Enzyme Enzymes : Enzyme Type Of Proteins

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

Students will be observing normal catalase reaction, the effect of temperature on enzyme activity, and the effect of pH on enzyme activity in this experiment. The enzymes will all around perform better when exposed in room temperature than when it is exposed to hot and cold temperatures. This is based on the fact that the higher the temperature, the better the enzymes will perform, but as the temperature reaches a certain high degree, the enzymes will start to denature, or lose their function.

Enzymes analysis enables scientist to look the what, why, and how of life. A majority of reactions inside to human body are endothermic, without enzymes lowering the activation energy of these reactions life would not be possible. By understanding what the optimum environments of enzymes are, specifically with sucrase, scientist can better understand enzyme kinetics. In the body thousands of enzymes help regulate and produce chemicals. One very important enzyme K-ATPase in the body help catalyze the reaction of ATP into ADP creating a free phosphate group and helping create an sodium and potassium electrochemical gradient in the body (Peluffo et al. 2004). If the body did not keep its temperature, pH, and concentration of substrate at the optimum levels enzymes would not be able to process required energy fully and the cells would start to die. Sucrose is an important aspect of life and its reduction to glucose has to be carefully controlled in photosynthesis. In the photosystem 2 stage of photosynthesis sucrose helps stabilize water so hydrogen's electrons can be taken and used to create energy (Barry and Halverson et al.2003). As the optimum environment for an enzyme is reached the need to accurately and analytically

These results show how temperature of extreme high, or low affects enzyme activity. The highest rate of enzyme activity occurred at 37 Cº. Anything that was hotter or cold than 37 Cº slowed the reaction rate. As I thought, 100 degrees would denature the enzyme, and that was the case. The data provided shows exactly what temperatures enzymes work best, and worst. The objective was achieved as we discovered the different reaction rates under different temperatures. The results are reliable, as we know enzymes do not work well when under extreme heat or denaturation occurs. What I learned in this experiment was that enzymes don’t work well under cold temperatures because they tend to move slower. My hypothesis did not quite match, because I thought they work best at lower temperatures.

In this lab experiment the action of the enzyme Amylase was observed on starch (the substrate). Amylase changed the starch into a simpler form, the sugar maltose, which is soluble in water. Maltose then breaks down the glucose chains of starch in the pancreas and intestines. Amylase is present in human saliva, and begins to act on the starch in the food while still in the mouth. Exposure to heat or extreme PH (acid or base) will denature proteins. Enzymes, including amylase, are proteins; if denatured enzymes can no longer act as a catalyst for the reaction. In the presence of potassium iodide, starch turns a dark purple color; however maltose does not react with I2KI. The rate of fading of starch allows a quantitative measurement of reaction rate.

An experiment was performed to test how temperature variations affect enzymatic activity of the enzyme amylase. The results of the experiment will also determine the optimal temperature of the amylase enzyme. The results of the experiment provide evidence for determining the environments that the enzyme amylase would most likely be present. By determining the possible environments, one can predict what and how environmental factors will affect the enzyme amylase. Two forms of amylase (Bacterial - Bacillus licheniformis and Fungal - Aspergyllus oryzae) were combined with starch molecules at four different temperatures (0⁰, 25⁰, 65⁰, 85⁰ Celsius). The combination of starch and the amylase enzyme resulted in a visual chemical reaction that was recorded. The enzyme activity was recorded every two minutes, starting at 0 and ending at 10. The start time 0 served as the control group of the experiment. The results concluded that both bacterial and fungal amylase has an optimal temperature around 65⁰C. This was possible to determine by recording the color change of the spot plate wells. Amylase catalyzes efficiently at its optimal temperature which resulted in yellow spot plate wells. Enzymatic activity decreased when the temperature was less than 65⁰C, resulting in a green-brown well. The green wells indicated that starch wasn’t broken down completely and was still present. Temperatures greater than 65⁰C resulted dark-green wells which resembled the denaturing of

An enzyme also known as a protein, is a biological catalyst which speeds up chemical reactions by lowering the activation energy to increase the rate in which the reaction occurs. The enzyme used was amylase, which breaks down starch molecules into maltose. PH, substrate concentration, salt concentration, and temperature. When enzymes reach a low temperature, the activity is slowed down of molecule movement, but the enzyme is not destroyed. Once enzymes are placed in optimal temperatures once again, it will restore its activity to a normal rate. When enzymes reach too high above optimal temperature, the enzyme is denatured and cannot be restored. In the experiment performed the activity of breaking down starch in fungal and bacterial amylase was being tested at a range of temperatures and time. The fungal and bacterial amylase work best at optimal temperature. Amylase will function best at sixty degrees Celsius at 10 minutes when starch had been one hundred percent hydrolyzed. Hydrolyzed is the breakdown of molecules through addition of water. The experiments independent variables were the time, temperature and enzyme used. The dependent variable was the enzyme activity that broke down the starch into maltose. The controlled variables were the temperature baths, the iodine drop amount, the mixture drop amount, and location of experiment. The control group was the zero minutes without amylase at

A protein has multiple existing structures, these are the primary, secondary, tertiary and quaternary structures which occur progressively. A protein is essentially a sequence of amino acids which are bonded adjacently, and interact with one another in various ways depending on the R group that the amino acid contains. There are 20 different amino acids which are able to be arranged in any given order, thus giving rise to a potential 2.433x1018 (4.s.f) different combinations, and therefore interactions between the various amino acids.

An enzyme is a biological catalyst that speeds up the rate of reaction in certain biological functions. They play a vital role in many aspects of human physiology and are necessary for the functioning of a number of systems, for example in the digestive system to help to break down food. All enzymes have a unique active site that can fit on to a particular molecular arrangement on a target substrate; a substance e.g. carbohydrate, protein, or fat, that the enzyme is designed to breakdown. There are a number of different enzymes in the human body; each type produced specifically to perform a certain role. Enzymes are not themselves destroyed in the reaction to break down a

The purpose of this lab experiment was to determine the relationship between temperature and the rate of enzymatic activity in yeast cells. In the lab, the temperature was the independent variable. The temperatures consisted of 6°C, 24°C, 34°C, 46°C. The dependent variable in the experiment was the rate of enzymatic activity in yeast cells. The temperatures were tested by using a LabQuest and pressure probe that tested pressure inside the plastic test tube. LabQuest graphed the data and created a line of best fit that was used to determine the slope of the graph. The slope of the graph represents the rate of enzymatic activity. The slope was found for each temperature in 2 different trials. Then, the rate of enzyme activity (kPa/sec) for each temperature in the 2 trials were averaged. These averages were used to develop a graph that shows the relationship between temperature and the rate of enzyme activity. According to the results of the experiment, as the temperature increases, the rate of enzymatic activity decreases. Each enzyme has its own optimal temperature in which it can function efficiently.

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

Bacterial amylases operate at higher temperatures than do fungal amylases. Fungal amylases react rapidly at lower temperatures; fungal amylases are used as an agent for alcohol fermentation for grain (Underkofler et al, 1958). Fungal amylases is said to be denatured – change shape (Alberte et al, 2012), at high temperatures above 60° C and bacterial amylases on the other hand are stable and show little denaturing at temperatures up to 85°C 3 The question answered by the experiment is if the temperature is not within the range of the enzymes (fungal and bacterial amylase) optimal temperature (higher temperature) then will the enzymes denature and if the enzymes are placed in lower temperature from optimal the activity then will it slow down enough to stop all reaction, meaning each enzyme will not be operating efficiently. Knowing about a bacterial amylases and fungal amylases optimal temperatures are important for knowing which food products and industrial products it can be used on to conserve the product because then the producer knows about which products it can be incorporated into depending on the temperature it is manufactured at.

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 our group observed the role of pancreatic amylase in the digestion of starch and the optimum temperature and pH that affects this enzyme. Enzymes are located inside of cells that increase the rate of a chemical reaction (Cooper, 2000). Most enzymes function in a narrow range of pH between 5 through 9 (Won-Park, Zipp, 2000). The temperature for which enzymes can function is limited as well ranging from 0 degrees Celsius (melting point) to 100 degrees Celsius (boiling point)(Won-Park, Zipp, 2000). When the temperature varies in range it can affect the enzyme either by affecting the constant of the reaction rate or by thermal denturization of the particular enzyme (Won-Park, Zipp, 2000). In this lab in particular the enzyme, which was of concern, was pancreatic amylase. This type of amylase comes from and is secreted from the pancreas to digest starch to break it down into a more simple form called maltose. Maltose is a disaccharide composed of two monosaccharides of glucose. The presence of glucose in our experiment can be identified by Benedicts solution, which shows that the reducing of sugars has taken place. If positive the solution will turn into a murky reddish color, where if it is negative it will stay clear in our reaction. We can also test if no reduction of sugars takes place by an iodine test. If starch is present the test will show a dark black color (Ophardt, 2003).

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