Enzyme Lab Report

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

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 essentially proteins and will only act in an aqueous environment. An enzyme is specific for a certain reaction or

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.

What does the changes in the amount of substrate on an enzyme’s reaction effect on?

Enzymes have things called ‘Active Sites’ this the spot where substrates bind and chemical reaction takes place. Each enzyme has a different shape, this allows the enzyme to receive only one type of

Experimental strategy: The experimental approach that will be taken, in order to test my hypothesis involves the use of the spectrophotometer. This machine will enable me to examine the effect of different substrate concentrations on the rate of reaction (Bio 5LA- Lab # 5, pp.3). In brief, I will have to take varying concentrations of a substrate, add an enzyme to each of tubes filled with different concentrations, and rapidly place the tube into the spectrophotometer, in order to measure the time it takes the varying substances to change color. As a result, when the color change is visible in any of the varying substrate concentrations, it will be safe to say that, the enzyme has reacted with the substrate, to form an enzyme-substrate complex. Similarly, the time it took for a color change to happen, will allow me to observe and record the rate at which each reaction

After the substrate solution was added, five drops of the enzyme were quickly placed in tubes 3, 4 and 5. There were no drops of enzyme added in tubes 1 and 2 and in tube 6 ten drops were added. Once the enzyme solution has been added the tubes were then left to incubate for ten minutes and after five drops of DNSA solution were added to tubes 1 to 6. The tubes were then placed in a hot block at 80-90oC for five minutes. They were then taken out after the five minute period and using a 5 ml pipette, 5 ml of distilled water were added to the 6 tubes and mixed by inversion. Once everything was complete the 6 tubes were then taken to the Milton Roy Company Spectronic 21 and the absorbance of each tube was tested.

Saturation of substrates was a phenomenon that was observed in Part II of the experiment. This was referenced from later in the discussion. When the enzyme activity from this experiment was compared to Enoch’s work, (Enoch) it was stated that he found that in certain liver cells of rats, enzyme activity would stop suddenly. The study proposed that the lower Enoch dropped the substrate concentration within these cells, the less activity he could record. This proved to both his data and to the date from this experiment that the substrate was necessary for catalysis, because as enzyme concentration rose, substrates bound more quickly to the active site of an enzyme. Once all substrates in the mixture were changed to products, the enzyme was stationary because it had no more substrate to catalyze. This meant that in order for the reaction to continue, substrate concentration had to increase.

The enzyme activity is affect by its surroundings especially when pH, temperature, and the concentration of activator and inhibitor are involved. When the pH rise or drops out of the enzyme stretch in tolerance, the structure of the protein can be alter or in other worlds denatured. Most of the enzyme in the bodies of humans

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.

Although we might not always acknowledge this small proteins, enzymes have come to be revolutionary when it comes to our survival. This is because enzymes are an example of catalysts, which affect the rate at which a chemical reaction occurs by speeding up. Moreover, this is imperative for our survival because chemical reactions provide the energy required by our bodies to perform several life processes that allow us to carry out many of the activities we perform as part of our everyday life. Thus, an enzyme's ability to function properly has become a major factor in our body's ability to function properly and maintain homeostasis. Unfavorably, however, there are some factors that can negatively affect an enzyme's ability to

Most enzymes require specific conditions for them to efficiently function. These conditions include temperature, concentration of salt, and the pH level. If the optimum conditions for an enzyme are changed, the enzyme may denature and deactivate. As a result, the enzyme would not be able to catalyze the reaction, and the reaction rate would considerably decrease (Worthington 2010).

Enzymes are small biological molecules that significantly speed up the rate of chemical reactions. Enzymes are a vital element for life and serve a vast amount of important functions inside the body, such as aiding in digestion and metabolism. Some enzymes help break down larger molecules into smaller pieces that can be easily absorbed by the body. Enzymes are highly selective catalysts, which means each enzyme catalyzes only one type of reaction. This occurs because substrates with which an enzyme acts, has a special that compliments the enzymes active site, fitting together like pieces of a puzzle. There are two models in regards to how the enzyme and catalyst fit together, the lock-and-key model and the induced-fit model. In the lock-and-key model, the active site of an enzyme is specifically designed to fit with specific substrates. In the induced-fit model, the active site and substrate don't fit perfectly together but instead, they both can alter their shape in order to connect. PH, Temperature and Concentration affect the rate of enzyme activity. Most enzymes would denature when exposed to extreme acidic or basic PH. As temperature rises molecules will have a greater kinetic

This lab report will explain the following: What is an enzyme? How do abiotic or biotic factors influence the rates of enzymatic reactions? Which factors can change the rate of enzyme activity? The relationship between enzyme structure and function. And, finally, which factors that affect enzyme activity could be biologically important? An enzyme speeds up the chemical reaction in a biological system. To do so, the enzyme lowers the activation energy. Activation energy is the energy that is needed for molecules to start reacting with each other. Enzymes form an enzyme-substrate complex which reduces the energy required for that specific reaction to occur. Enzymes have specific shapes/structures that regulate their functions. The active site