Enzyme has an active site in a specific shape because of its tertiary structure. Enzyme works for binding with substance of a specific shape that fits in it and break down the substance. Enzymes denature due to various factors. The temperature, PH level, and the concentration of the substance influence enzyme activities. When these factors vary, enzymes may change in shape so it will not be able to bond to the specific substance anymore.
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.
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.
Investigation of the effect of Substrate concentration on Catalase activity Research Question: To investigate enzyme kinetics, using catalase enzyme from the yeast extract. Background Information: Enzymes are proteins which catalyze reactions that take place in the body or they increase the rate of the biological reactions. In an enzyme catalyzed reaction, the substrate binds to the active site and forms the enzyme-substrate complex with the enzyme. The enzyme breaks the bonds present in the substrate; the final product of this reaction leaves the enzyme which remains unchanged after the reaction. Catalase is a substance which is produced by the liver to break down hydrogen peroxide.
I chose to do an experiment on ‘How temperature can affect the rate of enzyme activity in the liver?’ Temperature affects the “speeds of the molecules, the activation energy of the catalytic reaction and the thermal stability of the enzyme and substrate.” (2) At different levels of temperature the affects on the enzyme in the liver varies. The reason for this is because; “their molecules have low kinetic energy and collisions between them are less frequent.” (2) In other words at low temperatures, enzymes become ‘deactivated’. (2) Whereas on the other hand when the temperature is increased the activity that occurs in the
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.
Effects of Volume on Enzyme Activity Biology 103 Second Spring Semester Introduction Enzymes are biological catalysts that catalysis biochemical reactions in living calls. The purpose of a catalyst is to decrease the activation energy required for a reaction to happen naturally. Enzymes increase the reaction rate by molecules by two hundred million times faster opposed to if there no enzyme present. During a catalyzed reaction, a substrate binds to an active site which in-turn forms an enzyme-substrate complex. This is where the reactions occurs.
5. Describe how temperature and pH affect sucrase activity. Introduction Enzymes are usually protein molecules that act as biological catalysts. A catalyst greatly increases the speed of a chemical reaction by lowering the activation energy necessary to get the reaction started without itself being altered or consumed. On the surface of the enzyme is an active site that temporarily binds the reactants or substrates forming an enzyme-substrate complex.
Hydrogen Peroxide at high concentrations can be lethal. Catalase is there to help with the processes of breaking it down to assure that this doesn’t happen. The purpose of this lab was to help us understand what happens when an enzyme works with a substrate to make the reaction faster. It was to help show us what the effects of pH and temperature on the enzyme’s reaction. My hypothesis for the experiment was that the optimum temperature for catalase to function is 98.6o F because this is the optimum temperature for the human body.
The higher the hydrogen ion concentration, the lower the pH. A change in pH above or below will affect the enzyme rate of reaction and the actual activity of the enzyme. Changes in pH lead to the breaking of the ionic bonds that hold the tertiary structure of the enzyme in place. As a result, the active site of the enzyme denatures resulting in the substrate not being able to fit like a ‘lock and key’ mechanism. Hypothesis I predict that the outcome is that when the enzyme is catalysing at the pH 7, the volume of oxygen gas produced will be greatest as we already know that the enzyme catalyse is at its most active when exposed to its pH optimum (pH 7).