Catalysis

In the experiment, it was proven that Tube 13 had the highest enzyme activity condition. The question being asked in this experiment is how does substrate concentration and pH affect enzyme function. It was hypothesized that there will be an optimal condition outside which function is lower. The group predicted that optimal conditions are pH is 7 and substrate concentration is 6 percent. In conclusion, this whole experiment justifies that enzymes are affected by the changes in pH. Where enzymes are

We are investigating the relationship between enzyme’s Digesting speeds in different temperatures. We are going to measure the speed of amylase (Dependent) in different temperatures (Independent). Our goal of this lab is to find out amylase’s digest speed in different temperatures. To accomplish this goal we will need 4 test tubes with amylase and starch in it, water baths/water boiler with will be making the temperature 4, 21, 40, 60 and 100. And iodine to test the amount of leftover starch. We

ROS are unstable free radical species which are very reactive. A free radical is a molecule containing one or more unpaired electrons in its outer shell (Pham-Huy et al., 2008). At high concentrations, they are dangerous because they attack biochemical substances, such as fatty acids, protein, carbohydrates and nucleic acids, and cause damage to them (Maes et al., 2011; Valko et al., 2007). This damage causes change in their structure and function. There are three types of ROS, which include the

Title: The effect of temperature on the activity of catalase Research Question: To what extent does temperature have an effect on the amount of oxygen gas produced in a catalase reaction? Background Information: An enzyme is a globular protein that serves as a catalyst for biochemical reactions. Enzymes lower the activation energy because they stress the bonds in the substrates. A substrate is the reactant. When a substrate locks into the active site of an enzyme, a reaction is then catalyzed

As macromolecular crowding and confinement conditions can modify the structural stability and bioactivity of a soluble enzyme, my proposed work reflects on SLAC25 as a model enzyme encapsulated by biocompatible polymersomes that can offer tunable cell-like environments. Notably, the copper coordination with the active binding site of the protein is an imperative requirement for the enzymatic function, and this structural organization influences its biophysical properties such as stability and dynamics

Trypsin is an enzyme, which is a biochemical catalyst. Enzymes are spectators in reactions, and are usually proteins, though some exceptions exist. Enzymes work by binding to reactant molecules in such a way that the chemical bond-breaking and bond-forming processes take place more readily. Enzymes are classified based on the substrate and its reaction mechanism, substrate are the reactant molecules that enzymes react with. The reaction takes place at what is called an active site

Characterization of enzyme kinetics can provide valuable insights into enzymatic reaction mechanisms. We are often interested in the effects of specific amino acid side chains on catalytic efficiency, or the efficiency of an enzyme with various substrates. In this experiment, we will determine some of the kinetic properties of alkaline phosphatase (PhoA or ALP), an enzyme that is found in nearly all organisms. E. coli PhoA is a periplasmic enzyme that hydrolyzes phosphate monoesters and has a high

Abstract: To properly investigate the optimal temperatures for both bacterial and fungal amylase, it is simplest to do a visual comparison using a visual aide such as iodine. Iodine has chemical properties that, when introduced to starch, turn a dark bluish purple. In short, the iodine test uses this reaction to determine the presence of starch in the reaction. The lighter the color of the solution, the more the starch was broken down by the amylase, and, correspondingly, the darker the color, the

Every enzyme has a temperature range of optimum activity from 30°C to 37°C since the rate of reaction is highest (Meihua Zhaoa, Guangming Zenga, & Danlian Huanga, 2014). The temperature ranges outside the optimum temperature the enzyme peroxidase is rendered inactive and inhibited. It occurs because as the temperature changes (increases and decreases) would supply enough energy to break some of the intramolecular attractions between polar groups (dipole-dipole attractions and Hydrogen bonding) as

The purpose of these series of experiment was successful as seen from the results. The recombinant form of the green fluorescent protein was successfully expressed and purified from E. coli. Though a high yield and purity were not obtained, the qualitative monitoring of the rGFP activity was consistent with the quantitative values obtained. Qualitatively, the elution fraction E2 fluoresced the most when placed under a hand-held UV lamp. Quantitatively, E2 also had the highest activity with 41900