Enzymes are catalysts that lower the activation energy required to perform a reaction, thus making the rate quicker and energy efficient. Enzymes consist of an active site, which serve as the location of the chemical reaction, and is the area that the substrate will bind to. The substrate will be binded to the active site via hydrophobic interactions, hydrogen bonds, and ionic bonds. Once the substrate is attached, the enzyme will perform the chemical reaction that can either breakdown or form the new substances. An enzymes active site is stabilized by a multitude of weak reactions, that ultimately allow them to support the accelerated chemical reactions. In addition, there are many factors that may disrupt or perhaps increase the rate of …show more content…
Using this data, we shall determine how the factors promote or hinder the reactions. In my group, we were assigned substrate concentration, in which the enzyme, catalase, would originate from potatoes, and the substrate will be store bought hydrogen peroxide. The dependent variable would be the reaction rate and the independent variable, the manipulated variable, is the concentration of peroxide (substrate) in each solution. Using water, our group performed serial dilution, creating 5 different peroxide concentrated solutions: 0%, .75%, 1.5%, 2.25%, and 3.0% substrate, each having a total volume of 40 ml solution. This creates varying substrate concentrations allowing us to observe the different results from fluctuating amounts of substrate in the enzymes environment. We then obtained a container full of the enzyme (catalase), along with paper circles, which will be soaked (for 5 seconds) and absorb the enzyme. We then allowed 5 different paper holes soaked in catalase to air dry for a 10 seconds before putting each in a different diluted solution of peroxide. We dropped each paper circle in and started a timer, observing for any distinct
In this experiment the enzyme peroxidase and the substrate hydrogen peroxide were not mixed initially, instead they were both placed in separate tubes and were incubated at a specific temperature, to prevent hydrogen peroxide from undergoing any reaction with peroxidase until they both acquire the required temperature.
For example, substrate concentration, enzyme concentration, and temperature could all be factors that affected the chemical reactions in our experiment. The concentration of substrate, in this case, would not have an affect on how the bovine liver catalase and the yeast would react. The reason why is because in both instances, the substrate (hydrogen peroxide) concentration was 1.5%. Therefore, the hydrogen peroxide would saturate the enzyme and produce the maximum rate of the chemical reaction. The other factor that could affect the rate of reaction is enzyme concentration. Evidently, higher concentrations of catalase in the bovine liver produced faster reactions, and the opposite occurs for lower concentrations of catalase. More enzymes in the catalase solution would collide with the hydrogen peroxide substrate. However, the yeast would react slower than the 400 U/mL solution, but faster than the 40 U/mL. Based on this evidence, I would conclude that the yeast has a higher enzyme concentration than 40 U/mL, but lower than 400
When this substrate fits into the active site, it forms an enzyme-substrate complex. This means that an enzyme is specific. The bonds that hold enzymes together are quite weak and so are easily broken by conditions that are very different when compared with their optimum conditions. When these bonds are broken the enzyme, along with the active site, is deformed, thus deactivating the enzyme. This is known as a denatured enzyme.
Background information:. Enzyme Enzymes are protein molecules that act as the biological catalysts. A Catalyst is a molecule which can speed up chemical reactions but remains unchanged at the end of the reaction. Enzymes catalyze most of the metabolic reactions that take place within a living organism. They speed up the metabolic reactions by lowering the amount of energy.
According to the graph on amylase activity at various enzyme concentration (graph 1), the increase of enzyme dilution results in a slower decrease of amylose percentage. Looking at the graph, the amylose percentage decreases at a fast rate with the undiluted enzyme. However, the enzyme dilution with a concentration of 1:3 decreased at a slow rate over time. Additionally, the higher the enzyme dilution, the higher the amylose percentage. For example, in the graph it can be seen that the enzyme dilution with a 1:9 concentration increased over time. However, there is a drastic increase after four minutes, but this is most likely a result of the error that was encountered during the experiment. The undiluted enzyme and the enzyme dilution had a low amylose percentage because there was high enzyme activity. Also, there was an increase in amylose percentage with the enzyme dilution with a 1: 9 concentrations because there was low enzyme activity.
Purpose: This lab gives the idea about the enzyme. We will do two different experiments. Enzyme is a protein that made of strings of amino acids and it is helping to produce chemical reactions in the quickest way. In the first experiment, we are testing water, sucrose solution, salt solution, and hydrogen peroxide to see which can increase the bubbles. So we can understand that enzyme producing chemical reactions in the speed. In the second experiment, we are using temperature of room, boiling water, refrigerator, and freezer to see what will effect the enzyme.
Many factors, for example, pH and temperature affects the way enzymes work by either increasing the rate or determining the type of product produced (). The report, therefore, analyses the effects of the enzyme peroxidase in metabolic reactions and determining its optimum temperature in the reactions.
Enzymes, are macromolecules which serve as catalysts. Catalysts are a chemical that can increase the rate of a chemical reaction or slow it down, without being changed by the reaction itself. The enzyme as a catalyst promotes the activity of the reactant which subsequently produces the product.
Enzymes are large proteins that speed up chemical reactions. In their globular structure, one or more polypeptide chains twist and fold, bringing together a small number of amino acids to form the active site, or the location on the enzyme where the substrate binds and the reaction takes place. Enzyme and substrate fail to bind if their shapes do not match exactly. This ensures that the enzyme does not participate in the wrong reaction. The enzyme itself is unaffected by the reaction. When the products have been released, the enzyme is ready to bind with a new substrate.
The three-dimensional contour limits the number of substrates that can possibly react to only those substrates that can specifically fit the enzyme surface. Enzymes have an active site, which is the specific indent caused by the amino acid on the surface that fold inwards. The active site only allows a substrate of the exact unique shape to fit; this is where the substance combines to form an enzyme- substrate complex. Forming an enzyme-substrate complex makes it possible for substrate molecules to combine to form a product. In this experiment, the product is maltose.
Enzymes are the most efficient catalysts known. (1) Enzymes are biomolecules that catalyze chemical reactions by decreasing the Activation Energy (the minimum energy required in a chemical system in order for a chemical reaction to take place), which in turn increases the rate of the chemical reaction. The catalyst itself does not change or is not consumed in the reactions they catalyze. Enzymatic reactions consist of substrates and products. According to the Oxford Dictionary a substrate is “the substance on which an enzyme acts” and a product is “ a substance produced during a natural or chemical process”. (2) In general, all chemical reactions require enzymes in order to occur at an acceptable tempo for life in biological systems. Enzymes are very substrate-specific. This specificity of the enzyme molecule is due to the complementary shape of the active site of the protein and the substrate. An enzyme consists of two p...
Investigating a Factor that Affects Enzyme Activity Planning -------- Aim --- To investigate a factor which will affect the activity of catalase, whilst keeping all variables constant. Possible Independent Variables ------------------------------ Here are a number of possible independent variables that could be changed in the experiment: Independent variable Continuous/Discontinuous Easy to measure?
All Enzymes have an active site; this is the part of the enzyme where molecules with the right shape and functional groups bind to the enzyme [5]. The reacting molecule that binds to the enzyme is called the substrate [5]. Enzymes are known to have substrate specificity.
They are biomolecules that catalyze an enzymatic reaction without being consumed and do not interrupt the equilibrium of the reaction. The enzymatic reaction occurs through an enzyme-substrate binding complex in which a substrate binds to the active site of the enzyme in order to approach the transition state. Once the binding occurs, the cleavage and formation of bonds can occur through the following mechanisms: acid and base, covalent catalysis, exploitation of binding interactions, and metal ion catalysis. Enzymes are able to increase the rate of reaction by decreasing the activation energy. Understanding the enzyme-catalyzed mechanism can be explained through enzyme kinetics which entails determining the rate of reaction in response to changes in experimental parameters such as pH and substrate concentrations.
The shape of enzymes determines its function and which substrate the enzyme binds to and catalyzes is determined by the shape of its binding groove. If the shape is lost possibly due to denaturation, the enzyme cannot function anymore. The substrate is the reactant(s) of the reaction that is/are bound by the enzyme. While an active site is a region of the enzyme where binding to substrate