Enzymes: Clinical Applications
Enzymes mediate almost every single biochemical reaction, process or metabolic event in the body. Overall, enzymes are proteins whose primary function is to catalyze, increase the rate of the biochemical reactions (Champe et al., 2005). Enzymes are not only efficient in increasing the rate or velocity in a biological reaction, but also are incredibly accurate at recognizing other biochemical structures to create specific products. Taking into consideration how diverse the properties of enzymes are and their importance in the biological process of the human body, it is not a surprise how enzymes can be used as invaluable tools in the diagnosis of certain diseases, therapeutic applications and innumerable cases of clinical trials and lab analysis (Devlin, 2011). One example of the many application of enzymes in the medical field is how Proteases Pronase (Hydrolytic enzyme) and RNases are being used to remove adhesions in contaminated
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In essence, it is a circular process where an enzyme deficiency can result in the accumulation of metabolites in plasma, and then pinpoint the enzyme abnormality (Devlin, 2011). Furthermore, the presence of elevated enzyme activities in plasma may be an indication of damage somewhere in the body, such as liver, heart, skeletal muscle or any tissue (Champe et al., 2005). In other words, enzymes can be used as a lighthouse to give the clinicians an idea of what is going on in the body. Therefore, analyzing blood for cellular components is one of the convenient ways that clinicians use to look for tissue damage in the body (Devlin, 2011). In fact, it is the imperative to take into consideration the time of evaluation of the appearance and disappearance of some enzymes, increasing this way the accuracy of the diagnosis and prompt identification of the tissue affected (Devlin,
The more acidic a substance is the less oxygen it will produce when going through a chemical reaction. During the Lab “How Do Changes in pH Levels Affect Enzymes Activity”, the researcher conducted an experiment to test the effects that an acidic, neutral, and a base substance will have when combine it with hydrogen peroxide. The data table shows that HCL (acidic substance) barley produced any oxygen at all when it was combining with Hydrogen Peroxide. The pH level for HCL was 2.5; this level indicates that the substance was very acidic. When the H2O and NaOH were tested they produced more bubbles than HCL. NaoH produced a little more bubbles than HCL. The pH that NaoH produced was a 9, which is a base. H2O produced more bubbles than both substances;
Enzymes speed up metabolic reactions necessary for life. Without them certain vital processes would not take place and the body would be unable to function.
In the experiment we used Turnip, Hydrogen Peroxide, Distilled Water, and Guaiacol as my substances. On the first activity, Effect of Enzyme concentration of Reaction Rate for low enzyme concentration, we tested three concentrations of the turnip extract, and hydrogen peroxide. For the Turnip Extract I used 0.5 ml, 1.0 ml, and 2.0 ml. For hydrogen peroxide we used 0.1 ml, 0.2 ml, and 0.4 ml. We used a control to see the standard, and used a control for each enzyme concentration used. The control contains turnip extract and the color reagent, Guaiacol. We prepared my substrate tubes separately from the enzyme tubes. My substrate tube
Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is
Hold the IKI spray bottle 25 - 30 cm away from the paper towel, and mist with the IKI solution.
Enzymes are an organic substance that are made up of polymers of amino acids that help the digestive system and metabolic processes in living organisms (Funk and Wagnalls, 2016). Enzymes are able
Enzymes are a key aspect in our everyday life and are a key to sustaining life. They are biological catalysts that help speed up the rate of reactions. They do this by lowering the activation energy of chemical reactions (Biology Department, 2011).
“Enzymes are proteins that have catalytic functions” [1], “that speed up or slow down reactions”[2], “indispensable to maintenance and activity of life”[1]. They are each very specific, and will only work when a particular substrate fits in their active site. An active site is “a region on the surface of an enzyme where the substrate binds, and where the reaction occurs”[2].
Enzymes accelerate the breakdown of protein molecules and they get credit for chemical reactions that occur in all animals (Luteyn, 2006). Without enzymes our bodies would not metabolize food fast enough for us to live. Enzymes speed up the digestion process and are located in such places in our bodies as the saliva, stomach, pancreas, and intestines. One problem people face is that our production of enzymes can diminish with age, so it is important that we get our share of amino acids.
To test deviations from the standard killing curve of S. marcescens and its exposure to bacteria, we sought to discover if outside factors could influence the amount of light that affected the bacteria when it was exposed to the same strength of light for a consistent amount of time. By using different strengths of sunscreen over plastic wrap, we sought to discover any differences in the bacteria growth caused by the extra environmental factor.
This experiment showed how different situations can affect an enzyme's performance causing it to possibly become less effective. It also demonstrated how the bonding process can sometimes work faster than the breakdown process, or slower. The next step may be to understand how the relationship of enzyme breaks down versus bonding can help or hurt the various systems in the body
Enzymes are globular protein molecules that catalyze particular chemical reaction (Weem et al. 2010). They are biological catalysts which cause the process of a reaction to speed up, it does not change the reaction nor does it create different products, it allows the reaction to reach the end product faster by lowering the activation energy barrier (Reece et al. 2011). Each enzyme has an active site in which a substrate binds to which creates an enzyme-substrate complex. Each enzyme is very specific as to which substrate can bind to its active site; it is a lock and key model where only one specific substrate can fit perfectly into the active site. When the substrate fits in then the reaction is able to occur.
An enzyme deficiency is a genetic condition characterised by the inability to produce an enzyme or underproduction of that enzyme, leading to health problems caused by problems with the metabolism. (What is an Enzyme Deficiency, 2016) Some examples of deficiencies include Phenylketonuria (PKU), Acute Itermittent porphyria, Alkaptonuria, and Lesch-Nyhan Syndrome. These conditions are part of a larger family of diseases classified as inborn errors of metabolism. Such conditions may be inherited from one or both parents, or the result of spontaneous mutations. Enzymes are specialized proteins built in the body to accomplish a variety of tasks. In the metabolism, enzymes help the body break down, transport, and transform food products people ingest.
An enzyme is a macromolecule that works as a catalyst and speeds up chemical reactions through a substrate that binds to the active site of the enzyme. When this process occurs, the enzyme lowers the activation energy needed. This allows the reactant molecules to reach a state where they can complete a reaction in most temperatures. The enzyme is not consumed when a chemical reaction is taking place, however, it’s shape changes in order to create a proper space for a substrate to bind to. Since the enzyme is not consumed in the process of reactions, it can begin to lower the activating energy of another process as soon as the first process is complete and it has returned to its original shape. Without the assistance of enzymes, the pathways of metabolism in humans would be obstructed because every process would take so long (Smith et., 2015).
The enzymes inside the human body is a protein molecule which is a biological catalyst containing 3 types of characteristics. The first characteristic of an enzyme is to increase inside the human body depending on the rate of reaction. Secondly most of the enzymes inside the human body will take control and only act specifically upon one reactant, this is called the substrate, and this is the enzyme that produces products. Third most important is the enzymes strongly regulate in a circle, from a low concentration (activity) to a high concentration (activity) then back around vice versa. The enzymes can strongly be affected in the changes of both the temperature and the different ph levels. Every individual enzyme works to a certain extent reacting to a certain ph level and temperature, its activity decreasing at values above and below that point due to denaturation. For enzymes, denaturation can be defined as the loss of enough structure rendering the enzyme inactive. The tertiary structure of the enzymes and their function also includes the non covalent force in creating and determining the shape and the structure of all enzymes. The salivary amylase is found in the salivary glands inside the human body which is produced by the ptyalin. Maltose and Isomaltose are a