Objectives: Most antiviral vaccines are created by inactivating the virus using chemical methods. The inactivation and production of viral vaccine preparations after the irradiation of viruses with accelerated electrons has a number of significant advantages. Determining the integrity of the genome of the resulting viral particles is necessary to assess the quality and degree of inactivation after irradiation.
View Article and Find Full Text PDFBackground/aim: Enzymatic anticancer therapies are actively investigated as they can selectively deprive cancer cells of essential nutrients. L-lysine-α-oxidases of different origins have been reported as potential anticancer enzymes with a significant antitumor potency. This study aimed to evaluate the cytotoxic and antitumor activity of L-lysine-α-oxidase obtained from the domestic strain of Rifai VKPM F-180.
View Article and Find Full Text PDFL-asparaginase (L-ASNase) is a key industrial enzyme significant for cancer therapy and the food industry for reducing dietary acrylamide. The hyperthermophilic L-ASNase from (TsAI) was previously shown to exhibit high activity and thermostability and is promising for biotechnology. To gain insights into structure-functional relationships of TsAI, determination of the substrate specificity, kinetic parameters, structural characterization, and molecular docking were performed.
View Article and Find Full Text PDFThe Maillard reaction is a network of interconnected interactions yielding in formation a number of toxic derivatives in processed foods. Acrylamide, a potential carcinogen and a product of the Maillard reaction, is formed under food processing, predominantly from asparagine and reducing sugars at temperatures over 120 °C. In this study, we investigated the potency of recombinant hyperthermophilic L-asparaginase from TsAI to mitigate dietary acrylamide by hydrolyzing substrate for its synthesis under various operation conditions.
View Article and Find Full Text PDFLow-frequency electromagnetic fields, induced by alternating current (AC)-based equipment such as transformers, are known to influence the physicochemical properties and function of enzymes, including their catalytic activity. Herein, we have investigated how incubation near a 50 Hz AC autotransformer influences the physicochemical properties of horseradish peroxidase (HRP), by atomic force microscopy (AFM) and spectrophotometry. We found that a half-hour-long incubation of the enzyme above the coil of a loaded autotransformer promoted the adsorption of the monomeric form of HRP on mica, enhancing the number of adsorbed enzyme particles by two orders of magnitude in comparison with the control sample.
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