Investigating The Rate Of Enzyme Activity Within A Experiment Essay

In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or

Enzymes are biological catalysts, which means it decreases activation energy in reactions. The lower activation energy in a reaction, the faster the reaction rate. Many enzymes alter their shape when they bind to the activation site. This is called induced fit, meaning for the enzyme to work to its full potential it has to change shape to binding substrate. The location of enzyme’s activation site is on the surface of the enzyme, where the binding of substrates take place. Enzyme activity can be influenced by a variety of environmental factors. If the concentration of enzyme is low, and there is a great deal of substrate, then increasing enzyme concentration results in more molecules available to convert substrates to products. Thus, increasing enzyme concentration can increase reaction rate. If substrate concentrations are low, and many of the existing enzymes are idle because of a lack of substrate, then adding enzyme will have no effect on reaction rate. Enzyme concentration affects the enzyme activity, because the more enzyme concentration the faster the reaction rate, until it hits it’s limiting factor. When substrate concentration is increased, it also increases rate of reaction. Temperature plays an important

Used to see if the temperature of the water is at 37oc – 40oc and if

Enzyme catalysis is dependant upon factors such as concentration of enzyme and substrate, temperature and pH. These factors determine the rate of reaction, and an increase in temperature or pH above the optimum will

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

If different amounts of enzyme solution are added to the hydrogen peroxide, then the highest amount of enzymes will have the greatest reaction rate because enzymes catalyze reactions, meaning more oxygen will be produced quicker.

Background and Introduction: Enzymes are proteins that process substrates, which is the chemical molecule that enzymes work on to make products. Enzyme purpose is to increase the rate of activity and speed up chemical reaction in a form of biological catalysts. The enzymes specialize in lowering the activation energy to start the process. Enzymes are very specific in their process, each substrate is designed to fit with a specific substrate and the enzyme and substrate link at the active site. The binding of a substrate to the active site of an enzyme is a very specific interaction. Active sites are clefts or grooves on the surface of an enzyme, usually composed of amino acids from different parts of the polypeptide chain that are brought together in the tertiary structure of the folded protein. Substrates initially bind to the active site by noncovalent interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions. Once a substrate is bound to the active site of an enzyme, multiple mechanisms can accelerate its conversion to the product of the reaction. But sometimes, these enzymes fail or succeed to increase the rate of action because of various factors that limit the action. These factors can be known as temperature, acidity levels (pH), enzyme and/or substrate concentration, etc. In this experiment, it will be tested how much of an effect

In the first part of the enzyme lab, we mixed a substrate and an indicator with an enzyme. There was also a neutral buffer in each of the chemical mixtures. The neutral buffer regulated the pH to around 7. We got a color palette and once we mixed each together, we observed and saw a change in the color of the substance. The darker and more brown the substance got, the more oxygen produced by the reaction. Our results showed that amount of oxygen produced increased about 10% a minute until it sort of equilibrated at 4 minutes and didn’t change to the fifth minute mark. If we were to change anything we did in the experiment, we would make our comparisons to the chart more precise. Overall we thought it

As stated in the introduction, three conditions that may affect enzyme activity are salinity, temperature, and pH. In experiment two, we explored how temperature can affect enzymatic activity. Since most enzymes function best at their optimum temperature or room temperature, it was expected that the best reaction is in this environment. The higher the temperature that faster the reaction unless the enzyme is denatured because it is too hot. Similarly, pH and salinity can affect enzyme activity.

The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,

Enzymes are defined as catalysts that speed up chemical reactions but remain the same themselves. The shape of an enzyme enables it to receive one type of molecule and that specific molecule will fit into the enzyme’s shape. Where a substance fits into an enzyme is called the active site and the substance that fits into the active site is called a substrate. Several factors affect enzymes and the rate of their reactions. Temperature, pH, enzyme concentration, substrate concentration, and the presence of any inhibitors or activators can all affect enzymes. Temperature can affect enzymes because if the temperature gets too high, it can cause the enzyme to denature. pH can affect an enzyme by changing the shape of the enzyme or the charge properties of the substrate so that either the substrate cannot bind to the active site or it cannot undergo catalysis. Every enzyme has an ideal pH that it will strive in. Increasing substrate concentration increases the rate of reaction because more substrate molecules will be interacting and colliding with enzyme molecules, so more product will be formed. Inhibitors can affect enzymes and the rate of their reactions by either slowing down or stopping catalysis. The three types of inhibitors include competitive, non-competitive, and substrate inhibition.

An Enzyme is a protein, which is capable of starting a chemical reaction, which involves the formation or breakage of chemical bonds. A substrate is the surface or material on or from which an organism lives, grows, or obtains its nourishment. In this case it is hydrogen peroxide. This lab report will be explaining the experiment held to understand the effects of the changes in the amount of substrate on the enzyme’s reaction.

However, the rate of reaction only increases for a certain period of time until there is lesser substrate molecules than the enzyme molecules. The increase of enzyme concentration does not have effect if there are lesser substrate molecules than enzyme molecules initially.

Abstract: Enzymes, catalytic proteins that at as catalysis which makes the process of chemical reactions more easily. There are two main factors that actually affects enzymes and their functions which are temperature and pH. Throughout this experiment, the study how pH and peroxidase affects each other and the enzyme was made. The recordings of how the enzymes responded when it was exposed to four different pH levels to come up with an optimum pH which was predicted in the hypothesis and the IRV at the end.

Enzymes are proteins that act as catalysts and help reactions take place. In short, enzymes reduce the energy needed for a reaction to take place, permitting a reaction to take place more easily. Some enzymes are shape specific and reduce the energy for certain reactions. Enzymes have unique folds of the amino acid chain which result in specifically shaped active sites (Frankova Fry 2013). When substrates fit in the active site of an enzyme, then it is able to catalyze the reaction. Enzyme activity is affected by the concentrations of the enzymes and substrate present (Worthington 2010). As the incidence of enzyme increases, the rate of reaction increases. Additionally, as the incidence of substrate increases so does the rate of reaction.