Tn 4351 was originally isolated from bacteroides fragilis [30] . The transposon was successfully introduced into Cytophaga succinicans, Flavobacterium meningosepticum, Flexibacter canadiansis, Flexibacter strain SFI and Sporocytophaga myxococcoides by conjugation [25]. Tn 4351carries two antibiotic resistance gene. One of the codes for resistance to erythromycin and clindamycin which is expressed in bactroides but not in E.Coli. The other gene codes for resistance in tetracycline and is expressed in aerobically grpwn E. coli, but not in anaerobically grpwn E. coli or in bacteroides.
At last, at 95°C, or 85ºC, the enzyme activity is showed at being in its greater temperature. From black at 0 minutes, the color became bright yellow at 10 minutes, which specify the optimal temperature for
The human body consists of enzymes which allow foods to be broken down and enable organisms to build chemical substances such as other proteins, carbohydrates and fats that are necessary for life. This experiment will be testing the enzymatic reactions with toothpicks. This experiment depicts the process when a substrate binds with an enzyme. However, only a specific substrate can attach to a specific enzyme. This allows the substrate to attach to the enzyme and then disconnect the enzyme overall causing the substrate to break in two.
In order to learn more about macromolecules, we performed an organic compound experiment. The purpose of this experiment is to find and test the presence of carbohydrates(Starch & Sugar) and proteins in different food using tested distilled water as indicators(independent variable). Food that will be tested in this experiment are cookies, milk, hot dog, pretzels, applesauce, cake mix, popcorn, and potato. My hypothesis is that if the food listed are tested for carbohydrates and proteins, then most of them with the exception of water, will be positive. Materials that will be used in this experiment are 8 regular test tubes, cookies, milk, hot dogs, pretzels, applesauce, cake mix, popcorns, potatoes, tap water, 500ml pyrex measuring cup, Benedict’s solution, Biuret solution, and Iodine solution.
ST Report In the experiment, the problem was the contaminants that were affecting the quality of the water samples. To fix this issue, three scientists had to determine the contaminants that were present in the samples. One sample was from the school sink and the second sample was from an unknown source. The scientists conducted many tests to figure out what pollutants were present in the water.
The calpain and calpastatin enzymes system plays a role in protein muscle renewal, as well as in the process of postmortem proteolysis of the meat in cattle. Tenderness of the meat depends on the magnitude of this process. The main enzyme is Calpain whereas Calpastatin is its inhibitor; numerous studies have identified diverse polymorphisms of the genes that code for both enzymes. Polymorphism CASTt1 and CASTuog are two mutations on the calpastatin gene, which have been identified as potential forecasters of meat tenderness. The objective of this study was to supplement previous studies, realized at the Veterinary Science Faculty, about genotyping for Calpain gene with the allelic and genotypic polymorphism frequency of CAST1 or CASTuog in
This experiment allowed the testing for carbohydrates, lipids and proteins in high concentration and low concentration substances. The test for proteins was determined using Biuret Reagent which is a blue colored solution of sodium and potassium hydroxide and a small amount of dilute copper sulfate solution. When mixed with a substance, it will either turn purple or pinkish/ purple based on whether protein or peptides are present respectively. The reagent changes color when combined with a protein or peptide because peptide bonds are formed by combining with the copper ions in the reagent. In the test, the first tube of water acted as a control because the reaction is known before the test so if it is negative, the test is valid.
It was originally hypothesised that when mince combined with protease solution is heated in water, the rate of degradation would increase continuously from room temperature up to 50 degrees. It was expected that rate of activity would reach its optimum activity, at 50 degrees celsius and be most active between 50 and 60 degrees. Once reaching over 60 degrees, the protease would begin to denature and therefore, decrease the rate of reaction dramatically. The results of this experiment supported the hypothesis.
Research Question: What is the effect of heat on the activity rate of albumin protein? Introduction: Heat and pH are common factors that denature proteins and enzymes; in this case heat will be used to break down a specific protein known as albumin. Albumin is found commonly in egg whites, milk, and in blood serum but in this particular experiment egg whites will be used. When the albumin is denaturized its function and shape are changed, while there are instances where the protein can go back to its former shape, it will not happen in this case.
4. In order to determine if the nuclear localization signal will cause the cytosolic protein and any other proteins to move into the nucleus, there are experiments that can demonstrate this. 1. One such experiment includes the use of green fluorescent proteins. By fluorescently tagging the proteins, we can observe the proteins that are traveling to the nucleus.
Some proteins fold into ‘blobs’, where some amino acids are located in the center of the shape, and some are located on the outside. The protein structure is vital because it determines protein function. Proteins catalyze chemical reactions by bringing them together in the right orientation and helping them react together. However, if the protein structure is incorrect, then it won’t have the ability to build up these reactions because the ‘pieces’ will not ‘fit’ together.
It is the only macromolecule that is going to dictate the nature of the protein to be
In this experiment , we can prove that the temperature, pH and salt are the factors that will affect the structure and function of the enzyme as it is a kind of protein . Therefore, there may be an influence on the activity of enzyme which substrates cannot be binded on the active site if the amylase in too high or low ph and temperature and excess salt environment . On the other hand optimum ph and temperature and suitable salt concentration may favour the amylase activity . Reference : 1.2016, May 08). Effects of pH on Amylase Activity.
Proteins are made up of peptide bonds holding amino acids together to perform biological functions like enzymes, antibodies, for transport and structure (Asmus, 2007). Lastly, nucleic acids
In order to utilize casein, bacteria cells secrete proteolytic exoenzymes (amylases, proteases, pectinases, lipases, xylanases and cellulases) outside of the cell that hydrolyze the protein to amino acids. The amino acids can then be used by cells after crossing the cell membrane via transport proteins [169]. Starch hydrolysis test is used to differentiate bacteria based on their ability to hydrolyze starch with the enzyme α-amylase or oligo-l, 6-glucosidase. These enzymes hydrolyze starch by breaking the glycosidic linkages between the sugar subunits. It aids in the differentiation of species from the genera Corynebacterium, Clostridium, Bacillus, Bacteroides, Fusobacterium and members of Enterococcus [170].
