Introduction Without enzymes, certain chemical reactions in our bodies would not able to occur. An enzyme is a special type of protein, called a catalyst, that speeds up chemical reactions by lowering the amount of energy needed to start a chemical reaction, known as the activation energy. Every enzyme has a specific reactant or reactants that it helps. These reactants, known as the substrates, lock onto the enzyme’s active site, which is where the chemical reaction occurs more efficiently than it would have without the enzyme. By lowering the activation energy, the chemical reactions are able to take place more efficiently. Amylase is a specific enzyme that breaks down starch into a smaller form, known as the sugar maltose. Amylase can be …show more content…
Add heat to the mixture just before it commences to boil, stirring periodically. Allow the heated mixture to cool down. The initial step of the experiment is to fill the 250-mL beaker with approximately ¾ (about 180-190 mL) full of water. Place this beaker on the hot plate for a boiling water bath later. The water should be kept at just boiling. Next, label the three test tubes A, B, and C. Spit saliva into the test tubes until there is a relatively sufficient amount, which is about 1-2 mL of saliva for each test tube. After, put two mL of vinegar into test tube A. Put two mL of distilled water in both test tubes B and C. Thump the tubes, or repeatedly pushing on it with the index finger, to let the solution mix together. Then, treat test tube B into the boiling water bath for five minutes. After the five minutes are over, remove the test tube from the bath and put it back onto the test tube rack. Next, put five mL of the starch solution to all three tubes and thump all the tubes to combine. Let the tubes sit for ten minutes, thumping the test tubes every now and then. Lastly, put in three mL of the Benedict’s solution to each test tube and thump the tubes. Treat all three test tubes to the boiling water bath. The Benedict’s solution reacting with the amount of maltose present in each test tube will take a few minutes to …show more content…
Since vinegar is a strong acid, it would have altered the pH of the solution. Changing the pH can prevent the amylase enzyme from efficiently converting the substrates into products. In this case, the substrate was the starch and the amylase enzyme was trying to break it down into simple maltose sugars. Since there weren’t many maltose sugars produced because of the denatured amylase enzymes, the Benedict’s solution tested negative and it showed a color of dark blue. For test tube B, distilled water was added and the tube was treated to a boiling water bath. The Benedict’s solution tested a very weak positive and showed a color of greenish-yellow. The weak positive means that the amylase enzymes were starting to get denatured because of the temperature change and lose their ability to produce simple maltose sugars. The enzyme is starting to lose its shape which affects its ability to perform the chemical reaction. So, the amylase was not able to fully break down all the starch into simple maltose sugars, only some of the starch. Since some of starch was broken down, there was some maltose present. For test tube C, only distilled water was added, so this was the control group. The amylase was not exposed to changes in pH or temperature, so the enzyme was able to efficiently do its job. That means most if not all of the starch was broken down into simple maltose sugars by the amylase, so when the Benedict’s solution was added, the result
Each subsequent trial will use one gram more. 2.Put baking soda into reaction vessel. 3.Measure 40 mL vinegar. 4.Completely fill 1000 mL graduated cylinder with water.
Repeat for each trial. Rinse volumetric pipette with vinegar and drain into the waste beaker. Weigh and record the mass of each 200mL beaker. Add 10.00mL of vinegar into each beaker and weigh them and record their again. Add 50mL of de-ionized water to the beakers and place them under the drop counter on top of a stir plate, submerging the pH meter into the solution. Place the stir bar into the beaker and carefully turn on the stir plate so that the stir bar spins without splashing or hitting the sides of the beaker or the pH
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: = == ==
4. Pour about 300mL of tap water into the beaker. Set up a hot-water bath using a hot plate, retort stand, and thermometer clamp. Alternatively, use a Bunsen burner, retort stand, ring clamp, thermometer clamp, and wire gauze.
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: The sand is To make sure I carry out this experiment safely I will make sure I wear a pair of goggles. I will ensure I keep my stool under the table and all
Enzymes have the ability to act on a small group of chemically similar substances. Enzymes are very specific, in the sense that each enzyme is limited to interact with only one set of reactants; the reactants are referred to as substrates. Substrates of an enzyme are the chemicals altered by enzyme-catalysed reactions. The extreme specific nature of enzymes are because of the complicated three-dimensional shape, which is due to the particular way the amino acid chain of proteins folds.
Our hypothesis was incorrect, the more concentration of sucrose the less the weight of the object becomes. If the experiment were to be performed once again, we could probably place the samples in the accurate solutions at the same time, this way there should be less differentiation in the weight of the samples. The effect of pH on Amylase Activity: The closer the pH is to neutral, the faster the rate of change will be. Our hypothesis was proven wrong, the pHs that were a lot faster at disappearing starch were the pHs that were closer to neutral 7, the pH7, averaging from zero, two, three, and five.
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.
This hurdle is called the activation energy of the reaction. [IMAGE] By decreasing the activation energy, more substrate is changed to product in a certain amount of time. That is, the enzyme increases the rate of the reaction. [IMAGE] The activity of catalase can be measured by finding the rate of which the oxygen gas is released from the breakdown of Hydrogen Peroxide.
I blended on high to make the potatoes more liquid-like. I grabbed the cheesecloth and placed on the top of the blender. I poured the potato extract on the container and labeled it. I found out that I have to make 1% sugar solution so I grabbed the sugar and measured into 5 grams on the scale. I added 5 grams of sugar on 250 ml graduated cylinder and poured the water into the cylinder. I mixed the sugar with water and poured it into the saucepan. I refilled the water into the graduated cylinder and poured into the saucepan. I turned on the heat of the stove and saw the sugar dissolved. I poured into a container and labeled 1% sugar solution. I repeated the same thing with 1% salt solution by using 1 gram of salt and filled the water into graduated cylinder by 100 ml. I answered question three. In the first experiment, I grabbed four transfer pipets and used it to put solutions into the test tubes by 3ml. I labeled it and placed into the plastic cups so it can stand upright. I grabbed each test tube and poured 2 ml of catalase solution into it. I also tapped and swirled to measure the bubbles by using the ruler. I wrote the numbers into the lab report. In the second experiment, I labeled the room
2. In the large beaker, put water and boil it completely. After that, remove the beaker from heat. 3. Sample tubes (A-D) should be labeled and capped tightly.
Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is important that a specific enzyme is present during the process. For example, lactase must be able to collaborate with lactose in order to break it down (Madar & Windelspecht, 105).
Reducing sugar is the monosaccharide of carbohydrate which is form in aldehyde in the presence an alkaline solution. Examples of reducing sugar are glucose, lactose and glyceraldehyde. The reducing sugars that contain aldehyde group act as reducing agent during oxidation because it will oxidize to carboxylic acid. Benedict solution is used to test the presence of the reducing sugar in the solutions. Benedict solution is made from anhydrous sodium carbonate, sodium citrate and copper (ii) sulphate. In this experiment glucose solution is poured into the Benedict solution and let them in the water bath about maximum 2 minutes. From the experiment, we can observe that the blue color solution turn to green and red or dark brown. This change of color refers to the level of the sugar inside the solutions. If there is no reducing sugar inside, the color of the solution remain blue. If there has a little sugar inside, the color changes from blue to green. If there is a lot of reducing sugar, so that the color of the solution changes from blue to red or dark brown. How the color of...
Investigating the Effect of Copper Sulphate on Amylase Activity Aim The aim of my experiment is to observe the affect on amylase when adding copper sulphate to a starch solution. Introduction Enzymes are that act as catalysts, in other words they increase the rate of chemical reactions. Consider the following general reaction between two substances, A and B, which react together to form a product, substance C: A + B = C In biological systems, this reaction might occur very slowly, or not at all, in the absence of an enzyme. Enzymes will greatly increase the rate of formation of the product. They can increase the rate of reactions by a factor of at least one million.
tube. Add 6 mL of 0.1M HCl to the first test tube, then 0.1M KMnO4 and