How Does Amylase Affect The Rate Of Reaction

In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or

Step 1: Label the test tubes 1, 2, 3 and 4, where test tube 1 represents the sample placed on the counter at room temperature, test tube 2 represents the tube placed in the refrigerator, test tube 3 represents the tube placed in the freezer, and test tube 4 represents the sample exposed to boiling water. You will expose catalase to each of these four conditions.

Amylase experiment # 2 was done to see how the pH affected the efficacy of the enzyme. First we collected all of the materials that were necessary to make this experiment. We needed five clean test tubes, the following standard solutions, 1% Starch Solution pH 3,1% Starch Solution pH 5,1% Starch Solution pH 7,1% Starch Solution pH 9,1% Starch Solution pH 11

Students will be observing normal catalase reaction, the effect of temperature on enzyme activity, and the effect of pH on enzyme activity in this experiment. The enzymes will all around perform better when exposed in room temperature than when it is exposed to hot and cold temperatures. This is based on the fact that the higher the temperature, the better the enzymes will perform, but as the temperature reaches a certain high degree, the enzymes will start to denature, or lose their function.

Lab six requires students to observe the effects of pH and enzyme concentration on catecholase activity. Enzymes are organic catalysts that can affect the rate of a chemical reaction depending on the pH level and the concentration of the enzyme. As pH comes closer to a neutral pH the enzyme is at its greatest effectiveness. Also at the absorbance of a slope of 0.0122 the enzyme is affected greatly. The pH effect on enzymes can be tested by trying each pH level with a pH buffer of the same pH as labeled as the test tube and 1mL of potato juice, water, and catechol. This is all mixed together and put in the spectrophotometer to test how much is being absorbed at 420nm. As the effect on enzyme concentration can be tested almost the same way. This part of the exercise uses different amounts of pH 7-phosphate buffer and potato juice, and 1mL of catechol mixed together in a test tube. Each substance is put in the spectrophotometer at a wavelength set tot 420nm. The results are put down for every minute up to six minutes to see how enzyme concentration affects reaction rate. The results show that the pH 8 (0.494) affects the enzyme more than a pH of 4 (0.249), 6 (0.371), 7 (0.456), and 10 (0.126). Also the absorbance is greatest at a slope of 0.0122 with test tube C that has more effect on the reaction rate, than test tube A, B, and D.

An experiment was performed to test how temperature variations affect enzymatic activity of the enzyme amylase. The results of the experiment will also determine the optimal temperature of the amylase enzyme. The results of the experiment provide evidence for determining the environments that the enzyme amylase would most likely be present. By determining the possible environments, one can predict what and how environmental factors will affect the enzyme amylase. Two forms of amylase (Bacterial - Bacillus licheniformis and Fungal - Aspergyllus oryzae) were combined with starch molecules at four different temperatures (0⁰, 25⁰, 65⁰, 85⁰ Celsius). The combination of starch and the amylase enzyme resulted in a visual chemical reaction that was recorded. The enzyme activity was recorded every two minutes, starting at 0 and ending at 10. The start time 0 served as the control group of the experiment. The results concluded that both bacterial and fungal amylase has an optimal temperature around 65⁰C. This was possible to determine by recording the color change of the spot plate wells. Amylase catalyzes efficiently at its optimal temperature which resulted in yellow spot plate wells. Enzymatic activity decreased when the temperature was less than 65⁰C, resulting in a green-brown well. The green wells indicated that starch wasn’t broken down completely and was still present. Temperatures greater than 65⁰C resulted dark-green wells which resembled the denaturing of

enzymes that will be used during this lab to test the ability of amylase to break down starch ,a

test the pH of the amylase a drop of the solution should be put on pH

Enzymes are biological catalysts that lower the activation energy required for a reaction to take place. They speeds up the process of the reaction, while still not being consumed, they can function multiple times. Enzymes are specific to molecules or sets of molecules and only work with these specific substrates. The enzymes cause substrates to be converted to products faster than they would without enzymes. A substrate fits into an enzyme, which then catalyzes the conversion of the substrate into products. The enzyme facilitates reactions, however it can become denatured. When an enzyme is denatured its form changes, thus preventing its function of converting substrates to products faster, and the enzyme does not work. The enzyme used in this experiment is amylase. Amylase is an enzyme that catalyzes the breakdown of the polysaccharide starch into the disaccharide maltose. Amylase is produced by human salivary glands and aids in digestion and breaking down food substances.

This experiment consisted of setting up a control group of starch in various temperature and then placing both fungal amylases and bacterial amylases in a mixture of starch and placing the solution of amylase and starch in various temperatures of water. After a certain amount of time- different amount of time needs to be used in order to have reliable results- iodine is added in a well on spot plates, then two drops of the mixture of amylase-starch is added from each temperature used, by adding iodine into the plates the mixture will show how much starch was hydrolyzed, this is used to calculate the amount of

Amylase is an enzyme that is located in human saliva. It is solely accountable for breaking down starch as a way to start the breakdown of food and is one of the first steps of digestion. The time at which the enzyme starts the chemical reaction with starch is called the reaction rate. In order to study how amylase works against starch, this experiment consisted of two tests; each testing a different condition of amylase. The first test was to simply study the reaction between saliva and amylase and note the reaction rates. The second test was to see if increasing the pH would decrease the reaction rate or halt it all together. Saliva was collected, diluted, and tested for reactions between starch and amylase. Another sample of saliva was collected, diluted, and had its pH increased and tested for reaction rate. The findings after the experiment was conducted aligned with the original hypothesis. The change in pH did show a significant decrease in the reaction rate.

Enzymes take care of catalysis in living organisms. They are used mainly for commercial uses for example, to produce sugars. Throughout the experiment, bacterial amylase, Bacillus lichenifomis, and fungal amylase, Aspergillus Oryzae, were being tested in order to determine the optimal point of the temperature for the respective amylase. The optimal temperature is the temperature at which the enzyme works best. In order to determine the break down of starch, the mixing of amylase with starch would occur. With the help of iodine as an indicator, it could be noted which temperature was the optimum. The outcome showed that for the bacterial amylase, hydrolysis worked best at 55 degrees Celsuis. As for the fungal amylase, hydrolysis worked best at 25 degrees Celsius. As the temperature passed its optimal point, the enzyme would denature or change shape,3 due to the change in the environment. This can be seen with the color changes. Where hydrolysis worked best, it had a bright yellow color as seen in Figure 1. When the enzyme would denature, the color would change to black as seen in Figure 2. All in all, the experiment proved to be successful although there may have been possible sources of

In this lab our group observed the role of pancreatic amylase in the digestion of starch and the optimum temperature and pH that affects this enzyme. Enzymes are located inside of cells that increase the rate of a chemical reaction (Cooper, 2000). Most enzymes function in a narrow range of pH between 5 through 9 (Won-Park, Zipp, 2000). The temperature for which enzymes can function is limited as well ranging from 0 degrees Celsius (melting point) to 100 degrees Celsius (boiling point)(Won-Park, Zipp, 2000). When the temperature varies in range it can affect the enzyme either by affecting the constant of the reaction rate or by thermal denturization of the particular enzyme (Won-Park, Zipp, 2000). In this lab in particular the enzyme, which was of concern, was pancreatic amylase. This type of amylase comes from and is secreted from the pancreas to digest starch to break it down into a more simple form called maltose. Maltose is a disaccharide composed of two monosaccharides of glucose. The presence of glucose in our experiment can be identified by Benedicts solution, which shows that the reducing of sugars has taken place. If positive the solution will turn into a murky reddish color, where if it is negative it will stay clear in our reaction. We can also test if no reduction of sugars takes place by an iodine test. If starch is present the test will show a dark black color (Ophardt, 2003).

In this lab we looked at the role of pancreatic amylase in the digestion of starch and the effect that temperature and pH has on this enzyme. Enzyme’s work as catalysts that increase the rate of chemical reactions within cells (Cooper, 2000). In order to do this, enzymes must show two essential properties: these two fundamental properties of enzymes include increasing the rate of chemical reactions without being eternally altered by the reaction and accelerating the reaction rate with keeping the reactants and products in chemical equilibrium (Cooper, 2000). Enzymatic catalysis is necessary for life. Most biochemical reactions would not occur under the mild temperatures and pressures

According to Oxford Dictionary, metabolism is the set of chemical processes that occur within a living organism in order to maintain life. From these processes, organisms are allowed to develop and reproduce, maintain their structures, and respond to their environments. Metabolism is usually divided into two categories, which are catabolism- breaks down large molecules and anabolism- uses the energy to construct components of cells. The role of metabolism is to deploy starch or lipids stored in endosperm so the germination can take place. Thus, the energy was formed (catabolic) and new plant material as the seed germinates was synthesised (anabolic). The aim of the experiment was to enucleate amylase from barley and utilizing it for the catalyst of a biochemical reaction thus investigating throughout seed sprout the activity of amylase. Before the experiment, it is hypothesized that the higher the activity of amylase, the higher the sprout rate of seed. How high and radicle change in length can be used to observe this case. Therefore, when Benedict’s test is carried out, the solution is still blue for the inactive seed and the concentration of brick-red precipitate plants growing from seeds.