Effect Of Concentration On The Concentration Of Hydrogenase

This lab was to investigate fermentation, a cellular process that transfers the energy in glucose bonds to ATP. The energy in ATP can then be used to perform cellular work.

This experiment looked at how substrate concentration can affect enzyme activity. In this case the substrate was hydrogen peroxide and the enzyme was catalase. Pieces of meat providing the catalase were added to increasing concentrations of hydrogen peroxide in order to measure the effect of hydrogen peroxide concentrations on the enzyme’s activity. The variable measured was oxygen produced, as water would be too difficult to measure with basic equipment.

Used to see if the temperature of the water is at 37oc – 40oc and if

The purpose of this experiment was to determine how the body prevents the build up of H2O2 in tissues. During the process of cellular respiration Carbon Dioxide and water are produced but occasionally Hydrogen Peroxide is formed as an

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

My graph shows there is an almost perfect positive correlation between the hydrogen peroxide concentration and the rate of the catalase enzyme reaction, with a correlation coefficient of 0.99. The rate of reaction at 1% concentration was 0.46cm3 oxygen produced per minute and the lowest recorded rate. For 3% was 1.33cm3 per minute, and for 6% was 2.17cm3 per minute and was the highest recorded rate. The

Yeast is a fungus that can generate glucose into energy without using any oxygen molecules. We tested the fermenting ability of yeast from two different carbon sources: glucose and aspartame. We hypothesized that yeast is unable to use the carbon sources of aspartame. To do this, we decided to use both carbon sources in the same concentration. Each carbon source was mixed with the same amount of yeast solution. The experiment group of 5.5 mM aspartame solution was compared with the control group of 5.5mM glucose solution. We recorded the rate of fermentation for glucose and aspartame in the Vernier Lab Quest. The fermentation rate of aspartame is a negative number, and glucose is a positive number. Our results show that yeast was unable to ferment aspartame as yeast fermented glucose. The results indicate that aspartame has no effect on yeast fermentation rate because yeast do not catabolize aspartame because it does not have the appropriate enzymes to break it down.

Bacteria groups or species can be differentiated by the fermentation patterns. The end-product of carbohydrate fermentation is an acid or acid with gas production and is dependent on the organism involved in the fermentation process. The carbohydrate fermentation tests detect if an organism is able to utilize glucose, lactose and sucrose. Phenol red is used as a pH indicator because it can indicate a change in pH when acid products are formed. Bacteria can utilize certain sugars resulting in an alkaline by-product which changes the color of the carbohydrate broth from red to yellow. Bubbles trapped within the Durham tube indicate the production of gas. The Phenol red carbohydrate fermentation tests determine that my organism E. coli can utilize glucose, lactose and sometimes sucrose but can only produce gas in glucose and lactose. (Phenol red carbohydrate fermentation lab

Catechol, in the presence of oxygen is oxidized by catechol oxidase to form benzoquinone (Harel et al., 1964). Bananas and potatoes contain catechol oxidase that acts on catechol which is initially colorless and converts it to brown (Harel et al., 1964). In this experiment, the effect of pH on the activity of catechol oxidase was conducted using buffers ranging from pH2 to pH10. Two trials were conducted due to the first trial results being altered by an external factor. The results were acquired by taking readings every 2 minutes for 20 minutes from a spectrophotometer and then recorded on to the table. The data collected in the table were then made into graphs to illustrate the influence of pH on the catechol oxidase catalyzed reaction. After analysis, the data revealed that pH did have a significant influence on the enzyme as recorded by absorbance per minute. However, the data was collected was not accurate due to external factors, thus the results are debatable and should be experimented again for validation.

An Enzyme is a protein, which is capable of starting a chemical reaction, which involves the formation or breakage of chemical bonds. A substrate is the surface or material on or from which an organism lives, grows, or obtains its nourishment. In this case it is hydrogen peroxide. This lab report will be explaining the experiment held to understand the effects of the changes in the amount of substrate on the enzyme’s reaction.

Enzymes are high molecular weight molecules and are proteins in nature. Enzymes work as catalysts in biochemical reactions in living organisms. Enzyme Catecholase is found on in plants, animals as well as fungi and is responsible for the darkening of different fruits. In most cases enzymatic activities are influenced by a number of factors, among them is temperature, PH, enzyme concentration as well as substrate concentration (Silverthorn, 2004). In this experiment enzyme catecholase was used to investigate the effects of PH and enzyme concentration on it rate of reaction. A pH buffer was used to control the PH, potato juice was used as the substrate and water was used as a solvent.

The rate of fermentation in this investigation was represented by the amount of carbon dioxide produced as a byproduct of fermentation in the given time.

The enzyme catechol oxidase, extracted from masticated potato (Solanum tuberosum) lowers activation energy, as it is a catalyst. This enzyme can react with catechol to produce benzoquinone and water. Catechol oxidase is tested against a multitude of phosphate buffers, acidic, neutral and basic pH values, and chilled temperatures to hot temperatures. The purposes of these testes were to determine the optimal temperature and pHs at which catechol oxidase performs at. The method to measure results was the usage of a spectrophotometer (Vernier Spectrouis Plus). The spectrophotometer measures the absorbance levels of the pigment excreted when catechol oxidase undergoes a reaction. The high the absorbance, the more products produced and vise versa. The highest absorbance for the catechol oxidase submitted to different temperatures measured an average 0.6018 nm, when at 20 C. The highest absorbance for the catechol oxidase submitted to different pH values measured two averages of 0.658 at pH 6 and 0.6464 at pH 7. The conclusion taken from the available data explains that the optimal pH for catechol oxidase was between pH 6 and 7 and the optimal temperature was at room temperature at 20C.

As the diagram on the right displays, one molecule of Glucose produces two molecules of carbon dioxide and two molecules of ethanol. The fermentation of glucose to ethanol is only possible if oxygen is absent otherwise instead of producing ethanol and carbon dioxide, lactic acid is produced instead.

The Hypothesis was proven partially correct by the experiment. As the hypothesis stated, when the temperature was increased, the efficiency of the catalysed reaction decreased. This was due to the denaturing of the active site of the protein. However,