Enzymes And Substrate Concentration

In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or

Given the background, we hypothesized that for the first experiment, the lactase will break down lactose in milk and have a similar effect to sucrose. We also predicted that the Milk + Lactase reactant would have more glucose, the Milk + Water reactant would have a little bit of glucose broken down, the Sucrose + Lactase reactant would have less glucose than the Milk + Water reactant, and the Sucrose + Water reactant would have little to no glucose at all. As for the first procedure of the second experiment, we had hypothesized the more basic the solution would become, then the more glucose there would be. Our prediction for the first procedure of the second experiment was that there would be no glucose found in the solutions containing pH 4 and pH 7. For the second procedure of the second experiment, our hypothesis was that glucose would be present in the reactants at 4ºC and 25ºC while the reactant that had been in the hot water bath at 100ºC would have little to no glucose because it would have evaporated. We predicted that for this temperature experiment, the glucose would evaporate at 100ºC and would remain at 4ºC and 25ºC. For the first experiment we had found that a reactant of Milk + Lactase have high levels of glucose, while the other three reactants do not. As for the second experiment, for the first procedure, amounts of glucose were found in

-VariablesoIndependent:The temperature of the milkoDependent:The time taken for the milk to solidifyoControlled:The same amount and type of milk usedThe same amount and concentration of enzyme mixture usedThe same test tube sizeResults:-TableAmount of enzyme mixture (mL)Amount of milk (mL)Temperature (oC)Time for milk to clot (min)Ex: 1 Ex: 2 Average2.551060+60+60+2.552034.2036.0035.12.55303.554.203.882.55402.102.252.182.55505.004.454.73Discussion:The experiment showed that changing the temperature did affect the rate at which the milk solidified. At low temperatures of 10oC and 20oC the milk took the longest to solidify and at 10oC did not even go lumpy after an hour. As the temperature increased the speed at which it reacted got faster until it reached around 40oC where the speed began to drop.

Enzymes react differently under different conditions and concentrations, being the most productive at the enzymes specific optimum condition and concentration. The enzyme sucrase, extracted from yeast, breaks down the complex sugar sucrose into the simple sugar glucose. Testing for sucrase’s optimum environment, multiple reactions were ran using varying amounts and concentrations of sucrose and sucrase at different pHs and temperatures. The product was then treated with Benedicts solution to visually observe what amount of glucose was present after the reaction was ran; negative results being little to no glucose present and positive results being

I predict that at temperatures above 70°C the enzyme lipase will become denatured and at temperatures below 10°C the enzyme will become inactive. Since lipase operates within the human body I’d also predict that its optimum temperature would be around human body temperature which is approximately 37°C. I predict that before the optimum temperature the rates will gradually increase and preceding the optimum there will be a drastic decrease in rate until the enzyme is denatured.

Effect of pH on Enzyme Activity. 1. Dependent Variable. amount of product (glucose and fructose) produced 2. Independent Variable. pH 3. Controlled Variables. temperature; amount of substrate (sucrose) present; sucrase + sucrose incubation time

My graph shows there is an almost perfect positive correlation between the hydrogen peroxide concentration and the rate of the catalase enzyme reaction, with a correlation coefficient of 0.99. The rate of reaction at 1% concentration was 0.46cm3 oxygen produced per minute and the lowest recorded rate. For 3% was 1.33cm3 per minute, and for 6% was 2.17cm3 per minute and was the highest recorded rate. The

Background and Introduction: Enzymes are proteins that process substrates, which is the chemical molecule that enzymes work on to make products. Enzyme purpose is to increase the rate of activity and speed up chemical reaction in a form of biological catalysts. The enzymes specialize in lowering the activation energy to start the process. Enzymes are very specific in their process, each substrate is designed to fit with a specific substrate and the enzyme and substrate link at the active site. The binding of a substrate to the active site of an enzyme is a very specific interaction. Active sites are clefts or grooves on the surface of an enzyme, usually composed of amino acids from different parts of the polypeptide chain that are brought together in the tertiary structure of the folded protein. Substrates initially bind to the active site by noncovalent interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions. Once a substrate is bound to the active site of an enzyme, multiple mechanisms can accelerate its conversion to the product of the reaction. But sometimes, these enzymes fail or succeed to increase the rate of action because of various factors that limit the action. These factors can be known as temperature, acidity levels (pH), enzyme and/or substrate concentration, etc. In this experiment, it will be tested how much of an effect

Enzymes are proteins which can catalyse chemical reactions without changing themselves. The enzyme lipase breaks down the fat in dairy products such as full-cream milk for people who are lactose intolerant. Lipase acts on its specific substrate, lipids produces fatty acids. If enzyme concentration increases, random collisions between the substrates and active sites of enzyme increase due to the increasing amount of active sites which allow more collisions to happen, so the rate of breakdown of lipids to simpler substances will increase. During the experiment, sodium carbonate solution and pH indicator phenolphthalein will be added ahead of

5. Heat treatment was used to denature the sucrase that was added to the control test tube. In the experimental test tube, alkaline

The aim of this investigation is to explore the effect of different concentrations of bile salts on the time taken for the lipase enzyme to break down fat.

In part II of the lab six small glass tubes were obtained in a test tube rack. Ten drops of distilled water were then added to test tube 1, five drops to tubes 2-4, and no drops in tubes 5 and 6. Five drops of 0.1M HCl were added to test tube 5 and five drops of 0.1M NaOH to test tube 6. Five drops of enzyme were then added to all tubes except tube 1. Tube 3 was then placed in the ice bucket and tube 4 was placed in the hot bucket at 80-900C for five minutes, the remaining tubes were left in the test tube rack. After the five minutes five drops of 1% starch was added to every tube and left to sit for ten minutes. After ten minutes five drops of DNSA were then added to all the tubes. All the tubes were then taken and placed in the

We then tested the last set of test tubes containing milk and lactase, we did this to find which ones would present the most glucose concentration results, when placed in different temperatures, 4°C, boiling and room temperature. What we wanted to know was how far temperature could affect lactase to perform its enzymatic activity. We hypothesized that if the lactase is placed in a high or low temperature outside its active range, the temperatures would have a negative impact on the functions of the enzyme. If the temperature has an affect on lactose then we would see some temperatures in which lactase will be function able. We came to a conclusion that enzymes work at a temperature that is closest to body temperature (25°C); boiling water (100°C) denatures the enzyme, while the enzyme is not able to function properly if

Enzymes are high molecular weight molecules and are proteins in nature. Enzymes work as catalysts in biochemical reactions in living organisms. Enzyme Catecholase is found on in plants, animals as well as fungi and is responsible for the darkening of different fruits. In most cases enzymatic activities are influenced by a number of factors, among them is temperature, PH, enzyme concentration as well as substrate concentration (Silverthorn, 2004). In this experiment enzyme catecholase was used to investigate the effects of PH and enzyme concentration on it rate of reaction. A pH buffer was used to control the PH, potato juice was used as the substrate and water was used as a solvent.

The purpose of this lab is to examine the specificity of the lactase enzyme to a specific substrate and how it can denature due to the rise in temperature.