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Catalase is a critical enzyme in the human body because it is capable of converting potentially dangerous hydrogen peroxide into water and oxygen. This work asks whether ethanol affects catalase activity, as alcohol consumption has been often linked to hepatitis occurring in the liver, where catalase level is especially high, and ethanol is known to be capable of denaturing proteins. Testing different concentrations of ethanol found that higher concentrations reduced the activity of catalase. This work has important implications on the negative effects of ethanol on metabolism, in which catalase plays an important role, and protein function more broadly.

Catalase is a biocatalyst used to break down toxic hydrogen peroxide into water and oxygen in industries such as cheese and textiles. Improving the efficiency of catalase would help us to make some industrial products, such as cheese, less expensively. The best way to maintain catalase’s conformation, and thus enhance its activity, is to immobilize it. The primary goal of this study was to find a new way of immobilizing catalase.

Here, seeking to better understand the effects of gadolinium-based contrast agents, dyes typically used for MRI scans, the authors evaluated the activity of catalase found in beef liver both with and without gadodiamide when exposed to hydrogen peroxide. They found that gadioamide did not significantly inhibit catalase's activity, attributing this lack of effects to the chelating agent found in gadodiamide.

In this study, locally produced fall and spring honeys were tested to determine whether there was a significant difference in their abilities to limit or prevent bacterial growth of E. coli, S. aureus, P. aeruginosa, and S. epidermidis.