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Discussion on investigating the effect of amylase concentration on its activity
Investigating the effect of temperature on enzyme activity
Investigating the effect of temperature on enzyme activity
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Experiment to Demonstrate the Action of Amylase on Starch Solution
Plan
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Scientific knowledge: Substances called catalysts speed up many
chemical reactions. Catalysts called enzymes control the metabolic
reactions in the body. Amylase is an enzyme; it is present in the
digestive systems of many animals. Amylase speeds up the breakdown of
long chain starch molecules. I know that the more common enzymes work
best at around 37.c as this is our natural body temperature. If this
temperature begins to rise the reactions slow down, this will continue
to happen until the enzyme is denatured. It becomes denatured at
around 60.c, this happens because the enzyme becomes misshapen. This
means that the enzyme will no longer work because it will no longer
fit. When the two join then you get the chemical reaction.
Preliminary work: I watched someone else do this experiment and saw
how it was to be done. This helped me see how the experiment worked
and how to do things correctly. I have studied enzymes so this has
helped me understand what is happening.
Apparatus.
2 test tubes
test tube rack
Timer
3 Pipettes
2 syringes
Dotted tile
Starch solution
Amylase
Iodine solution
Thermometer
Bunsen burner
Tripod
Gauze
Water bath
Procedure
[IMAGE][IMAGE][IMAGE][IMAGE][IMAGE]Two drops of iodine solution is put
into each of the dimples.
[IMAGE][IMAGE][IMAGE][IMAGE]
Two drops of starch solution are put into the first
[IMAGE][IMAGE][IMAGE][IMAGE] dimple as a control.
10ml of starch solution and 1ml of amylase is measured using the
syringe. The Starch is put into a test tube, and then the amylase is
added, and the stop clock is
immediately started. With a pipette, 3 drops of the starch and amylase
solution are added to each dimple every thirty seconds. When the
solution has turned back to the original colour of the iodine solution
the stop clock is stopped. I will take 8 results and repeat all of
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
Iodine turns into a blue/black color when in the presence of starch, after using iodine if the blue/black color is absent then the starch has been used usually making a halo around the inoculum, resulting in a positive result. If it stays blue/black then the starch is still present meaning the organism cannot produce amylase causing a negative result. My color stayed blue/black and there was no evidence of a halo, meaning my organism is negative for producing amylase. (handout, amylase)
and this is a result of over production of H O . Although Hydrogen Peroxide left alone will eventually break down, Catalase will speed this reaction up a lot faster therefore in those circumstances it is inserted into the body. Hydrogen Peroxide broken down will produce Water and Oxygen. In our experiment the independent variable is the concentration of the Catalase Enzyme.
The optimal temperature appears to be slightly above room temperature for this enzyme. The reaction occurred more slowly at lower temperatures because the particles in the solution are slowing down and aren’t colliding as frequently, in the higher temperatures it slows down because the enzyme is getting denatured, this effect becomes larger as temperature increases.
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
I blanked it with 2 cm³ water, 1 cm³ amylase and 3 drops of iodine.
+ 2I¯ (aq) + H[-1] 2O2 (l) ÕI2 (aq) + 2H2O2 (aq) Iodide ions are firstly oxidised by the hydrogen peroxide, as shown in the above equation. The iodine that is then produced reacts immediately reacts with thiosulphate ions as follows: I2 (aq) + 2Na2S2O3 (aq) Õ 2NaI (aq) + Na2S406 (aq) As soon as all of the thiosulphate ions have reacted with the iodine, the excess iodine molecules react with the 2% starch solution that is present in the reaction. This can be seen as an instant change in colour, from a colourless solution, to a deep purple coloured solution. This change in colour denotes the completion of the reaction. Factors affecting the rate of reactions: All chemical reactions occur at a definite rate under particular conditions.
Purpose: This lab gives the idea about the enzyme. We will do two different experiments. Enzyme is a protein that made of strings of amino acids and it is helping to produce chemical reactions in the quickest way. In the first experiment, we are testing water, sucrose solution, salt solution, and hydrogen peroxide to see which can increase the bubbles. So we can understand that enzyme producing chemical reactions in the speed. In the second experiment, we are using temperature of room, boiling water, refrigerator, and freezer to see what will effect the enzyme.
The reason for this is that the energy being supplied to the enzyme begins to effect its stability. The energy supplied begins to make the atoms which make up the enzyme move and vibrate rapidly, at a certain point the enzyme atoms are vibrating at such a rate that the bonds that hold the active site together, such as the disulphide and hydrogen bonds are broken and the shape of the active site changed. This is vital as the Hydrogen peroxide substrate can no longer bind with the catalase enzyme and react. The activity of the catalase is dependent on the balance of increasing
Flannery O'Connor's short story "A Good Man is Hard to Find", is an example of Southern Gothic literature. This style according to dictionary.com is defined as, "a literary genre depicting life in the southern U.S. and featuring grotesque themes and imagery", or according to Professor Lupold Moody of the University of Montana, "In order to be Southern Gothic, the story must be set in the American South and have gothic characteristics (supernatural, ironic, or unusual events often guide the plot) that usually attempt to explore the social and cultural character of the South". In this story what begins as an account of a family planning a trip to Florida and the description of this journey once they leave their Georgia home, ends in the appalling death of this entire family. The qualities inherent in Southern Gothic literature are fulfilled in this work. Rather than a short story written simply as a quick read with a shock at the end, on deeper analysis this story points out flaws in the human race and peoples' capacity for change. Foreshadowing and characterization are two literary devices used effectively by O'Conner in her short story "A Good Man is Hard to Find", not only to build suspense, but to reveal weaknesses of the human race while still giving a small sliver of hope that people are able to change.
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.
However, in order to measure the rates of reaction, sodium thiosulphate and starch are added. Sodium thiosulphate is added to react with a certain amount of iodine as it is made. Without the thiosulphate, the solution would turn blue/black immediately, due to the iodine and starch. The thiosulphate ions allow the rate of reaction to be determined by delaying the reaction so that it is practical to measure the time it takes for the iodine to react with the thiosulphate. After the all the thiosulphate has reacted with the iodine, the free iodine displays a dark blue/black colour with the starch. If t is the time for the blue/black colour to appear, then 1/t is a measure of the initial rate.
If I was to do this experiment again I might use a Fungi amylase to
For my preliminary work, I used a 50 mm piece of potato. It was easy