Investigation of the effect of Substrate concentration on Catalase activity Research Question: To investigate enzyme kinetics, using catalase enzyme from the yeast extract. Background Information: Enzymes are proteins which catalyze reactions that take place in the body or they increase the rate of the biological reactions. In an enzyme catalyzed reaction, the substrate binds to the active site and forms the enzyme-substrate complex with the enzyme. The enzyme breaks the bonds present in the substrate; the final product of this reaction leaves the enzyme which remains unchanged after the reaction. Catalase is a substance which is produced by the liver to break down hydrogen peroxide.
Date : 18/02/2013 Micro-scale Determination of the Activation Energy of the Hydrogen Peroxide-Iodide Reaction Abstract: The purpose of this experiment was to determine the rate at which hydrogen peroxide decomposes to water and oxygen with the use of an iodide catalyst. Using the logarithmic form of the Arrhenius equation: ln k’ = -Ea/RT + ln A . the activation energy was determined to be 52.3 kJ/mol. It was also found that increasing the temperature also increased the rate, as there was more energy available to increase the speed of the reaction. Introduction: The purpose of this experiment was to determine the Activation Energy of the Hydrogen Peroxide-Iodide reaction.
All living organisms have enzymes. Enzymes are globular proteins that selectively speed up (catalyze) the rates of chemical reactions. In our experiment we used yeast which contains catalase, our enzyme, which will react with our substrate, hydrogen peroxide thus making oxygen gas that we can measure. In our first experiment we examined hot and cold temperatures impact on catalase activity our research question was, ‘what is the relationship between temperature and yeast catalase activity?’ Our hypothesis was: If we test cold and hot temperatures, then colder temperatures will have more catalase activity than hotter temperatures. In our 2nd, we examined the effect of warmer temperature.
Enzymes and temperature As the temperature increases, so does the rate of reaction, but very high temperatures denature enzymes. This graph shows how the rate of reaction changes due to increasing levels of heat. As the graph shows: at roughly 37ºC (body temperature) the rate of reaction starts to fall, and the rate falls rapidly as the enzyme is denatured. Enzymes and pH Like with heat, changes in pH levels can denature an enzyme, different enzymes work best at different pH levels. The pH level where the enzyme works best depends on where it is in the body.
Enzyme Activity Research Question: Does increasing the temperature of 3ml lipase increase the rate of reaction in enzyme-catalyzed reaction? Hypothesis: One of the main conditions that can affect enzyme activity is temperature. The rate of an enzyme-catalyzed reaction increases as the temperature is increased. A 10 degree Celsius rise in temperature will increase the activity of most enzymes by 50-100%. Somewhat, as small as 1-2 degrees Celsius may change to 10-20% in the results of fluctuation in reaction temperature.
The reason for this is because; this allows the substrate to bind to the active site, which is known as the ‘lock and key model’. The substrate is the key and active site is the lock. No other key will fit into the lock. There are many factors that affect the rate of enzyme activity in the liver, namely, Ph level, and substrate concentration. I chose to do an experiment on ‘How temperature can affect the rate of enzyme activity in the liver?’ Temperature affects the “speeds of the molecules, the activation energy of the catalytic reaction and the thermal stability of the enzyme and substrate.” (2) At different levels of temperature the affects on the enzyme in the liver varies.
Effect of Enzyme Activity on Temperature Aim: The aim of this experiment is to investigate how effectively the enzyme amylase breaks down starch at different temperatures Research Question: How does the increase in temperature affect the time taken for amylase to breakdown 2ml of starch? Purpose: Background Information: Enzymes are biological catalysts that comprise the largest and most highly specialized class of protein molecules. Enzymes act as catalysts to increase the rates of chemical reactions. A fundamental property of enzymes is their specificity. Various enzymes have unique shape and chemical composition that creates a site, called and active site.
In the case of α-phase FePO4, cell parameters tend to increase exponentially as temperature increase. The volume of the metal has the tendency to increase exponentially as well. It is governed by thermal expansion coefficient α (K-1)= 2.924 x 10-5 + 2.920 x 10-10 (T-300)2. There are two factors that affect the thermal expansions: 1. Angular variations due to the changes of Fe-O-P bridging angles.
When these factors vary, enzymes may change in shape so it will not be able to bond to the specific substance anymore. What is trypsin? Trypsin is produced in the pancreas as typsinogen originally allowing metabolic control. It is used widely in various biotechnological processes because it is very easy to be purified. Method: Material: • Trypsin • Casein • Water bath (to keep the temperature constant) • Colorimeter (to measure the rate of enzyme activity) • Thermometer • Test Tubes (to contain the casein and the buffer solution) • Stop watch (to control and measure the time) • Distilled water (to mix with trypsin to produce the buffer solution) • Test tube rack (to prevent the tubes rolling and smashing) Protocol: • Put 2.5 cm³ of 5% with reconstituted casein in 6 of the test
Pocholo Panhon Rachel Smith -5 9/29/1999 Enzyme lab conclusion The problem that had was solved by the experiment was whether the pressure of a body was affected by a large amount of H2O2 being absorbed into it. I thought that if the amount of H2O2 (mL) increases then the pressure created by the reaction also increases, because in real life when somebody has a lot of H2O2 absorbed into their bloodstream the blood will start to froth and bubble up and pressure is created from it. To test this hypothesis I used H2O2 solution, blended cow liver, a flask with a pressure sensor hooked up to a laptop, 2 test tube (one for H2O2, and one for the cow liver). For the experiment I put a certain amount of H2O2 in one test tube and 10 mL of cow liver in another, then quickly emptied both contents of the test tubes into the single flask and put on the pressure sensor to figure out how much pressure was created. I did this five times with an amount of H2O2 then changed it by 2 mL higher while keeping the amount of the cow liver the same and continued to do everything else the same.