Investigating the Effect of Substrate Concentration on Catalase Reaction Planning -Aim: The aim of the experiment is to examine how the concentration of the substrate (Hydrogen Peroxide, H2O2) affects the rate of reaction of the enzyme (Catalase). -Background information: Enzyme Enzymes are protein molecules that act as the biological catalysts. A catalyst is a molecule which can speed up chemical reaction but remains unchanged at the end of the reaction. Enzymes catalyze
The Effect of Substrate Concentration on the Rate of Reaction Between Yeast Catalase and Hydrogen Peroxide Useful info The Enzyme Catalase is a protein molecule which is found in living cells. It is used to speed up reactions in the cells. It is a very specific enzyme and just performs one particular reaction. Catalase is an enzyme found in cells in potatoes and liver and is used for removing Hydrogen Peroxide from the cells. Hydrogen Peroxide is the poison produced during metabolism
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
Affect of the Rate of Reaction of Amylase on Starch and How Its Affected by the Concentration of the Substrate Equipment list Ø Test tubes Ø Measuring cylinder Ø Thermometer Ø 3 pipettes Ø Starch solution Ø Amylase Ø Iodine solution Ø Water Ø Water bath Ø Spotting tile Ø A stop watch Ø Goggles Ø Beakers Health and safety ================= Remove all hazardous jewellery such as dangling earrings, bracelets, and chains. Make sure items of clothing
suggesting that an increase in substrate concentration will increase the height of bubbles until it reaches the optimum amount of substrate concentration, resulting in a plateau in the graphs (figure 2). Hence; supported the hypothesis. Acting as the controlled group to lessen the effects of all variables except the independent variable, at 0% concentration, the height of foam produced is 0 mm. Attributions to these results is because at 0% substrate concentration, no molecules were present to occupy
Effect of Substrate Concentration on Catalase Aims This is an experiment to examine how the concentration of the substrate Hydrogen Peroxide (H2O2) affects the rate of reaction of the enzyme Catalase. Background Information Enzymes such as Catalase are protein molecules, which are found in living cells. They are used to speed up specific reaction within the cell. They are all very specific as each enzyme just performs one particular reaction. Catalase is an enzyme found in food
effect of the substrate concentration on enzyme activity? Hypothesis As the concentration of the substrate increases, the rate of reaction also increases until it reaches its maximum point where all enzyme molecules are already active due to the solution becomes saturated with the hydrogen peroxide. Therefore, when the rate of reaction is finally at its maximum point, adding more substrate will not make any difference to the rate of reaction. The rate of reaction increases when the substrate is added
[IMAGE]Background Theory for this experiment: An enzyme is described as a biological catalyse. This means that its helps all of the reactions in the body by speeding them up and helping them react with there particular substrate to form a reaction. In the case of my experiment the substrate is starch, a polysaccharide which is broken down by an enzyme called amylase into maltose a disaccharide. Amylase is an enzyme found in various places in the body including the saliva and pancreas. An enzyme
mechanism by which HMB impacts muscle proteolysis and function is not currently known. Nevertheless there are a number of postulations. "The high substrate concentration required by the dioxygenase enzyme compared with the liver concentration of KIC suggests that HMB production in the body may be a first-order reaction controlled by enzyme and KIC concentrations. It has been calculated that, under normal conditions, about 5% of leucine oxidation proceeds via this pathway. Therefore, if humans are assumed
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
The Effect Of Substrate Concentration On The Activity Of The Enzyme Catalase A Level Biology Project Aims This is an experiment to examine how the concentration of the substrate hydrogen peroxide affects the rate of reaction of the enzyme catalase. Introduction This is a real A-level school project and as such is intended for educational or research purposes only. Extracts of this project must not be included in any projects that you submit for marking. Doing this could lead to being
measure? Volume of substrate used Continuous Yes Type of enzyme Discontinuous Yes Overall mass of piece of meat Continuous No Type of substrate used Discontinuous Yes Temperature of substrate Continuous Yes pH of substrate Continuous No -- Concentration of substrate used Continuous Yes The independent variable I have chosen, or the one to be changed throughout the experiment will be 'the concentration of substrate used', which will
starch and amylase will be. I predict this because of the lock and key hypothesis. The lock and key hypothesis explains how the substrate molecule (the starch) fits inside the enzyme. The substrate molecule is then broken up into many smaller pieces. In this experiment the larger the volume of amylase (enzyme/active site) there is then the quicker the starch (substrate) will be broken down, resulting in a fast reaction rate. Therefore, a smaller amount of amylase will result in a slower reaction
higher the temperature the faster the rate of reaction will be and the more oxygen there will be given off. I've based this prediction on kinetic theory (every 10 degree rise in temperature the rate of reaction doubles.) This is because the substrate will lock on twice as fast, as it is travelling twice as fast. To back up this prediction a pre experiment was carried out, one result was obtained, using this result here is a table of predicted values: Temp of 2H2O ËšC Amount of Oxygen
the catalysts reacts, called the substrate, is modified during the reaction to form a new product. But because the enzyme itself emerges from the reaction unchanged and ready to bind with another substrate molecule, a small amount of enzyme can alter a relatively enormous amount of substrate. This report will illustrate the enzymatic action of the enzyme catecholase, which is common in plants. To study this particular enzyme in a laboratory, the natural substrate catechol is oxidized by the removal
called its substrate. The diagram below shows an “E” (an enzyme) catalysing the breakdown of “S” (the substrate) into two different products (“P”). Catalysis occurs because substance S fits precisely into surface of the enzyme E, so this reaction and no others are speeded up. Diagram showing an enzyme catalsying the breakdown of its substrate into two product molecules. As can be seen from the diagram, if the enzyme changes shape, the active site (the area where the substrate reacts) would
dough and causes it to rise. Enzymes are catalysts which speed up reactions, they are made from protein and are specific as to which substrate they work on. Enzymes basically work due to the lock and key theory, where the substrate substance (the key) fits into the active site on the enzyme and they bind together, the reaction takes place and the substrate unlocks to
Investigating the Effect of Enzyme Concentration on the Hydrolysis of Starch with Amylase Aim: Investigate the effect of enzyme concentration on the rate of an enzyme-controlled reaction. Using amylase and starch as my example. Introduction: I am investigating the effect of the concentration of the enzyme, amylase on the time taken for the enzyme to fully breakdown the substrate, starch to a sugar solution. The varied variable will be the concentration and all other variables are going
the rate of reactions. Each enzyme has a unique 3D shape which means that they work with certain types of substrates. This is also known as ‘lock and key’ because the shape of the substrate fits into the shape of the enzyme, just the way a lock and key do. Enzymes work by attaching itself to the substrate molecule. The substrate molecule brakes down where the active site is. The substrate molecule splits and the enzyme is left unaffected. The factors that affect enzymes are: temperature, pH and
passes but also it shows that the more substrate present the more absorbance. We can clearly see that the line of the 6th test-tubes (more concentrated one) is way higher than the one with no substrate. All of the test-tubes data have each a linear-correlation (R2 >95%) with a slope more and more positive as the concentration of substrate increase. The only data that can be a little less precise is the data of the first test tube (trend line with 0mL substrate). Some issue with the spectrophotometer