Correlation Between Ecca1 And The 4414 Gene

This experiment was centered on metabolic and biochemical testing procedures. The rationale of performing these tests was to distinguish six different microbes from one another and to compare how their metabolic and biochemical processes differ from species to species to determine the unknown sample.

The experiment was performed on February 2nd 2016 at the University of Calgary in a Biological Science laboratory. The experimental procedure was done in a group of four students.

There are many substances that can be manipulated and cause the rate of reaction in fermentation to either speed up or slow down. Substances that alter the rate of the reaction could be temperature of the water, the yeast concentration, pH, and the glucose concentration. In the experimental group of the experiment the amount of yeast concentration was manipulated. The objective of this experiment was to determine what factors affect the rate of the fermentation. To test this objective we changed the amount of yeast being used. A higher yeast concentration replaced the controlled yeast amount. A prediction made by my group was that higher amount of yeast would speed up the process of fermentation. Our null hypothesis is there will be no

Fermentation is a metabolic pathway that produce ATP molecules under anaerobic conditions (only undergoes glycolysis), NAD+ is used directly in glycolysis to form ATP molecules, which is not as efficient as cellular respiration because only 2ATP molecules are formed during the glycolysis. One type of fermentation is alcohol fermentation, it produces pyruvate molecules made by glycolysis and the yeast will break it down to give off carbon dioxide, the reactant is glucose and the byproducts are ethanol and carbon dioxide. In this lab, the purpose is to measure whether the changes of

PH can affect the way fermentation occurs due to the irregularity of the acidity or alkalinity within the glucose solution. This is an enzyme-based reaction that is susceptible to pH. The aim of this experiment was to determine how pH affects the yeast fermentation rate by performing the experiment numerous times with a different pH of glucose solution which included pH 3, 5, 7, 9, 11. The hypothesis was ‘If the pH is lower than the neutral point then the fermentation reaction will occur faster?’ The experiment conducted was to measure the amount of C02 produced by the yeast going into fermentation, however varying the pH of glucose solution by using different pHs . To test this every 5 minutes the volume of gas in the test tube was observed and recorded until a period of 30 minutes had been. The end results

Salinity - All yeast spheres will be soaked in the same water, with no salt added

The experiment answered the question; How do yeast metabolize different fuels? My hypothesis was that yeast could metabolize some fuels and not others, but all the fuels would be metabolized at a different rate. My prediction was that yeast could metabolize all the fuels we used, but it would metabolize at different rates. Yeast metabolizes different fuels by fermentation without the presence of oxygen; this is the method we used in the lab. The control group produces carbon dioxide because there are still different sugars in the water. These sugars are there because we used normal tap water, which contains many different molecules and ions inside the solution. It is important to have the control group to compare to the other fuels because we can see how much the other fuels have created compared to the normal water from the

The GLAT enzyme itself belongs to the histidine triad super family and is a member of branch III. This enzyme shows specific nucleoside monophosphate activity and is a homodimer with each monomer containing a single domain comprised of 6 α- helices and a β-sheet which is formed by 13 antiparallel and 1 parallel strand. The mechanism of this enzyme is described as having ping-pong kinetics with the following two steps. In the first step the active site histidine attacks R-phosphorus of UDP-glucose which displaces glucose-1-phosphate and forms a covalent intermediate. The second step involves the previously formed intermediate reacting with galactose-1-phosphate to displace the histidine and produce UDP-galactose. (Facchiano, 103-104).

Apparatus: Spectrophotometer (UV-1201), cuvettes, water bath (set at 37°C), 200µl and 1000µl micropipettes and test tube

The procedure for this experiment was to first obtain four balloons and blow them up in order to stretch them. Then obtain and fill the four large test tubes each with thirty milliliters of warm forty degrees Celsius water and two grams of dry yeast which was weighed on a scale and scooped out by a spatula. After five milliliters of water, ten percent glucose, fructose or sucrose went into one of the four test tubes. Then parafilm was placed on top of each of the test tubes to seal them and they were swirled activating the yeast through rehydration. After swirling the film was removed and the balloons were tightly placed on the test tubes. Then finally observed the tubes build up of CO2 all the while swirling gently every fifteen minutes, recording observations.

All samples contained yeast and mold count in between 2.6 and 3.9 log CFU/ml (Table 2). All four Pico de gallo samples had a low pH therefore, yeast and mold growth were pretty consistent because they can tolerate low pH conditions better than bacteria and other spoilers

In analyzing the effect of 2-aminopurine on mutation frequencies of bacterial strain CC102 (ara∆(gpt-lac)5 thi rpsL/F’ lacZ-Y+A+proA+B+ , the bacterial strain CC102 was cultured in LB medium with 2-aminopurine and one LB medium without 2-aminopurine. The bacterial strain CC102 with and without the 2-aminopurine mutagens were diluted to 10-5 and 10-6 and were plated on LB plates with nutrients and sources of carbon compounds for growth. The undiluted bacterial strain CC102 was then plated on minimal medium with thiamine and lactose. In noting the genotype of the bacterial strain, there is a deletion in the lac gene as it is ∆(gpt-lac) and the lacZ gene is not functional, therefore β-galactosidase is not able to cleave lactose into the constituents of glucose and galactose. In table 1.1, when observing the number of mutant colonies on minimal lactose and single cell colonies formed on LB plates with no introduction of the 2-AP mutagen, the mutant colonies were not formed on the minimal lactose yet were formed on the LB nutrient rich plate. For example in looking at group 6 data, 163 colonies were formed on LB medium at 10-6 yet no colonies were formed on minimal lactose with no 2-AP. Since the lac gene and the lacZ gene need to be functional to cleave lactose, it would allow for growth on the minimal medium with lactose but since there was a deletion for the lac gene and lacZ gene was not functional, no growth occurred. However with the introduction of the

Higher levels of solution should produce higher levels of product. The independent variable for the control group data and the experiment data is the yeast concentration. The dependent variable for the control group data and the experiment data is how much oxygen is produced. The Constant for the control group data and the experiment data is time and amount of hydrogen peroxide. The products of the experiment will increase if the levels of reactants increase. Denatured yeast may cause change in the reaction of the experiment. For all trials of the control group, the concentration of yeast is 6ml. For the experiment data, the yeast concentration varies from 8mL, 10 mL, 12 mL, 14 mL, and 16 mL. The temperature may cause change in the reaction of the combination of yeast and hydrogen peroxide

The experimental protocol used in this investigation was as outlined in the GENE223 Lab Manual ‘Gene223 teaching staff (2015)’ in a team of three, using ‘bait’ yeast

Good quality genomic DNA was isolated (Sambrook, et al 2002) and bothansA1 and ansA3 genes were amplified by PCR. Clear bands of both the genes showing a size of 1kb were observed under UV transilluminator after agarose gel electrophoresis (Fig 1).