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One disadvantage of antibiotic therapy is the potential for unpleasant gastrointestinal side effects. Here, the authors test whether some common antibiotics directly interfere with the digestion of protein, fat, or sugars. This study provides motivation to more carefully investigate the interactions between antibiotics and gut enzymes in order to inform treatment decisions and improve patient outcomes.

Here, recognizing the recognizing the growing threat of non-biodegradable plastic waste, the authors investigated the ability to use a modified enzyme identified in bacteria to decompose polyethylene terephthalate (PET). They used simulations to screen and identify an optimized enzyme based on machine learning models. Ultimately, they identified a potential mutant PETases capable of decomposing PET with improved thermal stability.

The authors investigate whether amylase or yeast had a more prominent role in determining the bioethanol concentration and bioethanol yield of banana samples. They hypothesized that amylase would have the most significant impact on the bioethanol yield and concentration of the samples. They found that while yeast is an essential component for producing bioethanol, the proportion of amylase supplied through a joint amylase-yeast mixture has a more significant impact on the bioethanol yield. This study provides a greater understanding of the mechanisms and implications involved in enzyme-based biofuel production, specifically of those pertaining to amylase and yeast.

Enzyme chemotaxis is a thermodynamic phenomenon in which enzymes move along a substrate concentration gradient towards regions with higher substrate concentrations and can be used to steer nanovehicles towards targets along natural substrate concentrations. In patients with Alzheimer’s disease, a gradient of tau protein forms in the bloodstream. Tau protein is a substrate of the enzyme CDK5, which catalyzes the phosphorylation of tau protein and can travel using chemotaxis along tau protein gradients to increasing concentrations of tau and amyloid-beta proteins. The authors hypothesized that CDK5 would be able to overcome these barriers of Brownian motion and developed a quantitative model using Michaelis-Menten kinetics to define the necessary parameters to confirm and characterize CDK5’s chemotactic behavior to establish its utility in drug delivery and other applications.

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.

This study explores the interaction between precocene II and trichocethecene 3-O-acetyltransferase using molecular docking simulations. Computational analysis identified several potential binding sites on the enzyme surface and predicted favorable ligand-protein interactions involving key residues. These findings provide insight into how precocene II may interact with this enzyme and demonstrate the use of computational approaches to explore potential antifungal mechanisms.

Here the authors performed a comparative analysis to investigate the viability of using PLAY® instead of fetal bovine serum (FBS) as a growth medium to culture cells with an enzyme-linked immunosorbent assay.

Lipases are a common class of enzymes that catalyze the breakdown of lipids. Here the authors characterize the the activity of pancreatic lipase in different organic solvents using a choloremetric assay, as well as using molecular dynamic simulations. They report that the activity of pancreatic lipase in 5% methanol is more than 25% higher than in water, despite enzyme stability being comparable in both solvents. This suggests that, for industrial applications, using pancreatic lipase in 5% methanol solution might increase yield, compared to just water.

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.

In this study, the authors test whether excess copper exposure has neurobehavioral effects on Hirudo verbana leeches.