Wait a second!
More handpicked essays just for you.
More handpicked essays just for you.
Rate of a chemical reaction using enzymes
Investigating enzyme reaction rate
Don’t take our word for it - see why 10 million students trust us with their essay needs.
Recommended: Rate of a chemical reaction using enzymes
Investigating the Rate of Reaction between Amylase and Starch
Plan
Aim:
The aim of this investigation is to find out whether the volume of
amylase affects the rate of reaction between amylase and starch.
Prediction:
I predict that the greater the volume of amylase then the faster the
rate of reaction between the starch and amylase will be. I predict
this because of the lock and key hypothesis. The lock and key
hypothesis explains how the substrate molecule (the starch) fits
inside the enzyme. The substrate molecule is then broken up into many
smaller pieces.
In this experiment the larger the volume of amylase (enzyme/active
site) there is then the quicker the starch (substrate) will be broken
down, resulting in a fast reaction rate. Therefore, a smaller amount
of amylase will result in a slower reaction rate.
[IMAGE]
Text Box: Fischer’s ‘Lock and Key’ hypothesis (1890). Sequence of events when the union of a substrate with its enzyme occurs.
Preliminary Work:
The preliminary work was carried out to find a suitable range to
collect data in. From the preliminary work I was able to determine
suitable intervals of time to collect data. It showed that a volume of
amylase below 4cm³ took a very long time to react thus making the
experiment take too long. From this I worked out that I should start
at a volume of 4cm³. The preliminary work also proved to me that my
basic method worked without any set backs that may affect my results.
Variables:
The variables involved in the rate of reaction between amylase and
starch are:
The volume of amylase
The volume of starch
The temperature of amylase
The temperature of starch
Room temperature
Concentration
Ph values
The variable I will be changing is the volume of amylase.
Safety:
To make sure I carry out this experiment safely I will make sure I
wear goggles. I will ensure I keep my stool under the table and all
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
For example, substrate concentration, enzyme concentration, and temperature could all be factors that affected the chemical reactions in our experiment. The concentration of substrate, in this case, would not have an affect on how the bovine liver catalase and the yeast would react. The reason why is because in both instances, the substrate (hydrogen peroxide) concentration was 1.5%. Therefore, the hydrogen peroxide would saturate the enzyme and produce the maximum rate of the chemical reaction. The other factor that could affect the rate of reaction is enzyme concentration. Evidently, higher concentrations of catalase in the bovine liver produced faster reactions, and the opposite occurs for lower concentrations of catalase. More enzymes in the catalase solution would collide with the hydrogen peroxide substrate. However, the yeast would react slower than the 400 U/mL solution, but faster than the 40 U/mL. Based on this evidence, I would conclude that the yeast has a higher enzyme concentration than 40 U/mL, but lower than 400
This evidence alone suggests that higher increases in substrate concentration causes smaller and smaller increases in enzyme activity. As substrate concentration increases further, some substrate molecules may have to wait for an active site to become empty as they are already occupied with a substrate molecule. So, the rate of the reaction starts to level off resulting in a plateau in the graphs. This means that the reaction is already working at its maximum rate, and will continue working at that rate until all substrates are broken down. The only way the reaction rate would increase, is if more enzyme was added to the solution. This confirms that increases in substrate concentration above the optimum does not lead to greater enzyme activity. Therefore, the rate of reaction is in proportion to the substrate
called an active site. This active site is made by a few of the amino
The rate law determines how the speed of a reaction occurs, thus allowing the study of the overall mechanism formation in reactions. In the general form of the rate law, it is A + B C or r=k[A]x[B]y. The rate of reaction can be affected by the concentrations such as A and B in the previous equation, order of reactions, and the rate constant with each species in an overall chemical reaction. As a result, the rate law must be determined experimentally. In general, in a multi-step reaction, there will be one reaction that is slower than the others.
Abstract: Enzymes are catalysts therefore we can state that they work to start a reaction or speed it up. The chemical transformed due to the enzyme (catalase) is known as the substrate. In this lab the chemical used was hydrogen peroxide because it can be broken down by catalase. The substrate in this lab would be hydrogen peroxide and the enzymes used will be catalase which is found in both potatoes and liver. This substrate will fill the active sites on the enzyme and the reaction will vary based on the concentration of both and the different factors in the experiment. Students placed either liver or potatoes in test tubes with the substrate and observed them at different temperatures as well as with different concentrations of the substrate. Upon reviewing observations, it can be concluded that liver contains the greater amount of catalase as its rates of reaction were greater than that of the potato.
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:
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.
However, the decrease varied depending on the temperature. The lowest temperature, 4 degrees Celsius, experienced a very low decrease of amylose percentage. Temperature at 22 degrees Celsius and 37 degrees Celsius, both had a drastic decrease in amylose percentage. While the highest temperature, 70 degrees Celsius, experienced an increase of amylose percentage. In conclusion, as the temperature increases the percentage of amylose decreases; however, if the temperature gets too high the percentage of amylose will begin to increase. The percentage of amylose increases at high temperatures because there is less enzyme activity at high temperatures. However, when the temperature is lower, more enzyme activity will be present, which results in the decrease of amylose percentage. This is why there is a decrease of amylose percentage in 4, 22, and 37 degrees Celsius. In this experiment the optimal temperature is 37 degrees Celsius, this is because this is the average human body temperature. Therefore, amylase works better at temperatures it is familiar
The temperature of the reaction, as some of the energy produced converts into heat energy. At really high temperatures the reaction will stop because the heat will have denatured the enzymes.
With this information we were able to identify any patterns and similarities. Hypothesis: The higher the temperature of water, potato and H²O², the rate at which the Enzyme will work will be faster therefore producing more oxygen. The reaction will be the same without the catalase (potato). Therefore in both experiments the Enzyme will work more rapidly and produce more oxygen. Aim: To test the hypothesis.
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.
Reaction Rate Investigation Planning I am trying to work out the rate of reaction between marble chips (calcium carbonate) and Hydrochloric acid. This will be my plan of how to carry out my investigation. There are many factors, which I could change in this experiment. These are 1) Concentration. An increase in concentration means there are more particles.
and a fall in temperature will slow them down. In many cases a rise in