Enzyme Lab

Amylase experiment # 2 was done to see how the pH affected the efficacy of the enzyme. First we collected all of the materials that were necessary to make this experiment. We needed five clean test tubes, the following standard solutions, 1% Starch Solution pH 3,1% Starch Solution pH 5,1% Starch Solution pH 7,1% Starch Solution pH 9,1% Starch Solution pH 11

Introduction:Enzymes are made up of proteins which are produced within living cells and act as catalysts which speed up chemical reactions. They are made up of long chains of amino acids containing carbon, hydrogen, oxygen and nitrogen. Enzymes are structured to be

7 Corvettes These are used instead of test tubes as corvettes are required if a colorimeter is to be used. One corvette is needed for each pH and one for the control. These can then be reused for the repeats. Syringe calibrated at 0.1 cm³ intervals

The purpose of this experiment was to determine (1) the reaction rate of an amylase enzyme in starch and (2) the environmental factors that can affect the enzymatic activity. The hypothesis, in relation to the enzymatic activity by variables such as the substrate concentrations, temperature, PH and chemical interactions on the rate of reaction, stated

The first experiment begun by filling a 600-ml beaker, almost to the top, with water. Next, a 10-ml graduated cylinder was filled to the top with water. Once water was added to the beaker and graduated cylinder, a thumb was placed over the top of the graduated cylinder. This would ensure that no water was let out and no bubbles were let into the graduated cylinder. Next, it was turned upside down and fully submerged into the beaker. Then, a U-shaped glass tube was attained. The short end of the glass tube was placed into the beaker with the tip inside of the graduated cylinder. Next, a 50-ml Erlenmeyer flask was received. After, 10-ml of substrate concentration and 10-ml of catalase/buffer solution were placed into the flask. A rubber stopper was then placed on the opening of the flask. After adding these, the flask was held at the neck and spun softly

Measure and add 5cm3 of buffer solution using a measuring cylinder with the pH 3 into a test tube using a pipette and place the potato cylinders into the test tube.

enable the substrate to bind to the enzyme and form the enzyme substrate complex and

During these experimental procedures, the implication of multiple different temperatures on fungal and bacterial amylase was studied. In order to conduct this experiment, there were four different temperatures used. The four temperatures used were the following: 0 degrees Celsius, 25 degrees Celsius, 55 degrees Celsius, and 80 degrees Celsius - Each temperature for one fungal and one bacterial amylase. Drops of iodine were then placed in order to measure the effectiveness of the enzyme. This method is produced as the starch test. The enzyme was tested over the course of ten minutes to determine if starch hydrolysis stemmed. An effective enzyme would indicate a color variation between blue/black to a more yellowish color towards the end of the time intervals, whereas a not so effective enzyme would produce little to no change in color variation. According to the experiment, both the fungal amylase and bacterial amylase exhibited a optimal temperature. This was discovered by observing during which temperature and time period produced a yellow-like color the quickest. Amylase shared a similar optimal temperature of 55 degrees Celsius. Most of the amylases underwent changes at different points, but some enzymes displayed no effectiveness at all. Both amylases displayed this inactivity at 0 degrees Celsius. At 80 Celsius both the enzymes became denatured due to the high temperatures. In culmination, both fungal and bacterial amylase presented a array of change during it’s

test the pH of the amylase a drop of the solution should be put on pH

Introduction An enzyme is a catalytic molecule that speeds up reactions to a rate that limits at equilibrium. When a substance is going to have a reaction, it will require a activation energy and the enzyme lower that activation energy. The ability to do this comes from the substrate that the enzyme contains. In the enzyme molecule, there are active sites where it can interact with a substrate and then catalyzes reactions.

Background Research Enzymes are tertiary and quaternary structures of proteins and biological catalysts that accelerate the rates of chemical reactions. Enzymes are significant in that they are not permanently changed in the process and may be reused. Enzymes speed up chemical reactions by lowering the activation energy needed to start a chemical reaction. The process of speeding up a chemical reaction via the use of enzymes begins when a substrate, the substance (reactant) that an enzyme acts upon, binds to the active site of an enzyme. The active site is the region on an enzyme where substrate binds to and undergoes an accelerated chemical reaction; it is where catalysis occurs.

This experiment consisted of setting up a control group of starch in various temperature and then placing both fungal amylases and bacterial amylases in a mixture of starch and placing the solution of amylase and starch in various temperatures of water. After a certain amount of time- different amount of time needs to be used in order to have reliable results- iodine is added in a well on spot plates, then two drops of the mixture of amylase-starch is added from each temperature used, by adding iodine into the plates the mixture will show how much starch was hydrolyzed, this is used to calculate the amount of

In our third experiment we will perform the reaction with three different levels of pH in the solution. If the pH of the solution is changed, then the enzyme cannot work properly and will not result with an ideal initial reaction rate. Substrate and enzyme molecules are attracted to each other because of their opposite charges. When the pH is changed it can affect the charges between the two different molecules, causing them to repel from one another. This repulsion will defeat the purpose of using an enzyme to speed up the reaction rate, because very few molecules will be able to work in the

Amylase is an enzyme that is located in human saliva. It is solely accountable for breaking down starch as a way to start the breakdown of food and is one of the first steps of digestion. The time at which the enzyme starts the chemical reaction with starch is called the reaction rate. In order to study how amylase works against starch, this experiment consisted of two tests; each testing a different condition of amylase. The first test was to simply study the reaction between saliva and amylase and note the reaction rates. The second test was to see if increasing the pH would decrease the reaction rate or halt it all together. Saliva was collected, diluted, and tested for reactions between starch and amylase. Another sample of saliva was collected, diluted, and had its pH increased and tested for reaction rate. The findings after the experiment was conducted aligned with the original hypothesis. The change in pH did show a significant decrease in the reaction rate.

In this lab we looked at the role of pancreatic amylase in the digestion of starch and the effect that temperature and pH has on this enzyme. Enzyme’s work as catalysts that increase the rate of chemical reactions within cells (Cooper, 2000). In order to do this, enzymes must show two essential properties: these two fundamental properties of enzymes include increasing the rate of chemical reactions without being eternally altered by the reaction and accelerating the reaction rate with keeping the reactants and products in chemical equilibrium (Cooper, 2000). Enzymatic catalysis is necessary for life. Most biochemical reactions would not occur under the mild temperatures and pressures