Biology Assignment on Enzyme Activity PDF
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Uploaded by NiceBigBen9109
Linlithgow Academy
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Summary
This biology assignment investigates the effect of inhibitor concentration on enzyme activity. The experiment measures the volume of oxygen gas produced as an indicator of enzyme activity. The document outlines the underlying biology, including enzyme function and inhibition types.
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Biology assignment Aim - to investigate the effect of inhibitor concentration on enzyme activity Brief description - 5 measuring cylinders were set up with different concentrations of copper nitrate (0.6% solution). Equal amounts of a Hydrogen peroxide and detergent solution and a cube of...
Biology assignment Aim - to investigate the effect of inhibitor concentration on enzyme activity Brief description - 5 measuring cylinders were set up with different concentrations of copper nitrate (0.6% solution). Equal amounts of a Hydrogen peroxide and detergent solution and a cube of liver was added to each measuring cylinder and were left for an equal amount of time. Volume of oxygen bubbles was measured and the experiment was repeated multiple times. The volume of oxygen gas produced (indicated by the foam or bubbles) was measured as an indicator of enzyme activity. Underlying biology - Enzymes are essential proteins that control metabolic pathways in cells, which are crucial for processes like energy production, biosynthesis, and degradation. Metabolic pathways can be anabolic or catabolic. Anabolic reactions are those that build larger molecules from smaller ones, requiring an input of energy. These reactions are important for growth, repair, and maintaining the structure of cells and tissues. Catabolic reactions are those that break down larger molecules into smaller ones, releasing energy in the process. These reactions are crucial for generating the energy required to drive cellular activities. These pathways are regulated to prevent the accumulation of unnecessary products, often through the control of enzyme activity. Enzymes have a specific active site where substrates bind. The enzyme-substrate complex lowers the activation energy of a reaction, allowing it to occur more efficiently. However, enzyme activity can be influenced by inhibitors, which decrease enzyme function by binding to the enzyme and preventing substrate interaction. There are two main types of inhibitors: 1. Competitive Inhibition - The inhibitor competes with the substrate for the active site. The inhibitor has a similar shape to the substrate, so it can bind to the enzyme’s active site, preventing the substrate from binding. This reduces the enzyme’s ability to catalyse the reaction. As the inhibitor concentration increases, enzyme activity decreases, but this can be overcome by adding more substrate. 1. Non-Competitive Inhibition - The inhibitor binds to a different site on the enzyme (not the active site), altering the enzyme's shape and preventing substrate binding. This type of inhibition cannot be overcome by increasing substrate concentration, and enzyme activity is permanently reduced. 1. Enzyme activity is also regulated by feedback inhibition, where the end product of a metabolic pathway inhibits an enzyme at the start of the pathway, preventing overproduction. *line graph* Analysis My results show that as the concentrations of copper nitrate solution decrease from 100% to 20% the volume of foam increases by ___ This means that the rate of enzyme activity is higher at lower concentrations of copper nitrate The results from my experiment, when compared to data from an internet source, show similar trends with increasing inhibitor concentrations. This confirms that inhibitor concentration affects the enzyme activity. Conclusion As the inhibitor (copper nitrate solution 0.6%) concentration is decreased the enzyme activity increases. This is illustrated by the rise in volume of foam as the copper nitrate concentration is decreased. More foam production correlates with higher enzyme activity. Evaluation - I believe the results from my experiment were reasonably reliable. Since the results were consistent across each trial, it suggests there were no errors. Additionally, the similar findings from the internet source further support the reliability of my results. As temperature affects enzyme activity I could have ensured that the temperature was kept constant. This could've been done by placing the measuring cylinders in a water bath at a specific temperature. I used syringes to measure the volumes of reactants, which improved the validity of the measurements, ensuring accurate quantities of each substance were used.