Essay about Amylase Investigation

Use a glass beaker to pour an adequate amount of the liquid substance and use the pipette from the glass beaker.

Thereafter I used a pipette to meticulously drop in water up to the 250ml mark.

Tie a knot 3.4 mm. from the edge on one side of the tubing and use the 10 mL graduated cylinder twice to fill the tubing with 15 mL of water. Tie another knot 3.4 mm. on the other side of the tubing

0.0375 mg/ml Porcine Pancreatic Amylase Solution (amylase powder in 0.9% NaCl ), Iodine Solution; each solution were pipetted into each of the 5 test tubes with 5 ml of 1% starch. Each tube contained a 1% starch solution with a different pH. All tubes were at room temperature. Room temperature was 22C. 0.2 ml of porcine pancreatic amylase solution was then pipetted into each tube. A timer was started and every 3minutes the starch / amylase mixture were pipetted from each tube and pipetted into the spot plate for every sample tube, then the iodine solution were added to a spot plate cell for each sample. Iodine reacts with starch to change from yellow to deep blue /black in the presence of starch. A lightening of the blue/ black to a brown color will occur as less starch is present. Results were reported as (+) for presence of starch in the sample or (–) for the absence of starch. After every three minute increment had passed, these same

2. We measured 1 mL of turnip peroxidase (the enzyme) and 3 mL of neutral buffer (pH corresponding to the test tube number i.e. pH 5 in test tube 5) with a syringe and disposed it into tubes 3, 5, 6, 7, 8, and 10

The first experiment begun by filling a 600-ml beaker, almost to the top, with water. Next, a 10-ml graduated cylinder was filled to the top with water. Once water was added to the beaker and graduated cylinder, a thumb was placed over the top of the graduated cylinder. This would ensure that no water was let out and no bubbles were let into the graduated cylinder. Next, it was turned upside down and fully submerged into the beaker. Then, a U-shaped glass tube was attained. The short end of the glass tube was placed into the beaker with the tip inside of the graduated cylinder. Next, a 50-ml Erlenmeyer flask was received. After, 10-ml of substrate concentration and 10-ml of catalase/buffer solution were placed into the flask. A rubber stopper was then placed on the opening of the flask. After adding these, the flask was held at the neck and spun softly

Enzymes are a key aspect in our everyday life and are a key to sustaining life. They are biological catalysts that help speed up the rate of reactions. They do this by lowering the activation energy of chemical reactions (Biology Department, 2011).

Dispense .5 mL water into the already weighed conical vial, replace cap and face insert on its down side.

Procedure: 1. Use a spray bottle filled with water.

An increase in enzyme concentration will increase enzyme substrate speed up the rate of reaction until the saturation point is reached. (Enzymes and...) Meaning that all the enzyme active sites are occupied by substrate and can no longer enhance in activity. For the next experiment we tested on was temperature. I hypothesis, that the enzyme energy will increase as the temperature rises and have little energy as it lowers. When the temperature rises the activity of the enzyme and substrate collisions increases as well. But, it will hit its maximum point where its bonds will begin to break down. We first measured the absorbance rate at 0 Celsius giving a us .001405 (1/s) and giving the product a light shade of brown. The reaction rate became more active as the temperature rose and the color would darken. But, when reaching over 40 Celsius that’s when the enzyme began to denature. Also, when reaching 100 Celsius the enzyme reaction rate was less than .0005 (1/s) and the solution stayed transparent. Next, we tested the pH, it’s a scale that measures 0 to 14, 0 being the most acidic and 14 being the most

Procedure: Cut top off 2 liter bottle and bottom off another. Fill the one without a top with water and put a

Add the same amount of Benedict’s solution in each tube and for the ones that need iodine use the same amount.

Remove the tubes and add 2-3 drops of Iodine – potassium – iodide solution to each tube.

To find the effect of temperature on the activity of an enzyme, the experiment deals with the steps as follows. First, 3 mL if pH 7 phosphate buffer was used to fill three different test tubes that were labeled 10, 24, and 50. These three test tubes were set in three different temperature settings. The first test tube was placed in an ice-water bath for ten minutes until it reached a temperature of 2° C or less. The second tube’s temperature setting was at room temperature until a temperature of 21°C was reached. The third tube was placed in a beaker of warm-water until the contents of the beaker reached a temperature setting of 60° C. There were four more test tubes that were included in the procedure. Two of the test tubes contained potato juice were one was put in ice and the other was placed in warm-water. The other two test tubes contained catechol. One test tube was put in ice and the other in warm water. After

In the first part of the lab, 5 solutions were tested for the Benedict’s test along with Iodine test, what was observed was the reaction rate vs. enzyme concentration. As shown on the plot #1 graph, the concentration of the salivary amylase increases, the faster it turned into light brown, meaning the faster it broke down into glucose subunits. Specifically, in test tube 11, it contained 2ml of 10% salivary amylase and 2ml of the buffer, this solution turned into a light brown in 25 seconds. This because when the concentration of the enzyme is higher, there are more active sites for the substrate to bind to. Therefore, the enzyme is breaking down the substrate into smaller and smaller subunits of glucose, causing it to have a negative result for the Iodine test along with having a positive result for the Benedict’s test due to there being more reducing sugars (Valls, Rojas, Pujadas, Garcia-Vallve, & Mulero, 2012).Furthermore, in the test tube 12, it contained 5% of salivary amylase and 2ml of buffer. The Iodine test for this solution turned into a light brown colour in 30 seconds because the concentration of the enzyme was decreased, thus not having as many sites for the substrate to bind to and break down the starch into glucose subunits. For the Benedict’s test, the solution was broken down into smaller subunits and causing it to have a positive result by turning into a light brown. The tube containing 2% salivary amylase turned into a light brown colour for the Iodine