DESCRIPTIVE TITLE
The Effect of Different Amounts of Sodium Chloride on the displacement of oxygen.
INTRODUCTION
The dependability of the rate of an enzyme-mediated reaction is based on two factors: the substrate concentration and the concentration and action of the enzyme that catalyzes the reaction (Vander, et. al., 2001). Enzymes are catalysts that produce chemical reactions in cells. Enzymes which are large proteins perform a reaction which acts upon a substance known as a substrate. When combined, the substrate bonds to the active site on the enzyme creating an enzyme-substrate complex. It is from this complex that specific products are created.
Sodium Chloride is a compound known commonly as table salt. This compound is used for many things, including food flavoring, a means of preservation and to aid or inhibit a chemical reaction. Saline concentrations have been shown to affect certain enzymes by a process known as denaturing. This process can change the shape of the enzymes active site, possibly minimizing the ability of the substrate to bond to that specific enzyme (Starr and Taggart, 2001).
When specific enzymes are combined with hydrogen peroxide as a substrate, the resulting products are water and oxygen (Mader, Sylvia, 1998). By introducing sodium chloride, the predicted outcome would be the decreased production of oxygen as a product. By denaturing the enzyme, the reaction rate will decrease because sodium chloride will prevent the hydrogen peroxide from binding to the active site on a given number of the enzymes. This decrease in binding will inhibit the production of water as well as oxygen.
MATERIALS AND METHOD
• 2 POTATOS / KNIFE / ICE BATH WITH ICE
• TABLE SALT (NaCl) 6-10 grams
• 1% HYDROGEN PEROXIDE / Distilled Water (200ml each)
• 1-1000ml BEAKER / 8-SMALL BEAKERS (40ml)
• 1-STOPPER / 1- RUBBER HOSE / 1-GAS BOTTLE
• 1-INVERTED GRADUATED CYLINDER / 1-PLASTIC TUBE
• 1-WEIGHT SCALE / 1-WATER PAN / 1-BLENDER
We started by cutting the potato in pieces and weighing them until they weighed at 200 grams. While the potatoes were being done, we filled the blender with 2 handfuls of ice and 200 ml. of cold distilled water. Then we mixed the potato pieces, ice and 200 ml. of cold distilled water for about 15-20 seconds at high speed. I then grabbed the 1000 ml. beaker so I could pour the solution from the blender and place it in the ice bath. Next we took the 4-40 ml. beakers and labeled them A-D. The other 4-40 ml beakers were marked as 1-4.
In this experiment the enzyme peroxidase and the substrate hydrogen peroxide were not mixed initially, instead they were both placed in separate tubes and were incubated at a specific temperature, to prevent hydrogen peroxide from undergoing any reaction with peroxidase until they both acquire the required temperature.
Catalase is a common enzyme that is produced in all living organisms. All living organisms are made up of cells and within the cells, enzymes function to increase the rate of chemical reactions. Enzymes function to create the same reactions using a lower amount of energy. The reactions of catalase play an important role to life, for example, it breaks down hydrogen peroxide into oxygen and water. Our group developed an experiment to test the rate of reaction of catalase in whole carrots and pinto beans with various concentrations of hydrogen peroxide. Almost all enzymes are proteins and proteins are made up of amino acids. The areas within an enzyme speed up the chemical reactions which are known as the active sites, and are also where the
The shape of the molecules is changing and so the enzyme molecules can no longer fit into the gaps in the substrate that they need to and therefore the enzymes have de – natured and can no longer function as they are supposed to and cannot do their job correctly. Changing the temperature: Five different temperatures could be investigated. Water baths were used to maintain a constant temperature. Water baths were set up at 40 degrees, 60 degrees and 80 degrees (Celsius). Room temperature investigations were also carried out (20 degrees).
Jim Clark. (2007). The effect of changing conditions in enzyme catalysis. Retrieved on March 6, 2001, from http://www.chemguide.co.uk/organicprops/aminoacids/enzymes2.html
Background information:. Enzyme Enzymes are protein molecules that act as the biological catalysts. A Catalyst is a molecule which can speed up chemical reactions but remains unchanged at the end of the reaction. Enzymes catalyze most of the metabolic reactions that take place within a living organism. They speed up the metabolic reactions by lowering the amount of energy.
In this experiment as a whole, there were three individual experiments conducted, each with an individualized hypothesis. For the effect of temperature on enzyme activity, catalase activity will be decreased when catalase is exposed to temperatures greater than or less approximately 23 degrees Celsius. For the effect of enzyme concentration on enzyme activity, a concentration of greater or less than approximately 50% enzymes, the less active catalase will be. Lastly, the more the pH buffer deviates from a basic pH of 7, the less active catalase will be.
We then cut our potato tubes with the cork borer and cut them with the scalpel so they were the same length and weighed them. We then put one potato tube in each test tube and then added the same amount sugar solution in to each tube. The concentration of sugar solutions varied in each test tube.
Method: [IMAGE] Equipment needed: Ruler Measuring Cylinder Scalpel Tongs Pipette Thermometer Tri-pod Stop-clock Gauze Delivery Tube Bunsen Burner Beaker Matches/Lighter Potato Hydrogen Peroxide Solution (20%) Water Lead Nitrate The skin of the potato was removed using a scalpel and then cut into 1cm², using a ruler to measure the size of each cube, four cubes are required for each experiment, and therefore at least 36 cubes are required for the full experiment to take place. Fill a beaker half way with water, and place a thermometer in the water. Allow the thermometer to warm to room temperature to gather an accurate reading, and measure the temperature, using the thermometer. A measuring cylinder was used to put 10ml of Hydrogen Peroxide Solution into a
Materials used in the experiment included 5-7 g of the potato tissue, 50ml of 2.0M phosphate buffer coffee filter and guaiacol dye.
Introduction / Background Information. This is an experiment to examine how the concentration of the substrate Hydrogen Peroxide (H2O2) affects the rate of reaction of the enzyme Catalase. In this experiment I will be using yeast as a source of catalase. Enzymes are catalysts which speed up specific reactions. Enzymes such as catalase are protein molecules, which speed up a specific reaction within the cell.
Enzymes have the ability to act on a small group of chemically similar substances. Enzymes are very specific, in the sense that each enzyme is limited to interact with only one set of reactants; the reactants are referred to as substrates. Substrates of an enzyme are the chemicals altered by enzyme-catalysed reactions. The extreme specific nature of enzymes are because of the complicated three-dimensional shape, which is due to the particular way the amino acid chain of proteins folds.
Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is important that a specific enzyme is present during the process. For example, lactase must be able to collaborate with lactose in order to break it down (Madar & Windelspecht, 105).
Enzymes as mentioned before help speed up reactions, they generally work by bonding to a substrate, this bonding occurs at the active site. This link then forms a different molecule which will benefit its respective process. Every enzyme has its own optimum pH level to work under, if too low the enzyme will be very slow. However if too high the enzyme will then denature and be obsolete. This is why it is important to know the optimum pH level for whatev...
Equipment Potato, Borer, Beakers, Measuring Cylinder, Stopclocks, Distilled Water, Electronic Balance, Salt solutions of various concentrations. Diagram [IMAGE] [IMAGE] [IMAGE] When we leave the potato in the solution for the allocated time, water
all be cut out of the potato using a cork borer and will all be cut to