Determining an effective assay is often difficult; but the more specific the assay, the more effective the purification. For enzymes, which are protein catalysts the assay is usually based on the reaction that the enzyme catalyzes in the cell. In this experiment, amylase enzyme is tested. it hydrolyzes starch to monosaccharides. The amylose component of starch complexes with iodine as follows and produces blue to purple complex.
Literature review Research question is how different temperatures affect the catalase enzyme. What is an enzyme? Enzymes are macromolecular biological catalysts. Enzymes speed up chemical reactions. Substrates are molecules that enzymes could act upon and the enzyme converts the substrates into different molecules known as products.
Changes in pH affect the binding of the substrate at the active site of the enzyme and also the rate of breakdown of the enzyme-substrate complex. These can also be the change in conformation of enzyme at extreme
If the substance is a darker color, it will absorb more light, and if it is lighter it will absorb less light. In addition, the enzyme and substrate will be tested with different levels of pH and different temperatures in order to demonstrate if the reaction will improve or not based on these
4.1.2. Reactors with Enzyme Immobilized on Membrane In reactor with enzyme immobilized on membrane, the biocatalyst retains within the membrane itself, during mass transfer process the contact between the substrate and the enzyme takes place as a result of the transmembrane pressure and permeate contains the product. The better results and control of the reaction is possible through the “micro-reactor concept”, where the distance between the catalyst and the substrate is reduced considerably, then increasing the probability of reaction. In such a system, the contact between the molecules of the substrate and biocatalysts is improved as the mass transfer path is reduced, while the contact time can be controlled through the mass transfer rate.
Enzymes have a region called the active site. This is because a substrate has specific chemical properties that satisfy the chemical properties of the active site. Enzymes quicken reactions by decreasing the amount of energy needed for the reactant to undergo a specific reaction by providing an alternative reaction pathway. In this experiment, the enzyme catalase will be used. The enzyme catalase is commonly found in animal and plant cells, but a substantial amount is found in liver.
CRITICAL READING / A. THE KOJI PHASE Enzyme-substrate complex: Chemically, enzymes are protein molecules containing a specific area called active site. When a substrate comes and binds to this active site, biological changes takes place. The enzyme – substrate complex mechanism can be explained by different hypothesis. The lock and key hypothesis states that, the substrate fits exactly into the active site of an enzyme which is responsible for biological events to take place.
ABSTRACT To catalyze a reaction, an enzyme will grab on (bind) to one or more reactant molecules. In this experiment we examined how increasing the volume of the extract added to the reaction would affect the rate of the reaction. The enzyme used was horseradish peroxidase which helps catalyze hydrogen peroxide. Using different pH levels, the absorbance rate of the reaction was measured to see at which condition the enzyme worked best. The rates of absorption were calculated using a spectrophotometer in 20 second intervals up to 120 seconds.
One importance of chemical equilibrium reaction is that it helps the blood to control it’s pH level, which is between 7.35-7.45. If it were to be that the state of the blood changes to slightly alkalosis or acidosis, one would probably gain critical health problems and a possibility of death. For instance, if the pH of the blood becomes 6.8, due to alkalosis in the blood, the fluid would become more oxygen
David Lynn (Emory University), which helps the audience to have a good knowledge of the structures and forces during the supramolecular self-assembly process, and understand how the chemical information will be stored and translated into the new molecules in this process. His talk mainly focused on the mutant peptides of Aβ Amyloid protein that is well-known to be responsible for Alzheimer’s disease. By characterizing the properties of self-assembly of different pieces of peptides from Aβ Amyloid protein, he showed that this sequence specificity played an important role in self-assembly of these mutant peptides in vitro. In addition, I think he clearly explained the design of an in vivo genetic assay that is based on the use of the yeast prion, the Sup35 of S. cereviseiae. They studied the mechanism of this supramolecular self-assembly process according to the score able phenotype with this in vivo assay.