Introduction Chemical reactions occur around, and in, us every second. These chemical reactions can allow for a range of actions to occur, such as decomposition or even moving a muscle. Without these reactions, humans and other animals would not be able to move, digest, and therefore live. All reactions have a certain activation energy that must be reached before the reaction can occur. This activation energy cannot be reached under typical temperatures for many cells (Reese, 2014), so other
Several factors can affect the activity levels of catalase such as pH, temperature and concentration. In this experiment, the goal was to assess the effect of pH on the activity level of catalase. The results showed that pH levels and enzymatic activity are correlated. The purpose of this experiment was to investigate the effects of pH on catalase activity which was done by correlating the height of the bubbles to the amount of enzyme activity. It was hypothesized that the reaction rate of the
Figure 1. Enzymatic activity was measured by adding 200 microliter’s of 100mM citrate buffer at different temperatures to 10 separate tubes with two tubes for each temperature ranging from 4 to 70 degree’s Celsius and 250 microliter’s of 5mM p-nitro phenol phosphate. The solutions were then transferred to a water bath for 5 minutes, and the acid phosphatase enzyme was added at certain intervals (30 seconds) after each addition. Once the solutions were made the group of solutions were analysed in
Hypothesis we had was if you use peroxidase, isoenzymes in different roots and shoots of corn then, the results would not be different. The prediction I had was I will find that roots and shoots have the different banding patterns in a gel. The pattern for cytochrome c that was given to us is positive,the pattern we got from our results was also positive. The cytochrome c did migrate the way we expected it to as you can see in Figure 2 the cytochrome c moved 1.3 cm we expected this result because
Enzymes are essential to all living things. They help break down large molecules known as polymers, that we consume through our food, and turn them into their simplified forms of monomers which are individual molecules. Monomers are the building blocks of our cells, and they provide the energy our bodies need to perform everyday functions, which is harnessed through the help of enzymes. Enzymes are made up of proteins that fold into different shapes depending on how their amino acids are arranged
At normal body temperature proteins called enzymes allow chemical reactions to take place. Chemical reactions would be useless to the body due to the decreased speed if enzymes were not present in the cell. Energy is vital for most chemical reactions to begin. The heat energy from the match can then be used to start other chemical reactions such as burning a candle. Activation energy is the process of chemical reaction needing the energy to commence. To begin a reaction, the enzymes decrease the
Enzyme catalysis and enzyme inhibition are two essential biological mechanisms of organisms. In this experiment, WT-AP and MBP-AP enzyme are reacted with different concentrations of PNPP substrate in SpectrovVis time based assays. From the change in absorbance over time data, and the rates of the reactions are calculated, followed by the determination of the kinetic constants. Then, the MBP-AP assays are repeated with two different concentrations of phosphate inhibitor and the kinetic constants of
Chemical Background Hydrogen peroxide is a by-product of many reactions that occur within the body – however, it is toxic so needs to be broken down. The equation for this decomposition is as follows: 〖2H〗_2 O_2 → 〖2H〗_2 O+ O_2 In the body, this reaction can be catalysed by the enzyme catalase. Catalase is not removed or used up in this reaction, and speeds up the rate of reaction. It is acting as a catalyst. The decomposition can be catalysed by other catalysts, however, and this is the basis of
Other Binding Sites The active site on ACs are not the only place molecules can bind. Beyond the active site lies a Forskolin (FS) binding site. FS is a diterpene molecule that when bound to AC raises cAMP levels.5 FS binds to a hydrophobic pocket on the other side of the groove that the active site sits in. As previously mentioned, FS stimulates AC isoforms 1-8, but AC9 is largely insensitive to its binding, which raises questions as to the evolutionary purpose of this domain being conserved across
By solar photo catalysis using low TiO2 concentrations L. Prieto-Rodriguez et al., constructed the experimental setup to degrade the selected ECs (sulfamethoxazole, flumequine, carbamacepine, 2-hydroxybifenyl and progesterone) as per the figure 6. These laboratory-scale experiments were performed with 20 mg L−1 TiO2 at different light intensities and at 50 mg L−1 TiO2 over the normalized reaction time (t30W). Figure 6: Lab-scale photoreactor, Source: (Prieto-Rodriguez et al., 2012) Collected