Enzymes are highly specific and efficient biological catalysts whose applicability in biotechnology, pharmacy, and the chemical industry is becoming increasingly important. In recent years, much research has been focused on the development of green and sustainable technologies, where enzymatic catalysis represents a significant alternative to conventional chemical processes. High selectivity, mild operating conditions, and biodegradability enable efficient and environmentally friendly production of various compounds; however, these advantages are often limited by use under non-standard, industrial conditions such as high temperatures, extreme pH values, or the presence of organic solvents, in which enzymes are frequently unstable.
In this thesis, the effects of deep eutectic solvents (DES) were analyzed based on literature data. Over the past decade, DES have been considered a promising alternative to conventional organic solvents in biocatalytic processes. They are defined as mixtures of hydrogen bond acceptors and donors in a specific molar ratio, where strong interactions result in a significant depression of the melting point, which becomes lower than the eutectic temperature of the individual components, leading to the formation of a stable liquid phase. Their structure, classification, preparation, and physicochemical properties—such as viscosity, polarity, and hydrogen-bonding capacity—that influence their applicability were outlined. Special emphasis was placed on the interactions between solvents and enzymes, as these have a significant impact on enzymatic activity, stability, and selectivity under different reaction conditions.
The focus was on the impact of these solvents on the properties of selected industrially relevant enzymes: alcohol dehydrogenase, horseradish peroxidase, laccase, lipase B, cellulase, and β-D-glucosidase. The mechanisms of stabilization or inhibition of these enzymes in the presence of certain DES are described, along with the identification of the most effective solvent systems for their activity. A comparison of studies revealed that the most promising DES often involve combinations of choline chloride with polyols such as glycerol, ethylene glycol, and propylene glycol, particularly in the presence of small amounts of water. Such systems enhance enzymatic activity and prolong stability, highlighting the great potential of DES for further applications in biotechnology and green chemistry.
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