I. Introduction/Background/Purpose/Hypothesis: BACKROUND: An enzyme is a protein that controls the chemical reactions that take place in the body. Enzymes help by catalyzing (speeding up) the reaction and intern lowering the activation energy required for the reaction to occur. Molecules called substrates bind with enzymes during reactions. However each enzyme has a very specific purpose. The shape of the active site on the enzyme?s outer layer determines that purpose, along with deciding which substrates can bind with that specific enzyme. The active site of the enzyme is the spot where the substrate binds in order for the reaction to occur. The bond formed by the enzyme and substrate is a noncovalent chemical bond that exists little more than a millisecond. However, while bonded the substrate undergoes a chemical change and is converted into the product of the reaction. While held together by this weak bond the enzyme-substrate complex is formed. When the reaction is over this complex breaks down and the product leaves the enzyme and is used by the cell. Then enzyme returns to the catalytic cycle unchanged and it waits to be used again. Any one enzyme may be used over a thousand times per second: in turn requiring very little amounts of enzyme to convert large amounts of substrate into product. Since they are used at such an extreme pace enzymes do wear out and denature. Cellular proteinases are what cause the denaturation of the enzyme. The enzyme is then changed into the most basic amino acids and is used to make other proteins. The balance of the following determines enzyme amount: the process, which degrade the enzyme, and the processes that synthesize the enzyme. If a chemical reaction requires an enzyme to occur and none are present, than the rate of the reaction is very slow. However, if the amount of enzyme concentration is increased in a chemical equation than the catabolic rate is also increased.
The Essay on What Role Does Electrons Play in the Formation of Chemical Bonds?
Valence electrons are the electrons that are on the outermost shell of the atom's electrons which are can be either given away, added, or to be shared. When these electrons are given away, added to or shared, there is a chemical change occurring and the compound that is formed is changed from the original elements. This is called bonding which is pretty much the realm of the electrons. It is the ...
PURPOSE: The experiment we are going to investigate is meant to determine the effects of temperature on the activity of the enzyme. We will test temperatures ranging from 4?C to 48?C to find out if extreme temperatures either increase or decrease enzyme activity. Four different compounds will be tested, each having a different temperature, in order to determine what, if any, affect those temperatures will have on the enzyme activity. Comparing the color change in the substances will monitor enzyme activity. These color changes will be observed according to their absorbency of light. The absorbency will be monitored using a spectrophometer. Each compound will be tested several times to get an average set of data. This is done in order to avoid skewed results. All raw data will be recorded in table 1.1, and displayed by a graph. The averages will be recorded in table 1.2 and then displayed in there own graph. The averages will be used to get standard deviations. Those figures will be displayed in table 1.3 and also displayed in a graph.
HYPOTHESIS: enzyme activity will be increased as the temperature changes. However, at the extreme temperatures the enzyme activity will decrease. One thing should be kept in mind however, this experiment uses peroxidase as its enzyme, but every enzyme has a different optimal temperatures. MATERIALS: 9 test tubes, 2 hot water baths (one at 32?C and one at 48?C), Refrigerator, 30 ml guaiacol, 30ml H2O2, 30ml turnip extract, 30ml of Ph5 stock solution, spectrophometer, micro-pipet, roller pipet, 2 test tubes racks, 2 cuvets, cuvet rack, kim wipes, timer, gloves and goggles, distilled water, micro-pipet tips, sharpie METHOD: 1) Pre-incubate water baths to correct temperatures 2) Label test tubes 1-9 with Sharpie marker 3) Mix test tubes according to table 4.3 on page 4-9 of lab manual 4) Calibrate spectrophometer, according to directions given on page4-5 figure4.3, using test tube number 1 (the control) 5) Mix test tubes 2 & 3 and record absorbency every twenty seconds for 2 minutes. (be sure to start timing as soon as test tubes are mixed being mixed) 6) Mix test tubes 4 & 5 and record absorbency every twenty seconds for 2 minutes. (be sure to start timing as soon as test tubes are mixed being mixed) 7) Mix test tubes 6 & 7 and record absorbency every twenty seconds for 2 minutes.
The Term Paper on Test Tube Temperature Amylase Starch
... temperature on the activity of the enzyme amylase: Pour amylase solution into a test tube to a depth of 2 cm. Half fill another test tube ... rod lift a drop of the starch solution from the test tube and mix it with the first drop of iodine in the ... starch to be digested in each condition was calculated. Temperature (OC) 102132405055606780&90 Average Time (min) 9. 86. 75. 35. 53. 53. 03. ...
(be sure to start timing as soon as test tubes are mixed being mixed) 8) Mix test tubes 8 & 9 and record absorbency every twenty seconds for 2 minutes. (be sure to start timing as soon as test tubes are mixed being mixed) 9) Record observations in table provided in lab manual, page 4-10 table 4.4 **Complete three trials for each set of test tubes. Compare the different sets of data. If one set is extreme compared to the other, than ignore that set of data. After all data is collected, average each set of data. (An average should be found for each time increment for each set of test tubes) Then after the averages are calculated, calculate the standard deviations of the averages for each time increment. (Refer back to page 1-7 of lab manual if help is necessary) When all data is collected and calculated, use Microsoft Excel to create a graph for each data set. (A graph or chart should be created for the following: raw data, averages, and standard deviations) Refer to help sheet if help is needed using Microsoft Excel. Table 2 contains all of the raw data, each measurement taken at each time increment for each set of test tubes. Table 2 will also contain the averages calculated from the raw data. Averages recorded are obtained for each time increment for each set of test tubes. Table 2 contains the standard deviations calculated from the averages determined. All charts and graphs can be found on the pages attached to the end of the lab report.
The Essay on Test Tube Fermentation Yeast Tubes
Fermentation InvestigationPlanningAs a culture of yeast is merged with solution of sugar, a reaction called fermentation occurs. As products, ethanol and carbon dioxide are produced, in form of liquid and gas respectively. The reaction follows this equation: Glucose solution + Yeast Carbon dioxide + Ethanol + (Energy) And as one of the products is in the form of gas, the volume of the product can ...
Enzyme activity will be increased as the temperature changes. However, at the extreme temperatures the enzyme activity will decrease. One thing should be kept in mind however, this experiment uses peroxidase as its enzyme, but every enzyme has a different optimal temperatures. To prove this nine different test tubes were heated to four different temperatures. Those temperatures were 4 ?C, 23? C, 32? C, and 48? C. The test tubes that were kept at 23 and 32? C had the most drastic reaction rates. The test tubes at 4 and 48? C eventually slowed around the 100 seconds mark, unlike the other two test tubes. A spectrophometer was used to monitor the reaction rate. Absorbancy levels were taken every twenty seconds, from 0-120 seconds. An average was the collected for each set of test tubes at each time interval. These averages were recorded in Table 1. After the averages were collected then standard deviations were determined according to the formula found in the lab manual page 1-7. The averages were put into graph form and examined. By close evaluation of the data collected, the original hypothesis was proven to be true.
Bibliography:
LaFave,Carol. Foundations of Biology Laboratory Manual, Pgs.(4-1)-(4-14) The McGraw Hill Companies inc.
