ИСТИНА

In the field of biotransformation an optimal dehydration of enzymes might be particularly important to achieve an enzyme active in non-aqueous media. A strategy that has been adopted to prepare enzymes more active in non-aqueous media is the use of lyoprotectants, as proved with some additives as polyethylene glycol, trehalose, sucrose and mannitol. Several infrared spectroscopy studies have shown that these lyoprotectants are useful to preserve the native conformation of proteins during the freeze-drying process. Nevertheless, a better understanding of the role of additives to control protein hydration and flexibility is extremely important for more efficient enzyme applications in non-conventional media. In this presentation it is shown how some lyoprotectants have been employed to prepare enzyme formulations more active in organic solvent (especially hydrolases) or able to preserve enzyme activity in some ionic liquids (e.g., dehydrogenase from Pseudomonas sp.). Furthermore, based on FT/IR and fluorescence data, we speculate some rationale about the mechanism by which some additives might preserve the enzyme functionality in non-aqueous media [1-2]. This work partially supported by grants from Italian National Research Council, prot. n. 421- 09-03-2015 and Russian Foundation for basic research, grant 15-54-78035