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Effect of substrate concentration on enzyme activity spectrophotometry
Amylase activity + ph
Strengths and weaknesses of amylase
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The Effects of Enzyme Concentration on the Activity of Amylase
To investigate the effect of Amylase concentration on its activity.
the relative activity of Amylase is found by noting the time taken for
the starch substrate to be broken down, that is, when it is no longer
gives a blue-black colour when tested with iodine solution. This time
is referred to as the achromatic point.
Equipment:
v Amylase solution 0.1%
v Starch Solution 1.0%
v Distilled water
v Iodine in potassium iodine solution
v White tile and polythene pipette
v Graduate pipettes or syringes
v Test tubes in rack
v Beaker (used as water bath)
v Stopwatch, Thermometer
v Eye Protection
Method:
1) Wear your eye protection
2) Prepare five different concentrations of the enzyme solution:
undiluted,¾ diluted, ½ diluated, ¼ diluted, 1/10 diluted, and a
control
3) Set up water bath 40°c.
4) Pipette 5cm³ of the undiluted enzyme solution into one test tube
and 5cm³ of starch solution into another test tube. Stand both tubes
in the water bath and leave for several minutes to reach the
temperature of the water bath.
5) Mix the enzyme and starch solution together, replace the mixture
in the water bath and immediately start stopwatch.
6) At intervals of 1 minute, remove drop of the mixture and test it
with iodine solution on a white tile.
7) Continue the experiment until the mixture fails to give a
blue-black colour with iodine solution. Record this as the achromatic
point .
8) Repeat this procedure with the other concentrations of amylase.
Use exactly 5cm³ of enzyme solution and 5...
... middle of paper ...
...ation the faster it takes for the enzymes which is
the amylase concentration to break down the starch in the solution.
Evaluation:
If I was to do this experiment again I might use a Fungi amylase to
see if its results is different. I also have no anomalous results, but
if I did have any anomalous results I would try and find out how it
came about the possibilities are that could have not measured the
amylase concentration and the starch solution correctly, the
temperature was not the same throughout the experiment. The higher the
concentration of amylase the quicker the reaction between the amylase
and starch occurs because it has a higher concentration on the same
volume of starch therefore the more amylase concentration the
different times it takes to breaking down the same amount of starch
(achromatic point.
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
The sand is If the water with Alka-Seltzer tablets is stirred during the reaction, then the rates of reactions will increase because the particles will be forced to make contact with each other and... ... middle of paper ... ...results anomalies because they are the outcome of dissociation of calcium and magnesium ions,. Evaluation: What is the difference between My results were very reliable, because by looking at my graphs I can see a trend that relates to my scientific background. It is also evident that I have obtained a reliable set of results when I see that.
Even though the hypothesis was correct the experiment could be improved. If time had allowed longer tests could have been used. This would prove or disprove the idea that peppermint or Big Red would help aid with fatigue. Also, this test would be more realistic because most are not only two minutes long.
called an active site. This active site is made by a few of the amino
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: = == ==
Investigating the Effect of Substrate Concentration on Catalase Reaction. Planning -Aim : The aim of the experiment is to examine how the concentration of the substrate (Hydrogen Peroxide, H2O2) affects the rate of reaction. the enzyme (catalase).
I blanked it with 2 cm³ water, 1 cm³ amylase and 3 drops of iodine.
The purpose of this investigation is to test the effects of multiple sugar substances on the respiration of yeast. Most people think of yeast when they think of what makes bread rise, cheese, alcoholic beverages, or other food products. Another type of yeast can also cause yeast infections, an infection of the skin. Yeasts (Saccharomyces) are tiny, microscopic organisms with a thin membrane and are usually oval or circular-shaped. They are a type of single-celled fungi of the class Ascomycetes, capable of processing sugar into alcohol and carbon dioxide (CO2 ) ; this process is known as fermentation. Fermentation and the products are the main focus points for this experiment being that cellular respiration of yeasts happens via the process of fermentation, which creates by-products of alcohol and CO2. The level of CO2 produced by the yeasts will show how effective each sugar substance is in providing cellular energy for the yeasts.
== Refer to Chemistry Lab # 2 – Investigating Changes. No changes have been made in this experiment. Results = ==
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.
.... All things considered, this experiment was conducted as well as it could’ve been, unavoidable errors and all. Even still, there are still things that could be discovered throughout this topic.
The Effect of pH on Enzyme Activity. pH is a measure of the concentration of hydrogen ions in a solution. The higher the hydrogen ion concentration, the lower the pH. Most enzymes function efficiently over a narrow pH range. A change in pH above or below this range reduces the rate of enzyme reaction. considerably.
However, a strange phenomenon has occurred,
Now that you know what my situation was like going into the experiment, I will tell you what I did and what occurred as a result.