The effect of temperature and pH on the enzyme activity of the potato (Solanum tubersum) with the use of spectrophotometry.
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 this experiment, 4 grams of peeled turnip was used to prepare the enzyme extract opposed to the 1 gram of turnip suggested by Fundamentals of Life Science. Along with the change to the amount of turnip used, the amount of 0.1M phosphate buffer used to prepare the enzyme extract was changed from 50mL to 30mL. The affect of temperature on enzyme activity was not
The objective of Day 1 of this lab was to create a liquid fertilizer with 10% phosphorous by mass, 80% nitrogen by mass, and 50% potassium by mass using soluble compounds containing those elements. Additionally, a goal of Day 1 was to attempt to keep the pH of the final fertilizer within 6 and 7, although if the pH was outside this range it was not necessary to adjust the pH of the fertilizer to fit within this range.
Arana, M. V., Sánchez-Lamas, M., Strasser, B., Ibarra, S. E., Cerdán, P. D., Botto, J. F., & Sánchez, R. A. (2014). Functional diversity of phytochrome family in the control
The role of an enzyme is to catalyse reactions within a cell. The enzyme present in a potato (Solanum Tuberosum) is catechol oxidase. In this experiment, the enzyme activity was tested under different temperature and pH conditions. The objective of this experiment was to determine the ideal conditions under which catechol oxidase catalyses reactions. In order to do this, catechol was catalyzed by catechol oxidase into benzoquinone at diverse temperatures and pH values. The enzyme was exposed to its new environment for 5 minutes before the absorbance of the catechol oxidase was measured at 420 nm using a spectrophotometer. The use of a spectrophotometer was crucial for the collection of data in this experiment. When exposed to hot and cold temperatures, some enzymes were found to denature causing the activity to decrease. Similarly, when the pH was too high or low, then the catechol oxidase enzyme experienced a significant decrease in activity. It can be concluded after completing this experiment that the optimal pH for catechol oxidase is 7 and that the prime temperature is 20º C. Due to the fact that the catechol oxidase was only tested under several different temperatures and pH values, it is always possible to get a more precise result by decreasing the increments between the test values. However, our experiment was able to produce accurate results as to the
Based on the class data of the pH of phosphorylase reaction, the potato phosphorylase is reached the endpoint which the phosphorylase active at pH 6, it started active within 6 minutes. The optimal pH of phosphorylase is at pH 7 which active just within 4 minutes. At pH 6, it started to breaking down the starch primer +glucose-1-phosphase into starch + phosphate which reacted with the iodine test to formed the blue precipitate. At the optimal pH 7, it shows that it maximized its activity. Comparing the data of the pH of the potato phosphorylase reaction with the study published by Russell Pressey from Plant
Bacteria belongs to a group of organism that lacks cell nucleus and membrane bound organells. This group of organisms are termed as prokaryotes. Prokaryotes follows the central dogma of molecular biology first proposed by Francis Crick in 1958 to synthesize proteins from mRNA through a process called translation and the mRNA is being synthesized from the DNA by another process called Transcription. Temperature, nutrient availibity are some key factors that start the process of synthesizing proteins in response to these key factors. Example. This paper will provide an explanation as to how bacteria decode the genetic information to produce
Amounts of prussic acid are affected by the amount of nitrogen and phosphorus in the soil. It seems that if nitrogen is high it cannot be broken down if there is also low levels of phosphorous, so the plant uses the access nitrogen to make the cyanide compound. The South Dakota State University Cooperative Extension Service recommends splitting the nitrogen application into two to decrease the risk of prussic acid formation and the other concern of nitrate toxicity. Drought can cause the phosphorus to be a limiting factor in the plants growth because it does not allowing it reach the safe ratio of prussic acid to forage. Plus it allows for nitrogen to be in access.
The proteins were visualized using the Coomassie Blue stain. Coomassie Blue binds non-specifically and nearly stoichiometrically to all proteins [5]. Proteins have a higher affinity to the dye than the polyacrylamide gel; therefore, after removing excess stain, the protein bands can be visualized [4]. This non-selective binding was essential for analyzing the purity in each invertase fraction, as both non-target proteins and invertase were visualized. As shown in Fig. 1., excluding invertase fraction 2, the general trend was that the number of protein bands decreased from fractions 1 to 4, while a band with a molecular weight around 1.2 x 102 kDa became more prominent and intense. These results were expected for a successful purification [4]. During experiment 6, it was observed that the specific activity increased during each successive fraction. Since the same amount of protein, from each invertase
The intention of this experiment is to determine the effects of pH on the rate of photosynthesis in living leaves. Photosynthesis is a process by which plants convert light energy captured from the sun into chemical energy which they use to perform various plant functions. During the photosynthesis process, light, carbon dioxide, and water react to produce products: sugar and oxygen. The equation for photosynthesis is:
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.
To find the effect of temperature on the activity of an enzyme, the experiment deals with the steps as follows. First, 3 mL if pH 7 phosphate buffer was used to fill three different test tubes that were labeled 10, 24, and 50. These three test tubes were set in three different temperature settings. The first test tube was placed in an ice-water bath for ten minutes until it reached a temperature of 2° C or less. The second tube’s temperature setting was at room temperature until a temperature of 21°C was reached. The third tube was placed in a beaker of warm-water until the contents of the beaker reached a temperature setting of 60° C. There were four more test tubes that were included in the procedure. Two of the test tubes contained potato juice were one was put in ice and the other was placed in warm-water. The other two test tubes contained catechol. One test tube was put in ice and the other in warm water. After
The purpose of the experiment was to isolate plasmid DNA, followed by restriction digestion using restriction endonucleases and then visualizing the digested fragments after subjecting to gel electrophoresis. Plasmid DNA (pSP72 DNA) was isolated from Escherichia coli KAM32 (E.coli) cultures using the QIA prep miniprep kit and then subjected to restriction digestion by EcoRI and HindIII. The restriction digested DNA was then loaded into the wells of 0.7% agarose gel and subjected to electrophoresis. It can be concluded from our results that our plasmid DNA isolation was successful and the restriction digestion results were partially in agreement with our hypothesis.