Amylase Temperature Lab Report

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

The Effect of α-Amylase Concentration on the Rate of Starch Hydrolysis in a Porcine Pancreas

Specifically, alpha-amylase is produced by the salivary glands of Homo sapiens (Humans) as well as many other mammalian species and is encoded by the gene AMY1A (Tracey 2017, p.22). The enzyme alpha-amylase is able to uptake polysaccharides including starch and glycogen as a substrate then hydrolyze the alpha-1,4-glycosidic linkages that connect the monosaccharides together (Tracey 2017, p.37). This is the reason as to why salivary amylase is also referred to as alpha-amylase (Tracey 2017, p.22).

1. Gathered all required materials to designated lab bench. 2. Considered all safety precautions including the prevention of spilling water to avoid falls, handling glassware carefully to prevent shattering, avoiding long periods of working with warm water to avoid burns and avoiding the digestion/inhalation of by-products produced after the reaction (e.g. ethanol and carbon dioxide gas). 3.

amylase enzyme and the optimal temperature for fungal and bacterial amylase. In order to make

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

To calculate the amylase activity in the germinating barley (2g), we needed to know the amount of 0.5% starch used in the reaction tube (5mg) and the time taken to reach the achromic point, to get the average amount of starch hydrolysed / min to reach achromic point for 1mL of Diluted Amylase Extract(DAE), thus, we could get average amount of starch hydrolysed / min to reach achromic point for 25mL of DAE, which was same as the average amount of starch hydrolysed / min to reach achromic point for 5mL of amylase, therefore, we got the average amount of starch hydrolysed / min to reach achromic point for the total volume of the filtrated, non-diluted amylase extract, with knowing the weight of barley grains/germinant used to make the extract, we could calculate the amylase activity as mg starch hydrolysed/min/g barley tissue.

Using a 5 mL pipet, exactly 5 mL of distilled water was added to each of ten test tubes. The level was marked with a masking tape and the water was poured out. The test tubes were marked to their assigned temperatures (45°C, 40°C, 35°C, 30°C and 27°C).

In testing the differences that pH and temperature place on the enzyme, it will be possible to deduct the changes in enzymatic activity because of their surroundings. By using starch, a molecule that is hydrolyzed by amylase, it is possible to see the disappearance of substrate and creation of product with the addition of Lugol’s iodine (Fox 64). Adding the starch to the enzyme solution in the experiment allows for comparison between differing pH levels as well as the different temperatures that one might find amylase. It will be possible to determine what temperature and pH level are most effective for the enzyme to function at by running these comparisons.

The purpose of this experimentation is to find the differences of the concentration of the enzyme amylase to determine what outcome of the changes will have on the rate of the reaction between starch and amylase. We hypothesizes that as the reaction temperature of amylase solution and starch solution rises the pH reaction rate of both solutions will rise. Materials: 6 test tubes Marker

Effect of varying Temperatures on Enzymatic Activity of Bacterial and Fungal Amylase and hydrolysis of Starch

For example, the source of two types of proteases are Bacillus alcalophilus and Bacillus lentus. The most common sources of amylases are the bacteria Bacillus subtilis, Bacillus amyloliquefaciens, and Bacillus licheniformis. On the other hand, lipases are currently being sourced from yeast, bacteria, fungus, and from mammals. Biotex is the main source of cellulases, and have been in use since 1987.

Bacillus subtilis, is a Gram-positive, catalase-positive bacterium, found in soil and the gastrointestinal tract of ruminants and humans. Due to its excellent fermentation properties, with high product yields, it is used to produce various enzymes, such as amylase and proteases (Maarten van Dijl; Hecker ,

To determine the most favorable temperature for the reaction of alpha amylase's enzymatic conversion of starch to glucose water baths of various temperatures were used. First a stock solution was prepared prior to the experiment; it included alpha-amylase, I2KI indicator and .0033 g/ml of starch. Thirty-five mL of this solution was then combined with 35mL of distilled water into an Erlenmeyer flask in order to create the reaction flask. The flask was then added into one of the various water bath temperatures, 15, 35, 45, 55, 65 and 70 C. The reaction flask needed to be in the water baths long enough for it to reach the required temperature before the enzyme was added. 0.1mL of I2KI indicator was then added to each of the twelve cuvettes which were used in the timed readings. Then 5mL of the solution from the reaction flask was transferred into one of the cuvettes which contained I2KI indicator. Next, the starch-iodine complexes' absorbance were read on the spectrophotometer and recorded onto the appropriate table. Then, 1mL of alpha amylase was added into the reaction flask to begin the reaction, once

Alpha amylase is a protein enzyme present in grains that have starch. It is also present in humans, most commonly in saliva (Murray). The main purpose for alpha amylase is to break down, or hydrolase, polysaccharides, such as starch (Murray). When alpha amylase breaks down starch and glycogen, they cause a chemical reaction that creates the sugars maltose and glucose. Alpha amylose is also