Solid proteins immersed in organic solvents represent one class of enzymatic formulations in which structure, properties, and functionality of enzymes may be drastically changed by an organic solvent. Considering the variety of opportunities in use of different nonaqueous media, correct selection of organic environments presents a great challenge to biotechnological scientists and engineers. Such a selection needs the understanding of molecular mechanisms governing the interactions of proteins in nonaqueous media. This understanding should help also in elucidating the mechanisms controlling the conformational stability of the protein macromolecules, protein aggregation in solid state, aging of the protein preparation, and solubility of proteins in nonaqueous media.

Because of the ability to monitor any processes associated with heat evolution, calorimetric methods have a great potential in elucidating interactions in the protein formulations. Thus, the goal of this chapter is to provide calorimetric protocols for examining the interactions occurring in solid proteins immersed in organic solvents. We want to propose here isothermal immersion calorimetry and differential scanning calorimetry (DSC). Fundamentals of calorimetry may be found in ref. 1.

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