Effect of different size beads on the activity of immobilised catalyse Aim: To find out how varying the size of beads containing yeast varies the rate of activity of catalase in a fermentation reaction of hydrogen peroxide with immobilised enzymes. A catalyst is a substance that speeds up the rate of a chemical reaction, without itself being used up in the process however it maybe affected physically i.e. degradation of the surface of the catalyst. Catalysts work by reducing the activation energy needed for a particular reaction by offering a different path for the reaction to take place. Activation energy is the energy, which needs to be supplied before a reaction can occur, basically the amount of energy needed to overcome the bonds between the molecules and atoms. [IMAGE] Catalysts are usually specific to one reaction, that is, different reactions need different catalysts. This is the lock and key theory however there is another theory as well called the induced fit theory. Since a catalyst is not used up during a chemical reaction, it can be used over and over again to convert reactants to products. In this experiment I will be using the immobilised enzyme yeast. When an enzyme is immobilised in this case it is encapsulated in a sodium alginate gel. When an enzyme is immobilised it is in a more stable state, they are better able to resist alteration to shape and activity. In particular they are less likely to be inactive or denatured by changes in pH, presence of other chemicals, or high temperatures. Immobilised enzymes can also be used for longer periods before their activity reduces which is useful in the experimen... ... middle of paper ... ...might have a larger surface area to volume ratio however the bead might be so big that there might be more enzymes on the outer surface. Percentage errors I can work out the percentage errors for my measurements, by using this formula. Mass of calcium chloride (0.005 x 100)/1.4 = 0.7% Mass of sodium alginate (0.005 x 100)/0.4 = 0.2% Pipette (0.05cm3 x 100)/10=5% (0.05cm3 x 100)/5=2.5% (0.05cm3 x 100)/15=7.55% (0.05cm3 x 100)/2=1% (0.05cm3 x 100)/50=25% Measuring beaker (0.2 cm3 x 100)/250 =0.08% Measuring tube (0.1 cm3 x 100)/10 =1% Measuring tube containing hydrogen peroxide (0.1cm3 x 100)/50 =0.2% Measuring tube containing water (0.1cm3 x 100)/100 =0.1% Measuring tube to calculate volume of beads (1cm3 x 100)/8 =12.5%
To begin the study, I first calculated how much of each solution I would need. I knew that the final volume of my reaction solution needed to me 30ml, so I calculated how much of starch, amylase, and tris buffer I would need. I used the formula Concentration (initial stock solution) x Volume (initial stock solution)= Concentration (final solution) x Volume (final solution). Using this formula, I found that I would need an initial concentration of 21 ml of starch, 1 ml of amylase, and 8 ml of the tris buffer. After calculating the amounts of substances I would need, I created two different solutions, one with the Carb Cutter and one without. Carb Cutter claims to block starch, however, to find this I needed to test the absorbance level of the control to compare the effect Carb Cutter had on the solution. Below is a graph showing the concentration of the control reaction over one minute intervals through the
Each subsequent trial will use one gram more. 2.Put baking soda into reaction vessel. 3.Measure 40 mL vinegar. 4.Completely fill 1000 mL graduated cylinder with water.
We then took 1ml of the 0.1% solution from test tube 2 using the glucose pipette and added it to test tube 3, we then used the H2O pipette and added 9ml of H2O into test tube 3 creating 10ml of 0.01% solution.
For example, substrate concentration, enzyme concentration, and temperature could all be factors that affected the chemical reactions in our experiment. The concentration of substrate, in this case, would not have an affect on how the bovine liver catalase and the yeast would react. The reason why is because in both instances, the substrate (hydrogen peroxide) concentration was 1.5%. Therefore, the hydrogen peroxide would saturate the enzyme and produce the maximum rate of the chemical reaction. The other factor that could affect the rate of reaction is enzyme concentration. Evidently, higher concentrations of catalase in the bovine liver produced faster reactions, and the opposite occurs for lower concentrations of catalase. More enzymes in the catalase solution would collide with the hydrogen peroxide substrate. However, the yeast would react slower than the 400 U/mL solution, but faster than the 40 U/mL. Based on this evidence, I would conclude that the yeast has a higher enzyme concentration than 40 U/mL, but lower than 400
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
The purpose of this assessment was to research, design and conduct an experimental investigation on the effect of substrate concentration (manipulated by increasing concentration of pH buffer) of catalysed reactions by measuring the volume of oxygen produced as the reaction proceeded.
3. The higher the concentration of the enzyme the more there are to catalyze the reaction. Taking information from graph 1 (change in mL of enzyme), the more mL of enzymes that there are the faster the reaction rate is. It would increase until there was no substrate left available for a reaction.
The three-dimensional contour limits the number of substrates that can possibly react to only those substrates that can specifically fit the enzyme surface. Enzymes have an active site, which is the specific indent caused by the amino acid on the surface that fold inwards. The active site only allows a substrate of the exact unique shape to fit; this is where the substance combines to form an enzyme- substrate complex. Forming an enzyme-substrate complex makes it possible for substrate molecules to combine to form a product. In this experiment, the product is maltose.
There are millions of cars on the road in the United States, and each one is a source of air pollution. Especially in large cities, the amount of pollution cars produce everyday is a lot. To solve those problems, many laws have been enacted restricting the amount of pollution that cars can produce. To make their cars as pollution-free as possible, automakers have made many refinements to car engines and fuel systems and have developed the catalytic converter. The catalytic converter treats the exhaust before it leaves the car, and removes a lot of the pollution.
A Biological Catalyst A Biological catalyst is a catalyst that is produced organically. In other words, a cell makes it. It is usually a protein or steroid molecule that works to catalyse a specific reaction. For example, amylase is a biological catalyst. Biological catalysts are called enzymes.
The Effects of Concentration on Reaction Rate with Sodium Thiosulphate ---------------------------------------------------------------------- Planning = == == =
How the Concentration of the Substrate Affects the Reaction in the Catalase Inside Potato Cells Introduction Enzymes are made of proteins and they speed up reactions, this means that they act as catalysts. Hydrogen peroxide is a byproduct of our cell's activities and is very toxic. The enzymes in our bodies break down the hydrogen peroxide at certain temperatures they work best at body temperature, which is approximately 37 degrees. At high temperatures, the cells begin to denature. This means that the hydrogen peroxide is prevented from being broken down because they will not 'fit' into the enzyme.[IMAGE] Objective I am going to find out how the concentration of the substrate, hydrogen peroxide affects the reaction in the catalase inside the potato cells.
Purpose: This lab gives the idea about the enzyme. We will do two different experiments. Enzyme is a protein that made of strings of amino acids and it is helping to produce chemical reactions in the quickest way. In the first experiment, we are testing water, sucrose solution, salt solution, and hydrogen peroxide to see which can increase the bubbles. So we can understand that enzyme producing chemical reactions in the speed. In the second experiment, we are using temperature of room, boiling water, refrigerator, and freezer to see what will effect the enzyme.
Chemical Kinetics is the branch of chemistry that studies the speed at which a chemical reaction occur and the factor that influence this speed. What is meant by the speed of a reaction is the rate at which the concentrations of reactants and products change within a time period. Some reactions occur almost instantaneously, while others take days or years. Chemical kinetics understanding I used in the process of designing drugs, controlling pollution and the processing of food. Most of the time chemical kinetics is used to speed or to increase the rate of a reaction rather than to maximize the amount of product. The rate of a reaction is often expressed in terms of change in concentration (Δ [ ]) per unit of time (Δ t). We can measure the rate of a reaction by monitoring either the decrease in concentration (molarity) of the reactant or the increase in the product concentration.
Experimental Strategy: In this experiment, the yeast being used is called Saccharomyces cerevisiae. This type of yeast follows fermentation which is very unique and can tell how much carbon dioxide is produced by fermentation more accurately compared to cellular respiration. Three test tubes will be filled with a specific volume and concentration of sugar with a certain amount of yeast in each test tube. Two of the three test tubes will have similar concentrations of sugar with different amounts of yeast...