Effects Of Concentration On The Rate Of Reaction

Enzymes are biological catalysts that facilitate specific chemical reactions (Raven, et al., 2014). Enzymes do their job by

Enzymes are proteins that act as a catalyst in bringing about specific biochemical reactions when met with particular substrates. Substrates will merge into a suitable area of the enzyme called an active site – this becomes the enzyme/substrate complex. Once the substrate is attached to the active site, the substrate will undergo a procedure where the substrate is modified and released as a product. There are different types of this that can occur, where either a chemical bond is broken in a substrate to produce two separate products; as in the ‘Induced-Fit’ model illustrated in figure 1.a. Chemical bonds can also be built between two substrates to produce a single product.

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

Copeland, R. A. (2000). A Practical Introduction to Structure, Mechanism, and Data Analysis: Enzymes (Second ed.).

The experiment was carried out to investigate the effects of the increase in the enzyme concentration on the rate of reaction. By using self investigative and experimental skills, the experiment was done in order to determine how the rate of reaction will be altered, whether it will increase, decrease or remain constant when the different concentration of enzymes added.

References: "Biomolecules:Enzymes." Competitive Inhibition. Chempages Netorials, 2006. Web. .<http://www.chem.wisc.edu/deptfiles/genchem/netorial/modules/biomolecules/modules/enzymes/enzyme5.htm>.

Enzymes are essential proteins that lower the activation energy and provide standard living needs. They regulate pigments, breakdown starches and proteins, act as treatments for heart attacks, cancer and replace old tissues (Alberte et al., 2012). Enzymes act as catalysts which regulate how metabolic processes work. Enzymes are three-dimensional shapes that fit into a reactant molecule known as a substrate. This substrate binds to its specific home known as an active site. When a substrate binds to the active site it creates a process known as the enzyme-substrate complex which creates a final product. The purpose of an active site is to determine the specific characteristics of each enzyme for example the charge, shape and hydrophobic/hydrophilic (Alberte et al., 2012). During this process, the substrate’s chemical bonds are being modified but the enzyme itself is not changed or

Enzymes are present in all living things. These specialized proteins speed up chemical reactions fast enough to sustain life . Since enzymes are a huge topic to even begin to cover, we tested a

Enzymes are protein catalysts, which are substances that speed up chemical reactions without being consumed in the process. They are macromolecules consisting of hundreds of amino acids conformed together. A small part of the enzyme, called the active site, participates in the catalysis of biochemical reactions. (Novozymes) Biological substrates are shaped to fit into the active site of their specific enzyme; enzymes will not bind to isomers of their substrate in most cases. The unique arrangements of amino acids that conform together to produce the three-dimensional structure determine the function of the enzyme. The slightest changes in the sequence of amino acids on the string impact the structure of the protein causing a change in function. Subsequently, this change could cause the enzyme to have affinity for a different substrate and treat it differently. (Novozymes) One of the most important functions of enzymes is their ability to decrease the activation energy, which is the amount of energy, generally in the form of heat, needed to commence a chemical reaction. This function is crucial to mammalian bodies due to the fact that proteins would denature, lose their three dimensional structure, in the high temperatures used to start chemical reactions. In addition to heat, environments with varying acidity outside of their optimum range, which is different for each protein, cause the proteins to

An enzyme is a protein that increases the rate of a chemical reaction by lowering the activation energy of the reaction. This enables the reactant molecules to intake sufficient amount of energy to reach the transition state. The reactant that an enzyme acts on is referred to as the substrate. After the substrate molecule binds to an enzyme to form an enzyme-substrate complex, the enzyme converts the substrate to products of the reaction. The reaction that is catalyzed by an enzyme is very specific meaning that the enzyme will only bind to its specific substrate. For example, sucrase, an enzyme, will only bind to sucrose molecule. This specificity is due to a molecular recognition mechanism and it operates through conformational as well as structural similarities between the enzymes and the substrate.

Specific enzymes made up of proteins are used in biology to speed up a chemical reaction of any kind. Since a spontaneous chemical reaction can occur without help from any outside energy it could potentially prolong the reaction to where it becomes almost unnoticeable since it can take years for it to happen. For this reason, enzymes take action as a catalyst that speed up the reaction rate without completely being absorbed (Campbell et al., 2010). Enzymes are a form of regulation that allow for a through pathway in chemical reactions. It is able to perform as a catalyst by lowering the activation energy which is the energy required to drive the reactant to the top of the energy barrier allowing the downhill part to begin. An

In competitive inhibition, an inhibitor that resembles the normal substrate binds to the enzyme, usually at the active site, and prevents the substrate from binding.[9] At any given moment, the enzyme may be bound to the inhibitor, the substrate, or neither, but it cannot bind both at the same time. During competitive inhibition, the inhibitor and substrate compete for the active site. The active site is a region on an enzyme which a particular protein or substrate can bind to. The active site will only allow one of the two complexes to bind to the site therefore either allowing for a reaction to occur or yielding it. In competitive inhibition the inhibitor resembles the substrate therefore taking its place and binding to the active site of

Competitive inhibitor is a molecule similar to the substrate but unable to be acted on by the enzyme competes with the substrate for the active site. Generally speaking, the greater the concentration of inhibitor, the longer this will take. However, since the enzyme's overall structure could not affected by the inhibitor, it is still able to catalyze the reaction on substrate molecules that do bind to an active site.

The lock and key model has been one theory that has been proposed to show how enzymes work. This model shows how a substrate is binded to the enzyme’s active site. This model further shows how specific and accurate the substrate has to be in terms of its complementary shape and size in order to fit in into the enzyme’s active site. As a result of this structure, only certain amount of compounds will be able to fit successfully. When the substrate and active site bind to one another, a chemical reaction takes place that eventually will release the products that have been formed, an enzyme-substrate complex will be formed once the interaction of the substrate and active site of the enzyme happen. An enzyme-product complex can be made which can

The experiment was carried out to investigate the effects of the increase in the enzyme concentration on the rate of reaction. By using self investigative and experimental skills, the experiment was done in order to determine how the rate of reaction will be altered, whether it will increase, decrease or remain constant when the different concentration of enzymes added.