Investigating Enzyme concentrations and enzyme activity Enzymes are substances that are produced by living organisms that act as biological catalysts that speed up rates of reactions for specific chemical reactions. This occurs by attaching a substrate molecule (the substance that the active site of an Enzyme interacts with) into its highly specific active site. In chemical reactions a certain amount of energy is needed to start the reaction, this is called the activation energy. Enzymes lower the amount of activation energy that is needed to make the reaction happen; this in turn causes the rate of reaction to increase. Certain factors affect the rate of reaction:- Temperature – temperature increase the rate of reaction because the molecules gain kinetic energy and this increases the likelihood of an enzyme and a substrate colliding, subsequently increasing the rate of reaction.
This is where the reactions occurs. From there the enzyme breaks the bond in the substrate and the enzyme can continue to repeat the process. Catalase is an enzyme found in almost all living organisms. In the human body it is an enzyme that is produced by our liver to break down hydrogen peroxide into water and oxygen. Even though hydrogen peroxide is naturally produced by our body as a byproduct of our metabolic process, it is very toxic to our body.
Effect of Enzyme Activity on Temperature Aim: The aim of this experiment is to investigate how effectively the enzyme amylase breaks down starch at different temperatures Research Question: How does the increase in temperature affect the time taken for amylase to breakdown 2ml of starch? Purpose: Background Information: Enzymes are biological catalysts that comprise the largest and most highly specialized class of protein molecules. Enzymes act as catalysts to increase the rates of chemical reactions. A fundamental property of enzymes is their specificity. Various enzymes have unique shape and chemical composition that creates a site, called and active site.
When these factors vary, enzymes may change in shape so it will not be able to bond to the specific substance anymore. What is trypsin? Trypsin is produced in the pancreas as typsinogen originally allowing metabolic control. It is used widely in various biotechnological processes because it is very easy to be purified. Method: Material: • Trypsin • Casein • Water bath (to keep the temperature constant) • Colorimeter (to measure the rate of enzyme activity) • Thermometer • Test Tubes (to contain the casein and the buffer solution) • Stop watch (to control and measure the time) • Distilled water (to mix with trypsin to produce the buffer solution) • Test tube rack (to prevent the tubes rolling and smashing) Protocol: • Put 2.5 cm³ of 5% with reconstituted casein in 6 of the test
Digestive enzymes are hydrolytic enzymes. Their substances, or the molecules on which they act are organic food molecules which they breakdown by adding water to the molecular bonds, thus cleaving the bonds between the subunits or monomers. Digestive enzymes can function outside the body cells; their activity can be studied by test tubes (Marieb and Mitchell 2010). This experiment attempts to re-create the breakdown process that is normally done via digestion with Iodine as a vital component. It can be expected that once amylase reacts with the starch, maltose will then be broken down and less starch will be visible and more sugar will be apparent thus causing the solution mixed with iodine to become lighter and lighter.
This is a very essential part of hydrolysis as biomass consists of very large organic molecules and for this process to work efficiently we must break the large particles down into smaller particles. Think of it the same way our stomach works, before we digest the food that we eat, we must break it down. The large polymers, mainly consisting of proteins, fats and carbohydrates are broken down into amino acids, fatty acids and simple sugars. During this process hydrogen and acetate are also produced. These byproducts will be used in a later anaerobic digestion stage.
Enzymes are proteins that are used to speed up these reactions without being consumed by them. The activity of these enzymes can be altered by changing their environments, such as enzyme specificity (speed only a reaction that contains their substrate), increasing and decreasing temperature, concentration level, or adjusting the pH level. Catalase is a catalyst that digests potent hydrogen peroxide and converts it into H2O and O. It is due to this hydrogen peroxide digesting ability that we used catalase in this experiment. To record the role that environment plays in the reaction of an enzyme, we exposed the enzyme to various changes in temperature, concentration, and pH.
It also assists in synthesizing enzymes and hormones, maintaining fluid balance, and regulating such vital functions as building antibodies against infection, blood clotting, and scar formation. There are 20 amino acids required for growth by the human body and all but eight can be produced in your body. These eight amino acids are called essential amino acids and they are supplied by supplements and food sources. The other twelve non-essential amino acids are made within the body, but both essential and non-essential amino acids are needed to synthesize proteins. This means that insufficient supply of amino acids in the body can limit the amount of protein it can use to build muscle.
Catalase Lab Report Introduction Enzymes are proteins that speed up the rate of reactions that would otherwise happen more slowly. Enzymes work by fitting into certain substrates to lower the energy needed for the process to work. This is similar to the lock and key. The key being the substrate and the lock being the enzyme. If the substrate (key) doesn’t fit it won’t work with the enzyme (lock).
Urea is formed in the liver as an end product of protein metabolism and is carried to the kidneys for excretion. Nearly all kidney diseases cause inadequate excretion of urea, elevating BUN levels in the blood. Urea production will be increased during increased protein catabolism and increased protein digestion or decrease in glomerular filtration rate.Serum urea is measured by enzymatic method.In this method, urea is hydrolyzed enzymatically by urease to yield ammonia and carbon dioxide. The ammonia thus produced is converted to glutamate in a reaction catalyzed by L-glutamate dehydrogenase (GLDH).The reaction monitored by measureing the rate of decrease in absorbace at 340nm, due to NADH is oxidized to NAD