4007353
Juan, Victoria, Lilly, Tiffany Chung
The effect of varying temperature on amylase converting starch to maltose.
Lab Group 3
Abstract
This experiment shows the effect of rising temperature on enzyme amylase activity on converting starch to maltose. The reason for conducting the experiment is to find optimal temperature for enzyme activity. The enzymes that will be comparing are fungal and bacterial amylases. The enzymes were set at 4 temperatures 0-850 Celsius and checked at 4 different times from 0-10. The results showed the enzymes activity increased until 850 Celsius. Then the enzyme shows no hydrolysis. Enzymes denature at high temperature. To sum up, enzymes have optimal temperatures at which they operate. This experiment shows
…show more content…
This experiment is focused on the optimal temperature at which these enzymes operate and how various temperatures affect enzyme activity. An enzyme is a complex protein that is produced by all living organisms with the primary function of enhancing chemical reactions through a process called catalysis. These enzymes are part of our everyday life processes that keep us alive. The enzymes are used commercially, for example to bake bread, biscuits and crackers (Alberte et al., 2012). Knowing the optimal operating temperatures helps companies be efficient in creating and providing their products that use enzymes. Not providing the optimal temperatures and other conditions can result in an unwanted product and can even lead to conflict between the producers and consumers (Montes et al., 2008). Amylase converts starch polymers into monomers such as maltose. If amylase is doing the process correctly there should be no starch left in the solution. To check if any starch in left in the solution you can add a few drops iodine. After adding the drops the solution may turn yellow meaning there is no starch left in the solution. If the solution turns brown or a dark black it would show the presence of starch. This occurs because of the structure of iodine interacting with the shape of the starch molecule (Goldina and Simms, 2010). If the enzymes temperatures are not at optimal temperatures for catalyzation of the …show more content…
The first two materials were the amylases. The bacterial amylase was derived from the bacteria Lichenitormia and the fungal amylase was derived from the fungus Oryzac. The experimental set was as follows first you would label 4 napkins at 0C, 25C, 55C, 85C. Each one would be labeled from 0-10 mins in 2 minute intervals. Then one will label 4 test tubes each with one of the four temperatures previously mentioned and B or F, which represents bacteria or fungus. Add 5ml of 1.5% starch to each test tube and label each one “S” for starch. Add 1ml of amylase from the bacteria or fungus and into 4 test tubes not contain starch. Now add the 8 test tubes to the respect temperatures (4 containing amylases and 4 containing starch). All of the test tubes must be allowed to equilibrate for 5 minutes to reach their respective temperatures. The spot plates are set up 4 x 6 (4 labeled temperatures and 6 labeled time). Now add 3 drops of iodine to the first row label 0 minutes. Then add the starch solution from the respective temperatures to the first row labeled 0 mins. Now pour the starch solution into the tube containing amylase without taking it out of the water bath and set the timer for 2 minutes. Now add 3 drops of iodine to the 2 min slots. After the 2 minutes have passed transfer the starch-amylase mixture to the 2 minutes row. After another 2 minutes passes add another 3 drops of iodine to the 4 minutes row and add the
Living organisms undergo chemical reactions with the help of unique proteins known as enzymes. Enzymes significantly assist in these processes by accelerating the rate of reaction in order to maintain life in the organism. Without enzymes, an organism would not be able to survive as long, because its chemical reactions would be too slow to prolong life. The properties and functions of enzymes during chemical reactions can help analyze the activity of the specific enzyme catalase, which can be found in bovine liver and yeast. Our hypothesis regarding enzyme activity is that the aspects of biology and environmental factors contribute to the different enzyme activities between bovine liver and yeast.
The affects of pH, temperature, and salt concentration on the enzyme lactase were all expected to have an effect on enzymatic activity, compared to an untreated 25oC control. The reactions incubated at 37oC were hypothesized to increase the enzymatic activity, because it is normal human body temperature. This hypothesis was supported by the results. The reaction incubated to 60oC was expected to decrease the enzymatic activity, because it is much higher than normal body temperature, however this hypothesis was not supported. When incubated to 0oC, the reaction rate was hypothesized to decrease, and according to the results the hypothesis was supported. Both in low and high pH, the reaction rate was hypothesized to decrease, which was also supported by the results. Lastly, the reaction rate was hypothesized to decrease in a higher salt concentration, which was also supported by the results.
One of the most primitive actions known is the consumption of lactose, (milk), from the mother after birth. Mammals have an innate predisposition towards this consumption, as it is their main source of energy. Most mammals lose the ability to digest lactose shortly after their birth. The ability to digest lactose is determined by the presence of an enzyme called lactase, which is found in the lining of the small intestine. An enzyme is a small molecule or group of molecules that act as a catalyst (catalyst being defined as a molecule that binds to the original reactant and lowers the amount of energy needed to break apart the original molecule to obtain energy) in breaking apart the lactose molecule. In mammals, the lactase enzyme is present
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
The Effect of Temperature on the Activity of the Enzyme Catalase Introduction: The catalase is added to hydrogen peroxide (H²0²), a vigorous reaction occurs and oxygen gas is evolved. This experiment investigates the effect of temperature on the rate at which the enzyme works by measuring the amount of oxygen evolved over a period of time. The experiment was carried out varying the temperature and recording the results. It was then repeated but we removed the catalase (potato) and added Lead Nitrate in its place, we again tested this experiment at two different temperatures and recorded the results. Once all the experiments were calculated, comparisons against two other groups were recorded.
Gareth Williams Background knowledge (facts): Chemicals changed by enzymes catalysed reactions are called the substrate of the enzyme they fit into the active site of the enzyme; this is where the reaction takes place, this happens with a lock and key mechanism. The product of the reaction then leaves the active site, freeing it up for more similar reactions to take place. Amylase is a carbohydrase enzyme which is in our saliva gland, this helps digest the carbohydrates that we eat e.g. pasta and bread etc. [IMAGE] Starch is a large molecule which is made up of lots of other smaller
The temperature of amylase The temperature of starch Room temperature Concentration Ph values The variable I will be changing is the volume of amylase. Safety: The sand is To make sure I carry out this experiment safely I will make sure I wear a pair of goggles. I will ensure I keep my stool under the table and all
Investigating the Effect of Enzyme Concentration on the Hydrolysis of Starch with Amylase Aim: Investigate the effect of enzyme concentration on the rate of an enzyme-controlled reaction. Using amylase and starch as my example. Introduction: I am investigating the effect of the concentration of the enzyme, amylase on the time taken for the enzyme to fully breakdown the substrate, starch to a sugar solution. The varied variable will be the concentration and all other variables are going to be fixed. The different concentrations will be: 0.5% 0.75% 1.0% 1.5% 2% An enzyme is a class of protein, which acts as a biological catalyst to speed up the rate of reaction with its substrates.
The results of this experiment showed a specific pattern. As the temperature increased, the absorbance recorded by the spectrophotometer increased indicating that the activity of peroxidase enzyme has increased.At 4C the absorbance was low indicating a low peroxidase activity or reaction rate. At 23C the absorbance increased indicating an increase in peroxidase activity. At 32C the absorbance reached its maximum indicating that peroxidase activity reached its highest value and so 32 C could be considered as the optimum temperature of peroxidase enzyme. Yet as the temperature increased up to 60C, the absorbance decreased greatly indicating that peroxidase activity has decreased. This happened because at low temperature such as 4 C the kinetic energy of both enzyme and substrate molecules was low so they moved very slowly, collided less frequently and formed less enzyme-substrate complexes and so little or no products. Yet, at 23 C, as the temperature increased, enzyme and substrate molecules
The mixture for that table’s flask was 15 mL Sucrose, 10 mL of RO water and 10 mL of Yeast, which the flask was then placed in an incubator at 37 degrees Celsius. In my hypothesis for comparison #4 the measurements would go up again with every 15 min. intervals because of the high tempeture and also be higher that then Controlled Table’s measurements. Hypothesis was right for the first part but was wrong for the second part of the comparison, the measurements did increase in the table’s personal flask but the measurements did not get higher than the Controlled Table’s measurements, see chart below. In conclusion, I feel that the substitution of glucose for sucrose made the enzymes work just as hard as the Controlled Table’s flask but just not as much because sucrose was too strong for the enzymes to
Starch is constructed of glucose subunits linked to one another through glycosidic bonds. Amylase is a group of enzymes capable of digesting these glycosidic linkages by hydrolyzing, or splitting by addition of a water molecule, the starch into smaller carbohydrate molecules like glucose and maltose. It is best known for its function in beginning the chemical process of digestion in the human body, converting complex carbohydrates into forms usable in the body. However, with recent advances in biotechnology, the range of amylase applications has significantly expanded. Detergent industries, brewing companies, food/agriculture industries, textile industries, paper industries, and pharmaceuticals, all employ amylase during production. Over 80% of the global enzyme market is utilized in industrial settings and, of that, amylase contributes approximately 25-33% to industrial application. This paper will provide an overview of the genetics, structure, function, and regulation of alpha-amylase with a special discussion on industrial applications.
Influence of Temperature on the Activity of Potato Catalase Hypothesis That the higher the temperature the higher the reaction rate of potato catalyse to a point were denaturing occurs in the enzyme and the reaction rate of the potato catalase drops off. Prediction The rate of Catalase activity will be faster at higher temperatures until a point, because at higher temperatures there are more chances of collisions between the enzyme's (Catalase) active site and the substrate (hydrogen peroxide). However the rate depends on the active site being able to join with the substrate, and at higher temperatures the enzyme can be denatured, which changes the shape of the active site which thus prevents the reaction from happening. At first, as the temperature increases the activity of the Potato catalase also increases this is because the collision rate of the enzyme with the hydrogen peroxide is increased.
Abstract: Enzymes are catalysts therefore we can state that they work to start a reaction or speed it up. The chemical transformed due to the enzyme (catalase) is known as the substrate. In this lab the chemical used was hydrogen peroxide because it can be broken down by catalase. The substrate in this lab would be hydrogen peroxide and the enzymes used will be catalase which is found in both potatoes and liver. This substrate will fill the active sites on the enzyme and the reaction will vary based on the concentration of both and the different factors in the experiment. Students placed either liver or potatoes in test tubes with the substrate and observed them at different temperatures as well as with different concentrations of the substrate. Upon reviewing observations, it can be concluded that liver contains the greater amount of catalase as its rates of reaction were greater than that of the potato.
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
There were five test solutions used in this experiment, water being the control, which were mixed with a yeast solution to cause fermentation. A 1ml pipetman was used to measure 1 ml of each of the test solutions and placed them in separated test tubes. The 1 ml pipetman was then used to take 1ml of the yeast solution, and placed 1ml of yeast into the five test tubes all containing 1 ml of the test solutions. A 1ml graduated pipette was placed separately in each of the test tubes and extracted 1ml of the solutions into it. Once the mixture was in the pipette, someone from the group placed a piece of parafilm securely on the open end of the pipette and upon completion removed the top part of the graduated pipette.