Investigating the Temperature at Which Soap Powder Will Perform Best At
Introduction
I am going to conduct an experiment in the controlled environment of a
laboratory. The experiment will consist of placing a stained piece of
fabric into water with a fixed concentration of a biological washing
powder (Wizzo) in it. I will try this experiment several times trying
different temperatured water and leaving the it for a fixed period of
time to find the best possible temperature that the Wizzo works at.
Plan: Enzymes
Biological washing powder has bin around for many years to clean
clothes more efficiently. We know washing powder helps in the cleaning
process because it contains enzymes. Previous experiments have found
that the enzymes break down larger dirt molecules into smaller dirt
molecules. Therefore speeding up the process of cleaning clothes
(catalyse) as the water can wash them away quicker.
Another example of enzymes is the digestive system in the human body.
Enzymes called protease are produced by the stomach, the pancreas and
the small intestine. These enzymes catalyse the break down of fatty
acids into amino acids. These enzymes work best at 37 degrees celsius
whcih is body temperature.
Formalahdehyde is the enzyme which is commonly found in biological
washing powder. The enzymes break down the dirt molecules in clothes
into smaller dirt molecules thus making it easier for the water to
clean away. I will determine at what temperature the enzymes in the
Wizzo best perform at, which is the point of my experiment.
Hypothesis
I predict that 40 degress celcious will be the most effective at
cleaning the st...
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...s of stained fabrics I could
use therefore limiting the amount of times I could repeat each
temperature. Also some of the fabrics were not made out of the same
material and therefore may influence the time in which it takes to
clean it making the test void or unreliable.The size of the stains
also varied also making the test unreliabledue to it will also take an
untrue time to remove the stain in the sane concentration of solution.
To obtain more reliable results I would repeat the experiment more
times (about ten times for each temperature) to get a broader range of
results for the average.
To extend the experiment further I would conduct the same experiment
using lower temperatures to be able to copmile the results from this
experiment to get a broader range as it seems the Wizzo will be more
effective again.
Then, repeat steps 7-11 another 4 times but with the room temperature water. For the room temperature water just leave it in the room but try not to change the room’s temperature. 15. Try to put all your recorded data into a table for organization 16. Repeat the entire experiment for more reliable data.
The rate at which Alka-Seltzer tablets reacts with water Statement of problem The aim of the experiment is to find out the rate at which Alka-Seltzer tablets react with water. The input variable that I will change is temperature. The output variable will be measured by the time it takes for the Alka-Seltzer tablets to dissolve.
5.) One at a time, place your test tubes in the water bath and heat the first test tube to 25 , the second to 50 , the third to 75, and the last to 100 degrees c. Remeber to stir with your stirring rod every so often.
Thermal methods of analysis have been in use for quite a long time. Their application in the analysis of pharmaceutical materials has made it possible for pharmacists and researchers to understand their contents and characteristics. However, thermal methods have several disadvantages that have led researchers to opt for nano-thermal methods of analysis. Nano-thermal analysis methods use special resolution imaging potential that is enhanced by the availability of atomic force microscopy and thermal analysis methods.
There is an optimum temperature that enzymes have for maximum productivity and its rate of reaction. This temperature is usually not that far away from the temperature of the body or room temperature. But, when the temperature is substantially reduced, like being in the ice bucket for ten minutes, this usually reduces the productivity of the enzymes. Similar to the experiment, it takes more time for the same amount of work when the temperature is severely decreased. So, an increase in temperature increases the reaction rate of enzymes. But, there is also an upper limit to the factor of temperature. After a certain temperature, the extreme heat can be harmful for the enzymes and can cause denaturation, as bonds in the enzymes can break and can change the shape of the enzyme. So, extreme low and high temperatures has a decreasing effect on the activity and reaction rate of
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.
When molecules bump into each other, the kinetic energy that they have can be converted into chemical potential energy of the molecules. If the potential energy of the molecule becomes great enough, the activation energy of a reaction can be archived and a change in chemical state will result. Thus the greater the kinetic energy of the molecules in a system, the greater the resulting chemical potential energy. As the temperature of a system is increased it is possible that more molecules per unit time will reach the activation energy (2). Therefore the rate of reaction will increase. On the other hand if the temperature reaches a certain amount the enzyme might denature and therefore no longer able to carry out the reaction.
One of the most common methods for discovering and collecting latent fingerprints is by dusting a smooth or nonporous surface with fingerprint powder (black granular, aluminum flake, black magnetic, etc.). If any prints appear, they are photographed as mentioned above and then lifted from the surface with clear adhesive tape. The lifting tape is then placed on a latent lift card to preserve the print.
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...
The exocrine function of the pancreas is that it produces enzymes that aids in the digestion of food. There are three important enzymes that are crucial in helping with digestion. The first digestive enzyme is amylase. Amylase function is to break down carbohydrates. The amylase enzyme is made in two places: the cells in the digestive tract that produces saliva and the main one specifically found in the pancreas that are called the pancreatic amylase (Marie, Joanne; Media Demand, “What Are the Functions of Amylase, Protease and Lipase Digestive Enzymes”). The amylase in the pancreas passes through the pancreatic duct to the small intestines. This amylase in the pancreas completes the process of digestion of carbohydrates. Consequently, this leads to the production of glucose that gets absorbed into the bloodstream and gets carried throughout the body. The next enzyme that aids in digestion of food is protease. While amylase breaks down carbohydrates, protease breaks down protein. Protease breaks down protein into the building block form of amino acids. The three main proteases that it produces are: pepsin, trypsin and chymotrypsin (Marie, Joanne; Media Demand, “What Are the Functions of Amylase, Protease and Lipase Digestive Enzymes”). Pepsin does not occur in the pancreas but it is the catalysis in starting the digestion of proteins. Trypsin and chymotrypsin are the two proteases that occur in
take about 30 minutes for the water to cool down 20ºC, which is why I
In a 250ml beaker place 100mls of water, measure the temperature of the water and record this initial temperature onto a table. Set the timer and add one teaspoon of Ammonium Nitrate to the water, stir this continuously until the Ammonium Nitrate has dissolved. After 1 minute measure the temperature and record it, do this for a further 2 minutes (3 minutes in total). Repeat this process for a total of 10 teaspoons.
The preservation of food is essential to maintain life and growth. Its daily intakes nourish our bodies, providing enzymes, in turn giving us energy. The ability of matter exerts radiation in its domain by means of energy in selected foods. Such rationale debates whether a development of technology creates an effective way to reduce the incidence of foodborne diseases, while treating a variety of potential problems in our food supply. An effective method of research in food irradiation illustrates substantial evidence in its safety, nutritional adequacy, and social-economic global effects.
Detergent comes from the Latin word detergere meaning to clean, it is defined as a cleansing agent. Therefore, water itself is a detergent. This essay looks at soap and soapless (or synthetic) detergents. Both substances we use everyday and have a big market commercially, they effect everyone. Soaps are made from natural products and soapless detergents are produced chemically, each having advantages and disadvantages.
The type seen throughout the human body involve enzyme catalysis. Enzymes are present throughout many key bodily processes and keep the body from malfunctioning. An enzyme catalyzes a reaction by having the substrate bind to its active site.2 This is known as the Lock and Key Theory, which states that only the correctly oriented key (substrate) fits into the key hole (active site) of the lock (enzyme).2 Although this theory makes sense, not all experimental data has explained this concept completely.2 Another theory to better accurately explain this catalysis is known as the Induced-Fit Theory.2 This theory explains how the substrate determines the final form of the enzyme and shows how it is moderately flexible.2 This more accurately explains why some substrates, although fit in the active site, do not react because the enzyme was too distorted.2 Enzymes and substrates only react when perfectly aligned and have the same