How To Write An Enzyme Lab Report

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

The use of multiple test tubes and Parafilm was used for each experiment. Catechol, potato juice, pH 7 phosphate buffer, and stock potato extract 1:1 will be used to conduct the following experiments: temperature effect on enzyme activity, the effect of pH on enzyme action, the effect of enzyme concentration, and the effect of substrate concentration on enzyme activity. For the temperature effect on enzyme activity, three test tube were filled with three ml of pH 7 phosphate buffer and each test tube was labels 1.5 degrees Celsius, 20 °C, and 60 °C. The first test tube was placed in an ice-water bath, the second test tube was left at room temperature, and the third test tube was placed in approximately 60°C of warm water. After filling the test tubes with three ml of the

The practical was carried out to investigate the effect of pH on the reaction of the enzyme acid phosphatase.

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

The purpose of this lab is to understand how non-living systems can make it easier for chemical reactions to occur. In this lab, raw wheat germ acid phosphate was used to detach it from other chemicals. Raw wheat germ is an example of an enzyme which is defined as, “a biological catalyst, all catalysts work by speeding up the rate at which a chemical reaction occurs.” (Krane, 2018). Enzymes are made up of proteins that can be isolated in two different ways, assay and precipitation. Assay is defined as, “generally readily available for most enzymes and depend on the ability to detect a change (often in color) as substrates are converted to products as the reaction occurs.” (Krane, 2018). Precipitation can be described as, “procedures often begin with a series of trial and error experiments. There is no standard protein isolation technique that can be applied to all proteins and some large classes of proteins, like membrane-bound proteins.” (Krane, 2018). This lab was performed in three different sections, the first one being wheat germ suspension, where heat was used to purify and isolate the wheat germ. In the second portion of the lab, examiners found the concentration of the wheat germ protein. In the final step of the experiment examiners found the amount of acid phosphatase in each of the tested microtubes.

To prevent fluctuation in the pH, a solution known as a “buffer solution” was used in the experiment. Buffer solutions are mixtures of at least two chemicals which counteract the effect of acids and alkalis. Therefore, when a small quantity of alkali or acid solution is added the pH of the enzyme doesn’t change.

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

Introduction: Enzymes are protein catalysts facilitating the conversion of substrates into products (Alexander and Peters, 2011). They go through a whole chemical reaction which starts off with the substrate and then ends up with a product. The only way this reaction can be adjusted or not even work is if they end up going through some sort of affect which only temperature and pH levels can do determining the environment. When enzymes are in an environment that is too acidic or alkaline, their chemical properties, sizes and shapes can become altered (Magher, 2015) Chemical modification of proteins is widely used as a too; to maintain a native conformation, improving stability (Rodriguez-Cabrera, Regalado, and Garcia-Almendarez, 2011) In this experiment, four trials were conducted and recorded every 15 seconds for 5 minutes in order to calculate the optimum levels and IRV.

We did this to test which test tube would contain the highest concentration of glucose. What we wanted to know was if the lactase would affect the function of the enzyme. Our hypothesis is the lactase functions within a narrow pH and that will change in pH would affect the function of the enzyme. We predict that if we change the environmental factors it will have an effect the function of the enzyme if the pH is outside the range in its optimum activity. Our hypothesis was then proven because the reaction only occurred in a neutral and acidic state of pH, not basic. Which means the enzymes prime ability to function is a neutral, and acidic pH range.

For this experiment, we have to prepare our phosphorylase which extracted from a potato. We prepared by weighed about 250 grams of peeled potato and cut it into cubes. The extracts then blended with 100mL of 0.1M NaF. After filtered the contents into a clean 250mL centrifuge bottle, we centrifuged it for 3 minutes. Then, separated the supernatant into a centrifuge bottle, which is our phosphorylase preparation. The enzyme assay used in this experiment today is the iodine test. As the iodine reacts with starch, it will form a brown, blue or black precipitate due to the iodine ions forcing into a linear arrangement. The endpoint of the enzyme reaction indicates the presence of starch by using the iodine test to determine. The faster the endpoint is reached, the less active the phosphorylase is.

Enzymes are central to every biochemical process. Due to their high specificity they are capable of catalyzing hundreds of reactions that signifies their vast practical importance.

Sampling: Combine 450 uL of 0.15M NaCl, 20 mM Tris-HCL, pH 8, 500 uL of Azocasein, and 50 uL Trypsin into a micro centrifuge tube. We had six samples, three separate pH's were used, one for each of the control tubes with a consistency of three experimental replicates were used to Help with data variation. We allowed the samples to stay in the incubate for 10 minutes. The controls were used to show whether the substrate azocasein would hydrolyze without the enzyme present. We Use the Negative Controls and measured their absorbance because we need to see if the absence of the enzyme would affect the substrate and with an absorbance close to zero. we measured negative with reaction

Enzymes are an important part of all metabolic reactions in the body. They are catalytic proteins, able to increase the rate of a reaction, without being consumed in the process of doing so (Campbell 96). This allows the enzyme to be used again in another reaction. Enzymes speed up reactions by lowering the activation energy, the energy needed to break the chemical bonds between reactants allowing them to combine with other substances and form products (Campbell 100). In this experiment the enzyme used was acid phosphates (ACP), and the substrate was p-nitrophenyl phosphate.

The acid phosphatase was used to catalyze the reaction from p-nitrophenylphosphate to p-nitrophenol. The addition of base allowed for the stop of the reaction at various time intervals. The concentration of p-nitrophenol can be determined by measuring absorbance and calculating the correlating concentration from the standard curve. This would then allow for the calculation of Vmax and Km, which would determine the highest speed an enzyme can catalyze a reaction and the affinity of the substrate to bind to the enzyme. Consequently, the values would reveal the effect of substrate concentration, and the value of ideal concentration for which the enzyme will perform.

The present experiment was performed for analyzing the influence of the substrate concentration and inhibitors on the activity of alkaline phosphatase. p-nitrophenyl phosphate was used as a substrate for the hydrolytic enzyme and the inhibitory effect of sodium phosphate and L-phenylalanine was tested. The reaction rate was determined by measuring the absorbance change caused by the occurrence of p-nitrophenol, which was the product of the enzymatic reaction. During the tests performed for measuring the activity of the alkaline phosphatase in the absence of inhibitors, the following results were obtained: