Enzymes function best in a specific range of pH. Their activity is reduced if the pH goes below or over that optimum level. The effect of change in pH on rennet activity was recorded in table 4 and charted in a line graph in figure 4. The trend between the times for the milk to curdle when the pH was manipulated can be observed in figure 4. A positive correlation between the two variables can be seen because as the pH of the milk increase so does the curdling time. Qualitatively speaking as the pH of the milk increased from 5 to 9 the amount of curdles formed decreased and so did their size.
When comparing figure 1, the hypothesized diagram, to figure4, the experimental results, the two graphs considerably resemble each other. Thus the above
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It was expected that the change in pH disrupts enzyme’s structure when its side chains containing -COOH and –NH2 gain or lose H+ ions (Anglin, M., September 2, 2014). The deformed active sites are incapable of binding the substrate and facilitating the reaction. Altering the pH of the solution altered the tertiary structure of the enzyme rennet by changing bonds between each side chains on the amino acid. Some amino acid side chains have ionic charges and use ionic bonds in order to create tertiary structures (Clark, J., 2007). Modifying the pH of milk originally at 6.5 to 5, 7, 8 and 9 changed the charges on the ionic side chains. A higher pH results in fewer hydrogen ions and more hydroxide ions. The hydroxide ions bond to the positively charged side chains making them unavailable to bond to the negatively charged side chains. Since …show more content…
First source of error is observer subjectivity. The observations made on the qualitative results of the experiments are based entirely on observer’s ability to detect and interpret the results. A different observer may detect or interpret the same events differently. To avoid such errors, the observers should be briefed properly and in detail on the possible outcomes of the event so the record can have some uniformity between different observers, e.g., some guidance should be provided to determine what constitutes a small, medium and large piece of curd. Secondly, pH paper was used to determine the pH of the solution. The colors of the pH strip once dipped in the solution corresponded to the pH ranges usually in increments of 1. Thus using the pH paper did not give specific pH of the solution. In order to avoid such error pH meters can be used which provides its user with more accurate and exact pH
The reason this occur may also been due to the presence of CO2 in the room that may have reacted with hydrogen ions in, forming carbonic acid. This would make the pH lower throughout the rest of the
The purpose of this experiment was to analyze the effects of the variables: temperature, pH, and enzyme concentration, on the enzymatic reaction rate of catalase and the level at which its products are released, measuring the rate of absorption using the indicator solution guaiacol and a spectrophotometer to develop a hypothesis of the ideal conditions for these reactions. My hypothesis is that the extremes in concentration, temperature and pH will negatively affect the Au rate. This experiment used 11 solutions contained in cuvettes. Each cuvette, once mixed, is placed in spectrophotometer and then a reading taken every 20 seconds. Cuvettes 1, 8, and 10 are used as blanks to zero out the spectrophotometer.
By completing this experiment, knowledge collected about optimal pH in enzymes will help
The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.
3. Look at your graph for Part B, how does temperature affect enzyme activity? The colder the temperature the greater the reaction. 4. Look at your graph for Part C, how does pH affect the enzyme activity?
However, the experimental values were different due to human error. Error Analysis Discuss the
Each buffer was measured in a 100 mL graduated cylinder and contained in a 40 mL beaker. Once the reading of the buffer was stabilized, the program entered into reading 1. The probe was cleaned with distilled water and dried before being placed into the second buffer for reading 2. Once the second calibration was completed the pH probe was cleaned again. Next the probe was placed into the unknown solution.
Photograph Description: Photograph 1, shown on the previous page, was taken after 20 drops of the crystal violet dye was added to the solution, and photograph 2 was taken after 40 drops were added. As seen in the pictures, only a faint ring of violet was visible around the coacervates. Photographs 3-5 were taken after adding a drop of 20% concentration crystal violet dye onto the side of a slide. Discussion
LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.22.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3. Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2.
These enzymes have a secondary and tertiary structure and this could be affected by increases and decreases in temperature beyond the optimum temperature of the enzyme to work in. Mostly enzymes are highly affected any changes in temperature beyond the enzymes optimum. There are too
Introduction 1.1 Aim: To determine the kinetic parameters, Vmax and Km, of the alkaline phosphatase enzyme through the determination of the optimum pH and temperature. 1.2 Theory and Principles (General Background): Enzymes are highly specific protein catalysts that are utilised in chemical reactions in biological systems.1 Enzymes, being catalysts, decrease the activation energy required to convert substrates to products. They do this by attaching to the substrate to form an intermediate; the substrate binds to the active site of the enzyme. Then, another or the same enzyme reacts with the intermediate to form the final product.2 The rate of enzyme-catalysed reactions is influenced by different environmental conditions, such as: concentration
Acids are proton donors in chemical reactions which increase the number of hydrogen ions in a solution while bases are proton acceptors in reactions which reduce the number of hydrogen ions in a solution. Therefore, an acidic solution has more hydrogen ions than a basic solution; and basic solution has more hydroxide ions than an acidic solution. Acid substances taste sour. They have a pH lower than 7 and turns blue litmus paper into red. Meanwhile, bases are slippery and taste bitter.
ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells.
Practical I: Acid-base equilibrium & pH of solutions Aims/Objectives: 1. To determine the pH range where the indicator changes colour. 2. To identify the suitable indicators for different titrations. 3.
In direct titrations, the number of moles of acid can be easily derived by simply manipulating with the values of acid and base given in the experiment. In back titration, excessive volumes of acid are always added. Of which, only a certain quantity would be neutralised. The number of moles of acid is eventually derived from titrating this excess acid with a strong base and using mole fractions to calculate. The quantity of acid neutralised is obtained by subtracting the moles of acid given at the start of the experiment, with the moles of acid titrated.