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How Ethanol Concentration Affects Catalase Catalysis of Hydrogen Peroxide

Liu et al. | Nov 15, 2021

How Ethanol Concentration Affects Catalase Catalysis of Hydrogen Peroxide

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.

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Banana-based Biofuels for Combating Climate Change: How the Composition of Enzyme Catalyzed Solutions Affects Biofuel Yield

Klein-Hessling Barrientos et al. | May 27, 2020

Banana-based Biofuels for Combating Climate Change: How the Composition of Enzyme Catalyzed Solutions Affects Biofuel Yield

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.

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Assessing the Efficacy of NOX Enzyme Inhibitors as Potential Treatments for Ischemic Stroke in silico

Vinay et al. | Sep 18, 2020

Assessing the Efficacy of NOX Enzyme Inhibitors as Potential Treatments for Ischemic Stroke <i>in silico</i>

Ischemic stroke occurs when blood flow to the brain is interrupted, causing brain damage. This study investigated the effectiveness of different NOX inhibitors as treatments for ischemic stroke in silico. The results help corroborate previous in vivo and in vitro studies in an in silico format, and can be used towards developing drugs to treat ischemic stroke.

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Spectroscopic Kinetic Monitoring and Molecular Dynamics Simulations of Biocatalytic Ester Hydrolysis in Non-Aqueous Solvent

Chen et al. | Dec 20, 2020

Spectroscopic Kinetic Monitoring and Molecular Dynamics Simulations of Biocatalytic Ester Hydrolysis in Non-Aqueous Solvent

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.

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Covalently Entrapping Catalase into Calcium Alginate Worm Pieces Using EDC Carbodiimide as a Crosslinker.

Suresh et al. | Mar 31, 2019

Covalently Entrapping Catalase into Calcium Alginate Worm Pieces Using EDC Carbodiimide as a Crosslinker.

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.

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Assessing CDK5 as a Nanomotor for Chemotactic Drug Delivery

Jiang et al. | Sep 08, 2022

Assessing CDK5 as a Nanomotor for Chemotactic Drug Delivery

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.

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Homology modeling of clinically-relevant rilpivirine-resistant HIV-RT variants identifies novel rilpivirine analogs with retained binding affinity against NNRTI-resistant HIV mutations

Luk et al. | Jan 24, 2022

Homology modeling of clinically-relevant rilpivirine-resistant HIV-RT variants identifies novel rilpivirine analogs with retained binding affinity against NNRTI-resistant HIV mutations

Human immunodeficiency virus (HIV), which affects tens of millions of individuals worldwide, can lead to acquired immunodeficiency syndrome (AIDS). While there is currently no cure for HIV, the development of small molecule antiretroviral agents has greatly improved the prognosis of infected individuals, especially in developed countries. Here, the authors employ homology modeling and molecular docking towards the identification of novel rilpivirine analogs that retain high binding affinity to clinically relevant rilpivirine-resistant mutations of the HIV reverse transcriptase enzyme.

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Mutation of the Catalytic Cysteine in Anopheles gambiae Transglutaminase 3 (AgTG3) Abolishes Plugin Crosslinking Activity without Disrupting Protein Folding Properties

Pham et al. | May 02, 2014

Mutation of the Catalytic Cysteine in <em>Anopheles gambiae</em> Transglutaminase 3 (AgTG3) Abolishes Plugin Crosslinking Activity without Disrupting Protein Folding Properties

Malaria is a major public health issue, especially in developing countries, and vector control is a major facet of malaria eradication efforts. Recently, sterile insect technique (SIT), or the release of sterile mosquitoes into the wild, has shown significant promise as a method of keeping vector populations under control. In this study, the authors investigate the Anopheles gambiae transglutaminase 3 protein (AgT3), which is essential to the mating of the Anopheles mosquito. They show that an active site mutation is able to abolish the activity of the AgT3 enzyme and propose it as a potential target for chemosterilant inhibitors.

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