In recent years, enzyme immobilization has been presented as a powerful tool for the improvement of enzyme properties such as stability and reusability. However, the type of support material used plays a crucial role in the immobilization process due to the strong effect of these materials on the properties of the produced catalytic system. A large variety of inorganic and organic as well as hybrid and composite materials may be used as stable and efficient supports for biocatalysts. This review provides a general overview of the characteristics and properties of the materials applied for enzyme immobilization. For the purposes of this literature study, support materials are divided into two main groups, called Classic and New materials. The review will be useful in selection of appropriate support materials with tailored properties for the production of highly effective biocatalytic systems for use in various processes.

Grape byproducts were subjected to an extraction process under various different experimental conditions (namely, solvent type, temperature, solvent-to-solid ratio, time contact, and raw material) in order to study the effect of these conditions on the yield of phenolic compounds and the corresponding antiradical activity of extracts. Although the order of decreasing capacity to extract soluble materials was ethanol > methanol > water, methanol was the most selective for extracting phenolic compounds. Temperature and solvent-to-solid ratio were found to have a critical role in extraction efficiency; values of 50 degrees C (between 25 and 50 degrees C) and 1:1 (between 1:1 and 5:1) maximized the antiradical activity of phenolic extracts. In addition, extracts from grape samples previously subjected to distillation reached higher antiradical values in comparison to those coming directly from pressing; in both cases, seed extracts showed better results than those of stem when ethanol or water was employed, whereas the opposite occurred in the case of methanol. These differences were attributed to the different phenolic compositions of the considered fractions.

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Bioremediation, a biologically mediated transformation or degradation of persistent chemicals into nonhazardous or less-hazardous substances, has been recognized as a key strategy to control levels of pollutants in water and soils. The use of enzymes, notably oxidoreductases such as laccases, tyrosinases, various oxygenases, aromatic dioxygenases, and different peroxidases (all of EC class 1) is receiving significant research attention in this regard. It should be stated that immobilization is emphasized as a powerful tool for enhancement of enzyme activity and stability as well as for protection of the enzyme proteins against negative effects of harsh reaction conditions. As proper selection of support materials for immobilization and their performance is overlooked when it comes to comparing performance of immobilized enzyme in academic studies, this review summarizes the current state of knowledge regarding the materials used for enzyme immobilization of these oxidoreductase enzymes for environmental applications. In the presented study, thorough physicochemical characteristics of the support materials was presented. Moreover, various types of reactions and notably operational modes of enzymatic processes for biodegradation of harmful pollutants are summarized, and future trends in use of immobilized oxidoreductases for environmental applications are discussed. Our goal is to provide an improved foundation on which new technological advancements can be made to achieve efficient enzyme-assisted bioremediation.