Abstract
Protein-based drugs have been developed to treat a variety of conditions and assays use immobilized capture proteins for disease detection. Freeze-drying is currently the standard for the preservation of proteins, but this method is expensive and requires lengthy processing times. Anhydrous preservation in a trehalose amorphous solid matrix offers a promising alternative to freeze-drying. Light assisted drying (LAD) is a processing method to create an amorphous trehalose matrix. Proteins suspended in a trehalose solution are dehydrated using near-infrared laser light. The laser radiation accelerates drying and as water is removed the trehalose forms a protective matrix. In this work, LAD samples are characterized to determine the crystallization kinetics of the trehalose after LAD processing and the distribution of amorphous trehalose in the samples. These characteristics influence the long-term stability of the samples. Polarized light imaging revealed that LAD processed samples are stable against crystallization during low-humidity storage at room temperature. Scanning white light interferometry and Raman spectroscopy indicated that trehalose was present across samples in an amorphous form. In addition, differential scanning microcalorimetry was used to measure the thermodynamic characteristics of the protein lysozyme after LAD processing. These results demonstrate that LAD does not change the properties of this protein.