyophilised with sugars to produce dry therapeutic protein products in order to optimise their stability . Using lyophilisation proteins can be dried to yield a lightweight product which can be easily preserved, shipped, and rehydrated . In the lyophilisation process, a solution containing a protein is frozen, and subsequently ice is removed via sublimation, which can expose the protein to various stresses, such as denaturation at the ice surface, localised changes in pH, and the formation of new hydrogen bonds. Thus, lyophilisation requires a suitable organic molecular matrix to stabilise the protein of interest in the absence of protein molecules. The thermodynamic role of the matrix is to prevent degradation and provide stability to the protein while maintaining the native conformation of the protein as ice and bound water molecules are removed . Various studies have shown that non-reducing sugars, such as sucrose and trehalose, and non-ionic surfactants such as polysorbate 80 serve as effective stabilising agents . Additionally, excipients, for example L-arginine, have been used to increase solubility and minimise aggregation during lyophilisation .