engleski

The influence of aeration on activity and operational stability of two snake venom amino acid oxidases

Two L-amino acid oxidases from snake venom Crotalus adamanteus and Crotalus atrox were used as catalysts in the biotransformation of L- methionine to 2-oxo-4-methylthiobutyric acid. Catalase was present in all reactions to remove the hydrogen peroxide that evolves in the reaction, to prevent its reaction with an α-keto acid, and potential negative influence on amino acid oxidases. Batch reactor experiments without and with aeration were carried out with the two enzymes. It was found that aeration increases the reaction rate and decreases the time necessary to achieve 100 % L-methionine conversion due to the increase of oxygen concentration in the solution. It was also found that the increase of the air flow rate causes faster enzyme operational stability decay rate. As for L-amino acid oxidase from C. adamanteus is concerned it was found that bubbling did not cause enzyme activity decay, but the concentration of oxygen in the solution. As for L-amino acid oxidase from C. atrox is concerned it was found that the operational stability decay rate constant linearly depends on the air flow rate.

amino acid oxidase ; oxygen ; enzyme stability ; enzyme activity

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