Investigating the Effect of Copper Sulphate on Amylase Activity
Aim
The aim of my experiment is to observe the affect on amylase when
adding copper sulphate to a starch solution.
Introduction
Enzymes are that act as catalysts, in other words they increase the
rate of chemical reactions. Consider the following general reaction
between two substances, A and B, which react together to form a
product, substance C:
A + B = C
In biological systems, this reaction might occur very slowly, or not
at all, in the absence of an enzyme. Enzymes will greatly increase the
rate of formation of the product. They can increase the rate of
reactions by a factor of at least one million. Most enzymes are large
protein molecules, with complex three-dimensional shapes.
Enzymes increase the rates of reactions by reducing the free energy of
activation, so that the barrier to a reaction occurring is lower in
the presence of an enzyme. The combination of enzyme and substrate
creates a new energy profile, for the reaction, with a lower free
energy of activation.
Once the products have been formed, they leave the active site of the
enzyme, which is left free to combine with a new substrate molecule.
Enzymes, like chemical catalysts, are not used up in the reaction they
catalyse so they can be used over and over again. The overall reaction
between an enzyme and its substrate can be represented by the
following equation:
ENZYME+SUBSTRATE à ENZYME-SUBSTRATE complex àENZYME + PRODUCTS
Amylase is an enzyme that is found in saliva and pancreatic juice and
aids the digestion of starch and other polysaccharides, which it
breaks down into glucose, maltose and dextrins. It is required to
digest carbohydrates (polysaccharides) into smaller units
(disaccharides), and eventually converting them into even smaller
units (monosaccharides) such as glucose. So Starch being a
carbohydrate, Amylase hydrolyses the Starch.
Inhibitors are substances that reduce the activity of enzymes. They
act by interfering with the activity of the active site, either
To begin the study, I first calculated how much of each solution I would need. I knew that the final volume of my reaction solution needed to me 30ml, so I calculated how much of starch, amylase, and tris buffer I would need. I used the formula Concentration (initial stock solution) x Volume (initial stock solution)= Concentration (final solution) x Volume (final solution). Using this formula, I found that I would need an initial concentration of 21 ml of starch, 1 ml of amylase, and 8 ml of the tris buffer. After calculating the amounts of substances I would need, I created two different solutions, one with the Carb Cutter and one without. Carb Cutter claims to block starch, however, to find this I needed to test the absorbance level of the control to compare the effect Carb Cutter had on the solution. Below is a graph showing the concentration of the control reaction over one minute intervals through the
How Amylase Concentration Affects the Rate of the Starch Concentration In this piece of coursework, I have to carry out an investigation to find out how amylase concentration affects the rate of starch. Enzymes are biological catalysts that speed up the chemical reaction that goes on inside living things. An enzyme acts on substrate and may do its job inside or outside the cells. However, the rate at which enzymes work are affected by the following factors/variables: Concentration:
middle of paper ... ... Inhibitors are proteins called antibodies that are made by our immune system to defend us from harmful diseases. When our immune system identifies a foreign substance, it makes antibodies that will specifically recognize that substance and destroy it. In some individuals with severe hemophilia, the factor VIII replacement therapy is identified as a foreign substance by their immune system.
We hypothesized that the more heat that we put in or the more heat that we take out, would denature the enzymes and slow down the rate. We set up a plate of depressions the same way as above. We boiled water to 50o C, poured the water onto a tray and did the steps of placing the discs in same as above and timed it until they rose above the surface. We did the same process but instead of using heat, we put ice and cold water on a tray which was about 3.5o C. The control for this experiment was the one that we did before because it was at room temperature. The results for the hot tray showed no rate. The cold tray sped up the rate of reactions making it occur faster than at room temperature starting at 6 for 100% catalase. This lab supported and disproved our hypotheses. It supported our hypothesis for adding more heat because the enzymes were in such hot conditions that the heat denatured the enzyme, making it not possible to create a chemical reaction. So the rate of reaction was zero because the enzymes didn’t split apart hydrogen peroxide. The cold tray disproved our hypothesis. We thought that the cold tray would also denature the the catalase so that there would be little to no rate. Maybe the data came out this way because the catalase was left out in room temperature for a long time that maybe when we took away the heat, it sped up the reaction rate.
...e substances at 37.5̊C due to the fact that in the previous experiment, this was found to be the optimum temperature that catalase reacts at. It was because of this constant that I used the set of data of the catalase at 37.5̊C from the first experiment to provide a neutral environment for the experiment. The way in which the data was collected for the first experiment was identical to that needed to be done by the second. From this data, it was determined that the neutral environment for the catalase had the best results, which makes it clear that when the enzyme is in a pH of the opposite extremes such as basic or acidic, it is un able to function properly. When it is too basic then the enzyme will become inactive and when the enzyme is too acidic then the enzyme will denature, both rendering it unable to function at its optimum efficiency that all enzymes need.
6. The inhibitor slowed and almost stopped the reaction rate. The inhibitor was able to bind to the enzymes active site and made it hard for it to catalyze a reaction with peroxide.
Investigating the Effect of Enzyme Concentration on the Hydrolysis of Starch with Amylase Aim: Investigate the effect of enzyme concentration on the rate of an enzyme-controlled reaction. Using amylase and starch as my example. Introduction: I am investigating the effect of the concentration of the enzyme, amylase on the time taken for the enzyme to fully breakdown the substrate, starch to a sugar solution. The varied variable will be the concentration and all other variables are going to be fixed. The different concentrations will be: 0.5% 0.75% 1.0% 1.5% 2% An enzyme is a class of protein, which acts as a biological catalyst to speed up the rate of reaction with its substrates.
The efficiency of enzymes depends on a number of factors, such as temperature, pH and the concentration of the enzyme just to name a few. This experiment was conducted to show the effects of different pH levels on the activity of the catalase enzyme, the data obtained in this experiment supports the initial hypothesis of the experiment which states that the catalase enzyme will function optimally at a pH of 7 and efficiency will decrease as the pH of solutions moves further away from 7. This is true because in the experiment the test tube containing the distilled water which has a pH of 7, produced the highest amount of foam out of the four test tubes. The efficiency of the reaction can be determined by the amount of foam (foam = oxygen, which is the result of the breaking down of the hydrogen peroxide molecule into water and oxygen) produced, or the level of the fizzing that takes place when hydrogen peroxide is added. The pH of a solution that an enzyme has to function in is very important because if the pH turns out to be too low or too high the enzyme will denature making it unable to function, however, the pH of a solution may be far from the neutral level of 7 but the enzyme might not fully denature which means that the enzyme catalase would not lose its catalytic ability completely whereas a fully denatured enzyme’s shame will have been altered completely causing the active site and substrate to not fit together the way they’re supposed to. In certain reactions, the active site and enzyme substrate are still able to fit together which means that the reaction will continue to take place but at a very low rate, this seemed to be the case in one of the test tubes during the experiment. The foam produced in the react...
Enzymes are catalytic proteins that speed up biochemical reactions. Most enzymes are composed of proteins, while in some cases they are composed of RNA molecules called ribosomes. Enzymes are highly specific. Each enzyme catalyzes only one chemical reaction.
Our bodies involve and require many different biochemical reactions, which is achieved through the help of enzymes. Enzymes are proteins in our bodies that act as catalyst as they speed up vital biochemical reactions by reducing the “activation energy” needed to get the reaction going. To sustain the biochemistry of life, enzymes maintain temperature inside our living cells balanced and the concentration of reaction molecules. Enzymes are extremely efficient because they remain remarkably unchanged, therefore have the potential to be used over and over again. They are extremely specific with the reactions they catalyze, like a lock and key and, extremely reactive. The molecule to which enzymes make accelerated changes to is the substrate. The molecule that is present after the enzyme-catalyzed reaction is the product. Most enzymes require specific environmental conditions such as temperature and pH levels to be met in order for them to function properly and efficiently. In the first part of the lab we specifically examined a simple enzyme-catalyzed reaction using catechol (the substrate) which will be catalyzed by the enzyme catecholase and will then result in color change. This familiar color
In our body, chemical reactions are happening constantly. Now, how are the chemical reactions in our body able to occur quickly, to massly create the needed materials such as energy, to support our every second need? Enzymes! Enzymes are proteins that speed up chemical reactions in our body. Our goal for this lab was to see if the change in pH level or temperature would affect the rate of enzyme activity. To do this experiment we had to first find a way to use enzymes. We had chose potato puree to act as our subject to experiment with, since it contained catalase, which is an enzyme. To actually see the rate of enzyme activity, we decided to mix the potato puree with hydrogen peroxide. The reason behind that was because catalase breaks down
The Electrolysis of Copper Sulphate Aim Analyse and evaluate the quantity of Copper (Cu) metal deposited during the electrolysis of Copper Sulphate solution (CuSo4) using Copper electrodes, when certain variables were changed. Results Voltage across Concentration of solution electrode 0.5M 1.0M 2.0M 2 5.0 10.6 19.5 4 10.5 19.8 40.3 6 14.3 26.0 60.2 8 15.2 40.4 80.3 10 15.0 40.2 99.6 12 15.1 40.0 117.0 Analysing/Conclusion The input variables in this experiment are; concentration of the solution and the voltage across the electrodes. The outcome is the amount of copper gained (measured in grams) at the electrodes. By analyzing the graph, we can see the rapid increase of weight gained for the 2.0 molar concentration as the gradient is steeper.
The 6ml ½ strength stock solution was used for this experiment for dilution. That created the serial dilutions of (undiluted) full strength, ½ strength, ¼ strength, and 1/8 strength. 1 ml of the enzyme was added to each of the 4 spec tubes when ready to start recording enzyme concentration. Readings were recorded every 60 seconds for 5 minutes. After having the readings, the reaction rate was determined by using the following formula: (final absorbance- initial absorbance)/ time. From the first three minutes was how reaction rate was determined. Lastly, a graph was made to distinguish the change in reaction rate versus the concentration of the enzyme. Part 3 required similar steps as part 2, however, in the start of the dilution was a 0.024M catechol solution. This serial dilution required 5 tubes because the dilutions are to result in five different concentrations up to 1/16 strength of the catechol. Once the strengths in the regular tubes were added respectively to their spec tubes, immediate recordings of absorbance was done to each of the 5 spec tubes every 60 seconds for 5
To study the effect of substrate concentration on the activity of the enzyme catalase, which is found in living tissues and cells. In this experiment we will obtain catalase from yeast cells. The substrate will be hydrogen peroxide (H202), which vary concentrations from 1-10%. We will measure the rate of reaction by the volume of oxygen (02) released into the water.
In this experiment, researchers used different measurements of catechol and 1cm of potato extract. Researchers hypothesized that the increase in substrate would level out the enzyme activity by