Essay about E Science Lab 9

The control portion of a petri dish was used but we did not test to see if reacted with the hydrogen peroxide, so there was technically no control in this case.

4. There are other types of reagents used to determine what type of biomolecule a substance is. For example, copper ions present in Benedict’s reagent reacts with the free end of any reducing sugars, such as glucose, when heated. Originally blue in color, these copper ions are reduced by the sugar, and produce an orange-red colored precipitate. Alternatively, iodine-potassium iodide (IKI) may also be used when working with starch. IKI contains special tri-iodine ions which interact with the coiled structure of a starch

• Fourthly, we kept the temperature at a constant 25°C using a water bath. At low temperatures, an increase in temperature causes an exponential increase in enzyme activity. This is because an increase in temperature provides more kinetic energy for the collisions of enzymes and substrates, so

The same procedure was performed with 1 ml of potato blend and yeast sample. It took the chicken liver sample 56.94s to consume 1 cm peroxide solution, and it took yeast sample 22.42s. The potato sample didn’t seem to react with the solution at all. Therefore, the rate of reaction from the highest to the lowest was the active yeast, the chicken liver, and the potato. Enzymes in animal cells should run the reaction at the fastest rate because animals are

A common method of enzyme regulation is feedback inhibition, in which a metabolic pathway is turned off by its end product. A process in which the end product acts as an inhibitor of an enzyme in the pathway.

The topic of this lab is on biochemistry.This experiment was conducted to show how cells prevent the build of hydrogen peroxide in tissues. My group consisted of Lekha, Ruth, and Jason. There were used two different concentrations of hydrogen peroxide through this experiment , 1.5% and 3%. By testing two different types it is easier to understand how the H2O2 and catalase react with one another. To do this both the yeast, which was our catalase, and H2O2 were mixed together in a beaker. Each concentration was tested out twice for more accurate results . 1.5% concentrated H2O2 had an average reaction rate of 10.5 seconds while 3% concentrated H2O2 had an average reaction rate of 7.5 seconds. From this experiment we learned that by increasing the concentration of H2O2 and chemically combining it with a catalase it will speed up the reaction. Enzymes speed up chemical reactions . The independent variable in this experiment was the concentration of the H2O2. Some key vocabulary words are Catalase, enzyme, hydrogen peroxide ( H2O2), and concentration.

2) A small amount is required as the enzyme is used again and again as

Substrate concentration also affects the rate of reaction as the greater the substrate concentration the faster the rate of reaction and all the active sites are filled. At this point the rate of reaction can only be increased if you add more enzymes in to make more active sites available.

Experiment one tested how different concentrations of salt would change the rate of starch being broken down into maltose, using the enzyme amylase. For each of the solutions that did include enzyme, there was a dramatic change in the absorbance rate from time zero to 18 minutes. Figure 1 shows each absorbance level over the total 18 minutes. The 0% salt concentration had an absorbance of 2.5 at time zero and an absorbance of 0.056 after 18 minutes. The 2% salt concentration had an absorbance on 1.79 at time zero and an absorbance of 0.009 after 18 minutes. The 4% salt concentration had an absorbance of 1.86 at time zero and an absorbance of 0.006 after 18 minutes. The stock tube that contained no enzyme showed no abosrabance changes,

In bread making for example addition of amylases can yield more sugars from the starch in flour and barley grains, another commercial which is statue of import ants is the conversion of starch to sweet glucose syrups which are used generally as sweeteners in food industry as well as in the bread-making and brewing industry. Altering the balance between amyloglucosidase and the fungi alpha amylase can produce different proportions of glucose and maltose. A higher proportion of glucose is useful for fermentation whereas higher maltose is more useful in preparation of jam and confectionary. The Amylase Enzyme breaks down starch; which is a carbohydrate.

There were three test tubes in which the experiment was held. A relatively equal sized portion of raw potato (this contained the enzyme [a biological catalyst] hydrogen peroxidase) was placed in each tube. Then, enough water to cover the potato was added. Proceeding this, each of the test tubes were assigned a temperature; cold, room temperature or warm (this was written on the tag so that they were not confused). The test tube destinated ‘cold’ was placed in a ice bath for five minutes. At the same time, the ‘hot’ test tube was placed in a hot water bath for five minutes. Meanwhile, the room temperature test tube sat at room temperature for five minutes. When the five minutes were over, the test tubes were returned to the rack (so that they were able to be observed). Then, the test tubes were allowed to sit at room temperature for five more minutes. Once that period of time was over, 2 ml of hydrogen peroxide (the substrate) was added to each tube.

Our goal of this lab is to find out amylase’s digest speed in different temperatures. To accomplish this goal we will need 4 test tubes with amylase and starch in it, water baths/water boiler with will be making the temperature 4, 21, 40, 60 and 100. And iodine to test the amount of leftover starch. We will be mixing starch with amylase (test tubes) in different temperatures (4, 21, 40, 60, 100). Then we will add the mixture of amylase and starch, to the iodine in the wells. We add it because we want to see how fast amylase can digest starch in different temperatures.

The rate of reaction is also affected by the concentration of the substrate or enzyme. The more enzyme molecules (the higher the concentration) to facilitate reactions, the faster the rate of reaction (Figure 5) (Evans, Ladiges, McKenzie, & Spenceley,

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

Conclusion: The yeast was tested multiple times at different concentrations of 100%, 50%, and 10%. As