Enzymes Lab Report

Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is

10 microliters of the sample is then added and the assay absorption is measured at 340nm. If absorbance was above 1.5, samples were diluted.

Hydrogen Peroxide, or H2O2, is harmful to most living organisms but can be converted to oxygen and water before the damage is permanent. This is thanks to enzymes, the biological catalysts that increase the rate of reactions. Enzymes can be studied by measuring the rates of enzyme-catalyzed reactions. This can be done in a number of ways, including measuring the pressure of the product as it appears, measuring the rate of disappearance of the substrate, and measuring the rate of appearance of a product.

In part II of the lab six small glass tubes were obtained in a test tube rack. Ten drops of distilled water were then added to test tube 1, five drops to tubes 2-4, and no drops in tubes 5 and 6. Five drops of 0.1M HCl were added to test tube 5 and five drops of 0.1M NaOH to test tube 6. Five drops of enzyme were then added to all tubes except tube 1. Tube 3 was then placed in the ice bucket and tube 4 was placed in the hot bucket at 80-900C for five minutes, the remaining tubes were left in the test tube rack. After the five minutes five drops of 1% starch was added to every tube and left to sit for ten minutes. After ten minutes five drops of DNSA were then added to all the tubes. All the tubes were then taken and placed in the

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.

To start the serial dilution and create a standard, 100 mL of 0.00005M was prepared by adding 5 mL of the 0.001M potassium phosphate solution to a 100 mL flask. That solution was diluted with deionized water up until the 100mL line. Afterwards, 20mL of the first standard were pipetted into a 50mL volumetric flask, which was then filled with deionized water in order to dilute the solution to a concentration of 0.00002M. 25 mL of the second standard was then pipetted into another 50mL volumetric flask, which was then diluted to 0.00001M by then adding deionized water to the flask until it filled up. A “blank” solution was prepared in order to calibrate the spectrometer. This was done by taking 10mL of deionized water and pouring it into a 50 mL beaker, and adding 5mL of AVM.

reaction rate increases. If the temperature of an enzyme gets to high the reaction rate will slow

The stock solution for each test drug was diluted with potassium phosphate buffer pH 7.4 to obtain 7-9 different concentrations. Each concentration was prepared with three replicates. A flow diagram of the preparation of the test solutions for GC-MS/MS is depicted in figure 5-2.

3.1.9 Inoculation of microorganism inside enzyme production broth Pure fungi isolates were cultured on half strength PDA to enhance spore production. After 8 days incubation, 5ml sterile distilled water was added on to the agar using aseptic techniques. The top of the agar was scrapped with a sterile hockey stick glass rod to suspend the spore. Using hemacytometer, the concentration of the spore was determined.

The same solution of 0.5 ml BSA was then added from test tube 1 to the test tube 2 after being properly mixed, and from test tube 2 the solution was being added to test tube 3, and so forth all the way up to test tube 5, with the same exact procedure. From the last tube, we then disposed the 0.5 ml solution. After above procedures, we now labeled another test tube “blank”; 0.5 ml blank distilled water was purred into the tube with the serial dilution of 1:10. We also had a tube C labeled “unknown” with the same 0.5 ml of solution. And after adding 5ml of Coomassie Blue to each tube (1-5) and to the blank, the result of absorbance was read at 595 nm.

Chemical reactions happen in every cell in an organism and enzymes are very helpful and sometimes imperative for these reactions. Enzymes are biological catalysts with the purpose of increasing the rate of reaction of the chemical reactions happening inside the body (Castro, 2014). Enzymes are typically proteins which means that they are made up of polypeptide chains which take their shape using hydrogen bonds. Enzymes work by optimising the conditions for a reaction to take place and it is required for some reactions to even be able to take place.

The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,

Of the many functions of proteins, catalysis is by far the most vital. When catalysis is not present, most reactions in the biological systems take place very slowly to produce at an adequate pace for metabolising organism. The catalysts that take this role are called enzymes. Enzymes are the most efficient catalysts; they can enhance rate of reaction by up to 1020 over uncatalysed reactions. (Campbell et al, 2012).

In this experiment, I wanted to determine the effect that basic or alkaline solutions have on the enzyme, polyphenol oxidase that is found in apples. Given the idea that acidic solutions reduce the reaction rate of this enzyme, I conducted this experiment to see if alkaline solutions do the opposite and instead increase the reaction rate. With this in mind, the experiment was executed using two basic solutions to increase the credibility of the results which proved that alkaline solutions increase the reaction rate. I was able to determine this by comparing the apples that were treated with the control group, from this I understood that both the untreated and treated apples had a similar reaction rate. Though all of the apples had some brown

Introduction: Chemical reactions are constantly happening. Within a cell, these reactions serve several functions, everything from digestion to DNA replication. For any chemical reaction to occur, a certain energy threshold has to be reached (Royal Society of Chemistry, 2004). An example of this can be seen when water boils. Water does not just boil on its own but rather absorbs the heat energy from its environment to induce boiling.