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yeast extract The Effects Of Various Factors On The Growth Rate Of E. Coli

The Effects of Various Factors on the Growth Rate of E. coli
Introduction:
There are times in our lives (as human beings) when people do not feel well. A doctor might diagnose them with a disease or an infection. There are also times when people do not feel clean. This could be a person's feeling after exercising, sweating, or maybe he/she had not taken a shower in a couple days. In any of the preceding scenarios, bacteria most likely played a major role in initiating a person's feeling of illness or squalor. Sickness can be caused from bacteria. Someone may be sick because they ate food contaminated with bacteria or they could have easily taken a sip from the cup of a friend and shared some sort of bacterial disease. Bacteria surrounds us everyday, every second. It is difficult for people to accept this fact because they want to believe they are clean, after they shower. In relative terms, a washed person is clean, but they are not free of bacteria. Clean is simply an image, because bacteria are covering all substances and objects that you use to be clean; toothbrushes, soap, and even toilet paper. We live in a world of bacteria, maybe even a world that evolved from bacteria.
These microscopic organisms reproduce quickly, sometimes even exponentially. In the experiment today, my class is observing and measuring data of how different factors can influence the rate at which bacteria grows. We will use Escherichia coli (E. coli) as our bacteria. It is a Gram-negative bacterium that resides in the intestines of humans (Laboratory Experiences, 34).
Before you can fully understand the experiment and it purpose, it is important to understand the phases bacteria go through when reproducing in various media. In general, a bacterial will go through four distinct phases; a lag phase, log phase, stationary phase, and a death phase. The lag phase shows how bacteria reproduce at a very slow rate at first. At this point, the cells are preparing for division. They are making sure to manufacture fats and proteins for the reproduction ahead. The second phase is the log (logarithmic or exponential) phase. The bacteria is now replicating rapidly and becoming so large in numbers that space is growing smaller, as is non-hazardous room and nutrient. Due to this rapid growth, the next step is the stationary phase. In this phase, about fifty percent of the new bacteria population will become inactive, and the other fifty percent will remain and continue replication (binary fission). The last stage of bacteria generational grow is the death stage. In the death stage, there is not enough nutrients for the entire population. This causes the death rate of E. coli to increase, and the division will slow as well. At some point, the birth rate will be lower than the death rate, and this is displayed in the graph at the leveling off, or downward slope. From this growth curve that bacteria produces, the mean generation time (MGT) can be calculated. This will be shown later in the results section of this report.
Various types of abiotic, non-living chemical and physical factors (Biology, 1027), factors try to decide which will act as catalysts and which will limit the growth of the E. coli. There are many factors that could have an effect on the growth rate of bacteria, but we are only concerned withthree; aeration, temperature, and nutrients.
The conditions for optimal growth-temperature, pH, salt concentrations, nutrient sources and so on- vary according to species. Refrigeration retards food spoilage because most microorganisms grow only very slowly at such low temperatures (Campbell, 507). Temperature acts as a catalyst for many things, and it helps speed up many chemical processes. It is stated in the lab manual ( 35) that 37 degrees Celsius is the optimal condition for E. coli and that E. coli has a doubling time of about 20 minutes at this temperature. From this information, I predict that the higher the temperature, the higher the MGT.
Our next variable that we are testing is the effect of different nutrients on E. coli. Our first type of media to test is ... more

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Biology

Lab Report 1Principles of Biology 1(BIOL 100)
Fall 2001Gerard Chretien

Living cells perform a multitude of chemical reactions very rapidly because of the participation of enzymes.  Enzymes are biological catalysts, compounds that speed up a chemical reaction without being used up or altered in the reaction.  The material with which the catalysts reacts, called the substrate, is modified during the reaction to form a new product.  But because the enzyme itself emerges from the reaction unchanged and ready to bind with another substrate molecule, a small amount of enzyme can alter a relatively enormous amount of substrate.

This report will illustrate the enzymatic action of the enzyme catecholase, which is common in plants. To study this particular enzyme in a laboratory, the natural substrate catechol is oxidized by the removal of two hydrogen atoms. The substrates of the enzyme are catechol and oxygen. These substates react with one another within the active site of the enzyme. The products formed by this reaction are benzoquinone has a brown color, you can see that the reaction has taken place.  This is called the fruit browning reaction. Benzoquinone inhibits the growth of microorganisms and prevents damaged fruit from rotting. In undamaged cells catecholase is stored in vesicles and does not interact with catechol.


In the presence of the enzyme catecholase:
Catechol+1/2O2 benzoquinone+H2O
The structure of the enzyme is mainly dependent on the active site and variable groups. Extreme temperatures or extreme pHs can alter the structure of an enzyme.  Enzymes function to lower the activation energy to break the bonds. They achieve this by putting stress and pressure on the bonds or creating a microenvironment for the substrate.  A change in the temperature or a fluctuation in pH can alter the enzymes structure. Anent temperature the alteration of the enzymes occurs when the temperature is very high and the enzyme denatures and is unable to perform the desired task.  The temperature is so high that the active site of the enzyme changes and it is unable to bond with substrates.

Part I:
Effect of Temperature on Enzyme Activity(Invertase)
The rate of an enzyme-catalyzed reaction will increase with temperature to maximum rate and then sharply decrease.  The rate increases to about 40 degrees Celsius, at which point the structure of proteins is disrupted (denaturation), resulting in an abrupt loss of enzyme activity.
PROCEDURE:
1. Number 3 test tubes (1,2, and 3) with a permanent marker. Add 4 ml of a sucrose solution to each test tube.
2. Place tube 1 in a beaker of ice water; place tube 2 in a beaker of water at room temperature, and tube 3 in a beaker of boiling water. Wait 10 minutes for the sucrose solution in the tubes to equilibrate with the temperature of the water in the beakers.
3. After 10 minutes, add 0.5ml of 25 percent invertase (an enzyme derived from yeast) solution to each tube (swirl the invertase solution before use).  Cover each tube and invert it several times to mix the contents during the 5 minutes.
4. After 5 minutes add 1ml of Benedicts solution to each test tube.  Place the 3 tubes at the same time in a boiling water for 5 minutes.
5. Remove all 3 tubes from the water bath at the same time and observe the amount of precipitate and the color of the Benedicts solution in the tube. Then I would record my observation on a data graph sheet and write a statement concerning the effects of temperature on enzyme activity.

Test Tube # ColorResults




Part II:
EFFECT OF pH ON ENZYME ACTIVITY (Catechol Oxidase)
The active site of an enzyme is affected by the presence of ions that change the charges within the protein molecule.  The most favorable pH for an enzyme is called the optimum pH, because it is at this pH that the enzyme is most active. A complete loss of enzyme activity will occur at extremely low or high pHs because of the breakdown (denaturation) of the protein structure.


PROCEDURE:
1. Number 5 test tubes (4,6,7,8, and 10) with a water-soluble pen.  Put 3 ml of phosphate buffer (pH 4, pH 5, pH 6, pH 7, pH 8, and pH 10) in the appropriately numbered test tubes.
2. Add 10 drops of potato extract to each tube (an extract of potato will be used as ... more

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