1.Introduction: An enzyme is a large protein that acts as a biological catalyst which changes the rate of a reaction. It provides an active site which is an environment where a reaction can take place this is made up of amino acids. The structure and shape of the substrate, the structure and shape of an enzyme and the substance upon which the enzyme works all have to match exactly. This enables the substrate to bind, but it can 't do this if the shapes of the two are different. The Aim of Enzyme Catalase Experiment is making a series of experiments involving the enzyme Catalase which has been performed in order to determine some of the enzyme 's properties.
Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.
In many cases the association process is a part of biological function as in blood clotting or the formation of muscle fibers. Aggregation of proteins also leads to perturbation of the biological function with sometimes serious physiological consequences as in the formation of cataracts in the lens of the eye or amyloid fibrils associated with Alzheimer’ and other neurological diseases. From a colloid chemistry perspective, protein self-association is a special case of the general problem of colloid stability. There are two important aspects of the protein systems in this respect: first in contrast to colloids in general the system can be obtained in pure form and then represent a true single component. Second the protein has a complex molecular structure and one should expect protein- protein interactions to be highly directional.
As a result, the physical properties of the membrane can be restored to their optimal state, which will have a balanced maintenance of the ion gradients across the membranes, and the restoration of the functions of membrane associated enzymes. There are three types of fatty acid desaturases that have been described, such as acyl-CoA desaturases, Acyl-ACP desaturases and acyl-lipid desaturase. All of these fatty acid desaturases introduced a double bond into the fatty acids bound to the CoA, ACP and glycolipids sites (Chintalapati et al., 2004; Russell, 1997). Among all of the desaturases, acyl-lipid desaturases was known to be the most efficient fatty acids
Introduction Cyclodextrins (CDs) are cyclic oligosaccharides consist of (α-1,4)-linked α-D-glucopyranose units produced by bacterial digestion of cellulose. These structurally related natural products contain a central cavity that was lined by the skeletal carbons and ethereal oxygens of the glucose residues, which gave it a lipophilic character to a certain extent while the outer surface is hydrophilic. The 3D-structure of CDs are shaped like a truncated cone rather than perfect cylinders due to the chair conformation of their glucopyranose units. The hydroxyl functional groups are orientated on the cone exterior with the primary hydroxyl groups of the sugar residues at the narrow edge of the cone, and the secondary hydroxyl groups at the wider edge. The polarity of the cavity has been estimated to be similar to that of an aqueous
The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate. All enzymes are under the class of protein biomolecule. Amino acids are the basic units that are combined to make up an enzyme.
Sodium dodecyl sulfate polyacrylamide gel electrophoresis also known as SDS-PAGE is one of the methods for determining the molecular weight of unknown proteins. SDS is an anionic molecule which denaturizes proteins and brings it back to its’ primary structure and it also provides a negative charge to the uncharged molecule. The SDS-PAGE enables the separation of proteins based on their sizes. The larger the size of the protein, the harder it is to travel through the gel thus heavier proteins stay near the cathode side of the gel. For this experiment, a software named Gel Analyzer was used in order to obtain the molecular weight of the unknown proteins with the help of a protein ladder with known molecular weight and protein concentration.
Biosynthesis Pathway A biosynthesis pathway describes the steps that take place in a chemical reaction which occurs when living organisms create new molecule from simpler ones. The word "biosynthesis" comes from two words: "bio," which means that the reaction is occurring in living organism and "synthesis," which indicates that large products are made up by simpler molecules. To describe a pathway completely some compounds are involved which includes such as which enzymes, coenzymes and cofactors are used in each reaction. Not all molecules are synthesized by humans, some molecules such as some essential amino acids i.e. lysine, these nutrients come from the protein rich food we consume including beans.
OBJECTIVE The objective of this experiment was to analyze and determine the unknown concentration of a protein solution by utilizing two different colorimetric techniques; Biuret and Lowry. The Biuret method was used with unknown #2 and the Lowery method was used for unknown #1. After the concentration of each unknown was analyzed (by Biuret or Lowry method), the alternate objective was to compare the results achieved by each method and to determine if the results from the approaches were consistent in contrast to each other. THEORY Biuret and Lowry methods use colorimetry as a tool to analyze protein concentration quantitatively. While both methods are respected and widely used, the Lowry method has a sensitivity level that is
CZE, also known as free solution capillary electrophoresis, is a separation technique that predominantly takes into account the ratio of the particle’s charge to mass, where those with large charge to mass ratio separate from the rest first; therefore, the larger the ratio, the quicker the separation. In addition to the electrophoretic mobility of the molecules, CZE is heavily dependent on the application of constant field strength throughout the capillary and on the pH of the buffer solution. CZE is an excellent choice of technique to employ in cases where there are very small pI (isoelectric point) differences in protein
Even though transport proteins are involved in facilitated diffusion, it is still considered passive transport because the solute is moving down its concentration gradient. Facilitated diffusion speeds up the transport of a solute by providing an efficient passage through the membrane, but it does not alter the direction of transport. Active transport requires energy to move a solute against its concentration gradient. As in most other cellular work, ATP will most often provide this energy, usually by transferring its terminal phosphate group directly to the transport protein. With ATP, the donated phosphate group induces the transport protein to change its shape in a manner that translocates the solute bound to the protein across the membrane.
The purpose of stacking gel is to make sure all the proteins start separating at approximately the same time. The pore size is larger so that it is easier for large protein to move in order to catch up with the smaller protein. As heating, SDS denature the proteins, the proteins are loaded onto the wells on the stacking gel. The denatured proteins have a uniform mass to negative charge ratio. Since the current run from negative (top) to positive (bottom), the proteins move toward the bottom.
The membrane structure is determined by the lipid bilayer, and proteins determine the membrane functions. The membrane has a lipid bilayer containing hydrophobic and hydrophilic regions. This bilayer blocks hydrophilic substances from passing while still allowing water diffusion. This allows oxygen and carbon dioxide molecules, both lipid-soluble molecules, to diffuse through the bilayer easily. Water molecules, due to their small size,