How Temperature Affects the Degeneration of Proteins in Fish Food

The null hypothesis will be that the test tubes with an increase in temperature, pH values, enzyme concentrations, and substrate concentration will have a very small color change or no color change at all. The alternate hypothesis is that the test tubes containing an increase in temperature, pH values, enzyme concentrations, and substrate concentration will all have an intense color change; the more the change, the more intense the color change will be.

This Lab Report is an analysis of the results of a two-part experiment. In the first part, we used a gel filtration column to separate the components of a mixture composed of protein and non-protein molecules. By doing so we hoped to obtain fractions that contained single components of the mixture, while also gaining insight into the relative molecular weight of each component compared to each other. We would then plot these fractions onto nitrocellulose paper in order to determine which fractions had protein. In the second part, we would use the fractions which we had determined had protein to conduct an SDS-PAGE. By doing so we hoped to determine an estimate on the molecular weight of the proteins present in each fraction by comparing it to a tracker dye composed of a variety of molecules of differing molecular weight.

In this task the concentration of an unknown sample of copper sulphate using colorimetry was used to find the concentration. In this investigation copper sulphate was used which is CuSO4.5H20 as a formula. To make a standard solution which was 1M, the same clean equipment was used to make up the standard solution as used to make sodium carbonate. However there was one difference and that was that the hot distilled water was used to dissolve the copper sulphate crystals. There had to be enough hot water in order to dissolve the crystals into the beaker and then add cold distilled water to cool the solution.

Aim: The aim of the experiment is to test the effect temperature has on the activity of the enzyme rennin.

Colorimetric assay is a process of determining a concentration of a solution based on absorbance of light. The purpose of this lab is to determine if the Bradford assay is an accurate way to determine an unknown concentration of two samples of protein. The Bradford assay is done by measuring wavelength of light passing through a cuvette filled with Bradford dye and concentrations of PBS and proteins. After the cuvettes are mixed they are placed into a spectrophotometer to measure wavelength. The wavelength given will be used to plot a standard curve based on concentration (x-axis) and wavelength (y-axis). The standard curve is then used to measure an educated guess on the concentrations of unknown protein concentrations. We hypothesized that if we use the Bradford assay and colorimetric spectrophotometry we can determine an accurate concentration of two unknown concentrations of proteins. The results of this lab failed to reject our hypothesis based on accurate measurements of protein concentrations. The standard curves are drawn with a linear increasing slope. The Bradford assay is an accurate way to demine the concentration of an unknown concentration.

Abstract: The Effects of Temperature on Catechol Oxidase. Lania Ellis, 2014, 102 Student Center Dr. San Marcos, TX 78666.

Next, add enough bromothymol blue solution to each test tube until the water is blue. Next, using a straw, blow into the four test tubes until the color blue turns to the color of a yellowish/green. Then cut a sprig of Elodea from the plant and place one sprig into each of the four test tubes. Then the test tubes were sealed with a stopper. Two of the test tubes will be labeled light and placed into sunlight for about 2 hours. Then the other two test tubes will be placed into complete darkness for about 2 hours. After time is up, record the color of the solution from the four test tubes (Gunstream,

Finally, the test tubes were placed in the the rack and we recorded the color of the solution for day one in table

The lab performed required the use of quantitative and analytical analysis along with limiting reagent analysis. The reaction of Copper (II) Sulfate, CuSO4, mass of 7.0015g with 2.0095g Fe or iron powder produced a solid precipitate of copper while the solution remained the blue color. Through this the appropriate reaction had to be determined out of the two possibilities. Through the use of a vacuum filtration system the mass of Cu was found to be 2.1726g which meant that through limiting reagent analysis Fe was determined to be the limiting reagent and the chemical reaction was determined to be as following:-

This experiment consisted of setting up a control group of starch in various temperature and then placing both fungal amylases and bacterial amylases in a mixture of starch and placing the solution of amylase and starch in various temperatures of water. After a certain amount of time- different amount of time needs to be used in order to have reliable results- iodine is added in a well on spot plates, then two drops of the mixture of amylase-starch is added from each temperature used, by adding iodine into the plates the mixture will show how much starch was hydrolyzed, this is used to calculate the amount of

In this experiment the scientist will be testing if all proteins denature at the same temperature? Denaturation of a protein is when the structure of the protein is broken down and the protein loses its strength and ability to work, so it ended up dying.The independent variable is the different types of protein, albumen (egg), casein(milk) and keratin (hair) .The dependent variable is the temperature(F°) that the proteins start to change.The constant variable are the materials, room temperature and work space.

A simple but lengthy method for the estimation of the protein, determination by dry weight gives a very accurate amount of the protein in a given sample. Drying a protein-containing sample in a 104ºC to

The importance of hydrogen bonds in predicting stability of thermophilic proteins is well documented in literature (Vogt et al., 1997). The number of hydrogen bonds in thermophilic proteins and their mesophilic counterparts were calculated and the results normalized with the length of proteins show no significant difference in the total number of hydrogen bonds of thermophilic proteins and mesophilic proteins in the pairs (Figure 4). Further analysis on separating the total number of hydrogen bonds into four categories; Main chain – Main chain, Side chain – Side chain and Main chain – Side chain was also not able to reveal the reason behind the thermal stability of thermophilic proteins. These values are therefore not attributable to the increased stability of the thermophilic proteins in the dataset and are consistent with earlier findings of Gromiha et al., (2012) which observed a trend where the 50% of thermophiles and 50% of mesophiles had more hydrogen bonds than their respective partners. The study also identifies number of hydrogen bond as a factor not able to discriminate proteins of thermophiles from mesophiles.

Meanwhile, if temperature is increased denatures the proteins. Proteins then unfold and the non-polar groups which were previously in the interior of the molecule become exposed. This leads to a decrease in the solubility of the protein in aqueous environment. Addition of ethanol, methanol, acetone and the like decreases the dielectric constant and thus decreases protein’s solubility. (Boyer, 2000)

The study on blood of fish dates as far back as 1920. Hall and Gray [1929] have given the concentration of haemoglobin iron in few teleosts, and elasmobranch showing that the elasmobranchs have lesser concentration, Vars [1934] reported the values of iron, blood sugar, RBC Count and blood volume in a few fresh water fishes, Field [1943] gives cell numbers, cellular volumes, hydrogen-ion concentration, blood proteins, non protein nitrogenous