Lysozyme Lab Report

Enzymes are catalysts that function to speed up reactions; for example, the enzyme sucrose speeds up the hydrolysis of sucrose, which breaks down into glucose and fructose. They speed up reactions but are not consumed by the reaction that is taking place. The most important of the enzyme is the shape as it determines which type of reaction the enzyme speeds up. Enzymes work by passing/lowering and energy barrier and in doing so; they need to bind to substrates via the active. Once they do, the reaction speeds up so much more quickly than it would without the enzyme. Coenzymes and cofactors aid the enzyme when it comes to binding with the substrate. They change the shape of the active site so the substrate can bind properly and perform its function.

2. We measured 1 mL of turnip peroxidase (the enzyme) and 3 mL of neutral buffer (pH corresponding to the test tube number i.e. pH 5 in test tube 5) with a syringe and disposed it into tubes 3, 5, 6, 7, 8, and 10

bonds and taking a glucose molecule off of the structure (Ball, Vialle, Alonso-Casajus, Duavillee, Munoz, Baroja-Fernandez, Moran-Zorzano, Eydallin, Pozueta-Romero, 2006). The conditions for the reaction of Phosphorylase and

8. If an enzyme is present, it also lowers the activation energy needed to get the reaction started.

16a. A water molecule gets added to a disaccharide to split it into two monosaccharides.

To understand how and why the experiment was performed, one must understand what enzymes and substrates are. Enzymes are defined as proteins that are capable of speeding up a chemical reaction by reducing the amount of activation energy needed to catalyze that reaction (Raven, Johnson and Mason 2014). Enzymes regulate these biochemical processes

As mentioned in question two, pH is another important factor regarding how active an enzyme could be. Although not all enzymes have the same optical pH levels, a majority of enzymes work the most effectively when the pH of their environment is between six and eight. If most enzymes are put in more acidic or alkaline environment, the enzymes would no longer function and would be irreversibly damaged. For example, the enzymes would not form the proper shape to bond with the substrates or they would not be able to bond with the substrates. As a result, the imbalance of the pH level would inhibit the rate of reaction since reactions would no longer be able

In this study, the effects of temperature and pH were measured on the catalytic ability of the enzyme catechol oxidase (also known as tyrosinase, diphenol oxidase, or polyphenal oxidase). Enzymes are defined as catalysts in biological systems that lower that energy of activation or Ea of a reaction. When a substrate bonds to a the active site of an enzyme, this forms an enzyme-substrate complex. An enzyme substrate complex consists of one or more substrates bonded to the enzymes active site, which changes shape slightly when bonded to, so as to appropriately fit the substrate(s). This slight change in enzyme shape is called induced fit.

There are two major structures found in dog saliva that apply to this experiment: lysozymes and histatins. Lysozymes are enzymes that have antimicrobial capabilities. They are found in many organisms such as plants, birds, bacteria, mammals, and insects. Lysozymes were first found in the chicken egg by Laschtschenko in 1909. Many scientists have specifically tested its potential use as a natural antibiotic. Lysozymes work by hydrolyzing the peptidoglycan of bacterial cell walls. Because of this, these enzymes are more efficient when breaking down gram-positive bacteria.

Organisms cannot depend solely on spontaneous reactions for the production of materials because they occur slowly and are not responsive to the organism's needs (Martineau, Dean, et al, Laboratory Manual, 43). In order to speed up the reaction process, cells use enzymes as biological catalysts. Enzymes are able to speed up the reaction through lowering activation energy. Additionally, enzymes facilitate reactions without being consumed (manual,43). Each enzyme acts on a specific molecule or set of molecules referred to as the enzyme's substrate and the results of this reaction are called products (manual 43). As a result, enzymes promote a reaction so that substrates are converted into products on a faster pace (manual 43). Most enzymes are proteins whose structure is determined by its sequence of its amino acids. Enzymes are designed to function the best under physiological conditions of PH and temperature. Any change of these variables that change the conformation of the enzyme will destroy or enhance enzyme activity(manual, 43).

As an enzyme-catalyzed reaction may be the main reason for a reaction to occur faster, many factors can

It decreases the activation energy in reaction. When the substrate binds to the active site on enzyme, it will change the conformation of enzyme to make the enzyme-substrate complex and catalyze reactions2. The reason we want to analyze enzyme kinetic in order to quantitative biocatalysis, understand the catalytic mechanism and understand regulation of

generally act as a catalase that initially bring about a chemical reaction.” Enzymes play an

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.

W. John Albery (1976) stated that the “improvement in the catalytic efficiency of enzymes, compared with simple organic molecules, is separated into three broad types of alteration to the Gibbs free-energy profile” (Albery, 1976).