The purpose of this experiment was to apply all knowledge gained from the entire semester while in the lab and apply it to be able to identify an unknown genus and species gram positive bacteria. Each student was given a petri dish with an unknown Gram positive bacterium inside. The petri dish with the unknown gram positive bacteria that was used in my experiment was #8. The possible bacteria inside my petri dish could be any of the following:
This experiment involved the chosen enzyme, B-Galactosidase, to be tested with a substrate called o-nitrophenol-B-D-galactopyranoside (ONPG). The purpose was to determine over time the effects the enzyme had on the substrate concentration, as well as to examine the effect of lactose, a disaccharide on the formation of o-nitrophenol. The experiment utilized a spectrophotometer to determine at which the rate that the enzyme catalyzes, by timing the change in absorbance every 15 seconds, as well as observing any colour change. The amount of enzyme added to the B-Galactosidase is increased over time, and the ONPG is set to a constant value each trial. It was determined that through the trials of testing the absorbance of the enzyme, the faster
Lastly only germinating and whole barely seeds showed the presence of maltose, indicating only within these two there is amylase present which actively hydrolyzing starch into maltose, as per reaction 1 stated above. As dormant seeds have amylase concentrations that are far too low to be detected by this type of assay, as during dormancy energy demands for this state is considered to be zero. Hence the amylase concentration in the dormant seeds are far too low to be detected in the Benedict’s reagent test (Ernst,
The competitive inhibitor that was added was lactose. We predicted this because competitive inhibitors block and bind to the active site so it will slow down the binding of the desired substrate. An alternative hypothesis that came up was that the reaction of substrate would stay consistent as if no inhibitor was added. The enzyme could reject the inhibitor if it does not fit in the active site, causing the substrate to bind as it normally would. Our results showed that with the addition of lactose, the reaction did slow down a considerably
Bio Chem lab Report 04 Enzyme Biochemistry Group Member: Chan Man Jeun Duncan (16002621) Law Sze Man (16000478) Introduction Enzyme is a protein base structure substance in our body. It works at a biocatalyst that will catalyzing the chemical reaction, which helps to speed up the chemical reaction. Enzyme could only function in specific shape, and the shape of enzyme is depending on the environment, therefore it is hard for an enzyme to function well in an extreme environment. The aim of this experiment is to see can the enzyme functions normally in different environment(pH, temperature and salt concentration) via using starch solution, amylase from saliva, 0.5M HCl solution, 0.5M NaOH solution and NaCl solution, and using iodine solution
the propose of this experiment was too see if the chemical reaction of a enzyme can be made faster.
If cells become oxygen deficient, the condition known as hypoxia (no oxygen) occurs. This condition can be due to abnormally acidic blood or a lack of critical enzymes necessary for releasing oxygen from red blood cells, so when this oxidative cycle is oxygen deficient, it can’t produce the quantity nor quality of ATP necessary for normal cellular functioning.
In an organism 's body, chemical reactions are constantly taking place. These essential reactions can make or break the well-being of the body, yet the brain behind these changes is often times not recognized. This little brain or “macromolecule” is called an enzyme. An enzyme is a type protein that is able to speed up over 5,000 different reaction types an organism (2). Through catalyzation, the process of speeding up chemical reactions, enzymes attach to a substrate/molecule and break it down so that it can be used throughout the organism. Enzymes break down substrates in a very efficient way; through an assembly line (3). One enzyme starts off by attaching itself to a substrate at the active site, where the two undergo chemical reactions.
Mitochondria are known as the powerful parts of the cell. It is an organelle in cells that allows respiration to take place. The chemical reaction that lets out energy from glucose is called respiration. When this happens in mitochondria the body gets energy for it to work properly.
We use peroxidase as our enzyme in the experiment. Peroxidase is found in plants, such as turnip, and can convert hydrogen peroxide to water and oxygen. We had which were hydrogen peroxide (3%) and hydroxylamine. The hydrogen peroxide competes with the hydroxylamine for the active site molecules from peroxidase. The peroxidase needs the hydrogen peroxide in order to separate it into water and oxygen. If enough of the hydroxylamine is used in the test tube, it will stop the enzyme from binding with the hydrogen peroxide causing competitive
For the next 5 minutes, record the observed data at each minute (0, 1, 2, 3, 4, 5)
The different possible substrates for avocado catechol oxidase have very different Km’s and Vmax’s (Table 1). The Km’s range from 0.7 to 95, and the Vmax’s range from 0.58 x 105 to 17 x 105. The enzyme’s own substrates catechol has a Km of 6.5 and a Vmax of 5.4 x 105. Some of the substrates are better suited for catechol oxidase than others. For example, dopamine has a Km of 95 and a Vmax of 11 x 105. Both of these values are fairly high and would not make an effective substrate for catechol oxidase since the enzyme has a low affinity for the substrate. An example of a good alternative substrate would be 4-methylcatechol that has a low Km of 1.1 and a Vmax of 3.4 x 105. The enzyme now has a high affinity for the substrate and therefore requires less substrate to meet its Vmax.
For instance, we could not conclude that mitochondrial activity is present in Supernatant II. However, our experiment showed that the boiled corn kernels did not undergo any mitochondrial activity while the raw corn kernels did. This might indicate that raising the temperature might have an effect on the function of dehydrogenase. Moreover, our found that starch granules are present in both sediment I and the “gunk”. Indeed, some parts of this experiment were not successful because the procedure was not followed
ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells. The 3 concentrations of enzymes were 0.5 ml, 1.0 ml, and 2.0 ml of turnip extract, while the substrate consisted of 0.1ml, 0.2 ml, and 0.4 ml of hydrogen peroxide. In a separate tube, the control was made up of turnip extract and guaiacol, known as the color reagent. This was recorded the absorbance every 20 seconds for 3 minutes.
Reece, Jane B., Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, and Robert B. Jackson. "Concept 8.4." Campbell Biology AP*. 9th ed., 2005. N.p.: Pearson, n.d.