Environmental Factors Influencing Amylase Enzyme Activity

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

However if the temperature exceeds the optimum temperature the enzyme becomes denatured. This is because there is too much energy causing the enzyme molecules to vibrate causing the bonds maintaining their tertiary structure to break. The enzyme unravels causing the shape of the active site to change so it can no longer fit with the substrate.

Mostly made of protein, enzymes help catalyze chemical reactions quicker by lowering the cell’s activation energy to complete a reaction, all while keeping its shape. A molecule or substrate will bind with an enzyme on its active site and reactants

The purpose of this experiment was to come up with the optimal temperature of the Fungal Amylase, Aspergillus oryzae, and the Bacterial Amylase, Bacillus liceniformis, as well as to identify if different temperatures would indeed affect the enzyme amylase by either slowing down the process or denaturing the enzyme. Enzymes are complex proteins, they can be thought of as a substance fabricated by a living organism that behaves as a stimulus, otherwise known as a catalyst, to cause a specific biochemical reaction. This experiment was performed by keeping the amylase mixed with starch at different temperatures, either in the heated water or in the ice bath. The temperatures varied at either 0, 25, 55, or 85 degrees Celsius. After a certain amount of time we would then move the test tubes containing the amylases and position them on a plate where iodine was then added to the starch amylase solution. We would do the same thing at different time intervals to see exactly how the enzyme catalyzed the starch. The hypothesis of this experiment was thought to be that the higher the temperature the slower the enzyme would then hydrolyze the starch. Both the Fungal and the Bacterial Amylase had an optimal temperature of 55 degrees Celsius as shown by our concluded results in this

Enzymes function best when they are set at a specific temperature.

Enzymes are globular proteins meaning that they are tertiary proteins, Globular proteins are made up of amino acid subunits that are merged together by hydrogen bonds, ionic bonds and disulphide bridges. They act like catalysts, they are known as biological catalysts. Catalysts are substances that increase the rate of chemical reactions. Enzymes are also proteins that have the structure of complex shapes, they allow smaller molecules to fit into them. This place where the substrate molecules are able to fit into the enzyme is known as the active site.

This laboratory experiment was carried out to establish the optimal temperature for bacterial and fungal. Besides, it will evaluate the effect of temperature on the ability of amylase to break down starch maltose. Collect 4 test tubes for each of the amylases. The test tubes were then labeled with their matching temperatures. 5ml of the 1.5% starch was added into half of each of the test tubes. Thereafter, each of the test tubes is placed into the corresponding temperatures. An Iodine test was carried out to observe the starch hydrolysis process. The two spot plates were established for fungal

In this lab, we became familiar with the importance of thermoregulation and the effects of temperature on enzyme functions. In this exercise, we prepared five solutions. Four of the five solutions were mixed with amylase (saliva), HCl, starch, and iodine and potassium iodine. The solutions were placed in different temperatures and we used a spectrophotometer to determine the each absorbance readings. A low absorbance indicates a low presence of starch and high enzymatic function. A high absorbance indicates a high presence of starch and low enzymatic function.

Procedure A (Testing Enzyme Activity)- How do different types of extreme temperatures affect enzyme activity?

Between 60ºC and 80ºC the rate of enzyme decreased slowly until no enzyme are found at 80ºC. (Decreased because the line is going down. Slowly because the slope of the line between the two points is not as steep as it was previously and the line is flattening slowly). 4. This graph 3.1 shown most the enzyme reaction optimum temperature at 40ºC. But at higher temperature enzymes are denatured.

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.

Hypothesis: If we decrease the level of pH in the enzyme Amylase, it will not be able to denature the carbohydrates in the potato starch solution after 10 drops because enzymes are very sensitive to pH levels and lowering it too much will compromise its ability to break them down.

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.

Amylase is an enzyme that is in human’s saliva as well as the pancreas. Enzymes are biological catalysts that speed up a chemical reaction. They break down complex molecules into simple ones. In this case, amylase converts starches (complex molecule) into simple sugars. That is why foods like potatoes for example, may taste sweet to us, because they contain starch. The optimum pH for pancreatic amylase is the pH of 7. In the experiment I have used buffer solutions with the pHs of 2.8, 4 and 6.5. I have also used iodine and starch. Normally, iodine is orange-yellow, however when you add starch to it, the solution will turn blue-black.