Investigating the Best Temperatures betweem Calf Trypsin and Fugal Trypsin

Investigating the Best Temperatures betweem Calf Trypsin and Fugal Trypsin
problem being investigated background Trypsin is an enzyme so to be able to conduct a suitable plan, this idea will help me to predict the best temperature that can be achieved on its activities in different conditions. ?Collins Advanced Science Biology defines an enzyme as biological catalysts, speeding up reactions that would otherwise happen too slowly to be any use to the organism, that is it has catalytic properties, in other words they alter the rate of reaction without themselves undergoing a permanent change. Most chemical reactions require an initial input of energy called activation energy, to enable them to occur. Enzymes reduce the need for activation energy and so allow reactions to take place more readily than would otherwise be. An active enzyme may speed up a particular reaction, but living organisms do not need all reactions to be going at the maximum rate all of the time. It would be perfect to say after considering this fact that, enzymes do actually control rather than speeding up, because they interact with other molecules to produce an ordered, stable reaction system in which the products of any reaction are made when they are needed in the amount needed.
Enzymes are globular proteins. They have complex tertiary structure in which polypeptides are folded around each other to form a roughly globular shape. This ship is very important once altered, the enzyme cannot bind to its substrate and so cannot function, this shape is maintained by hydrogen bonds and ionic forces and their function can be affected by changes in temperature and pH, these are not the only factors that can affect enzymes are competitive inhibitors they compete with the substrate for the active site, The greater the concentration of the substrate the more likely it is to occupy the active sites and the less the effect of the inhibitor. and non-competitive inhibitors which attach themselves to the enzyme other than the active site, As the substrate and inhibitor are not competing for the same site, an increase in substrate concentration does not diminish the effect of the inhibitor temperature As temperature increases, the molecules move faster, due to increased energy. Therefore, the enzyme and substrate molecules will meet more often and the rate at which the product is formed will increase this is according to the Kinetic Theory. However, as the temperature continues to raise the hydrogen and ionic bonds, which hold the enzyme in shape, break and the active site will no longer accommodate the substrate. The enzyme will denature and when this occurs it cannot be reversed. PH Changes in pH may not only affect the shape of an enzyme but it may also change the shape or charge properties of the substrate so that either the substrate connot bind to the active site or it cannot undergo catalysis. In general enzymes have a pH optimum. However the optimum is not the same for each enzyme. the induced fit hypothesis This is a simply hypothesis explaining the way that an enzyme breaks up its substrate. It is recently known that the active site in many enzymes is not exactly the same shape as the substrate, but moulds itself around the substrate as the enzyme-substrate complex is formed. The hypothesis explains my comment that enzyme binds to a substrate momentarily, allowing a reaction to happen, but do not themselves undergo any chemical change. The image below explains the induced fit hypothesis better. [image] simple procedure and scientific communication Trypsin is an enzyme secreted by the pancreas, it digest proteins breaking them down into shorter chain of amino acids. I am going to find the optimum temperatures between normal trypsin which is found in the pancreas of most warm blooded animals and a genetically engineered trypsin. I will do so by mixing and heating these different types of trypsin and it?s substrate a suspension of powdered milk in various water baths at various temperatures. This will help me determine the various optimum temperatures of these different trypsins. I will repeat the procedure several times at the different water bath and then conclude my experiment. I also know that enzymes work best at an optimum temperature. For warm blooded enzymes such as trypsin it is close to the normal body temperature (37?C). Below this temperature, the molecule of enzyme and substrate have less kinetic energy and are moving less slowly and the chances of colliding is high. At high temperatures (50?C) enzymes are destroyed or denatured by heat. I will therefore carry out the my experiment at range of temperatures from room temperature (20?C) to a temperature that should cause denaturing(80?C) precautions and key factors needed TO obtain valid data I am going to use same concentration of trypsin in all my experiment, If I increase the concentration it will mean that the chance of the trypsin colliding with the substrate would be higher which would affect the rate of reaction and my results as well, I would also use the same concentration of my substrate throughout the experiment for the same reason. The volume of trypsin and the milk suspension should also be constant. If either varies this would upset the final concentration of the enzyme and substrate which would make it difficult to determine the optimum temperatures The end point of the optimum temperatures is difficult to judge with accuracy, so I will attempt to measure the volume of trypsin solution using a graduated pipette, which I believe is accurate to 0.1cm3 which is a 2% margin of error. I will repeat the experiment 3 times at each temperature to check whether my findings are reliable equipments
Test tube rack
Test tubes.
Milk solution
Trypsin 1(cow) and trypsin 2(fungal)
Water bath
Pipette
Thermometer
safety Some people are allergic to enzymes so I will mop up any spillages and will wash my hands after. I will take care when using the water bath. I will also ware safety goggles and lab coat throughout. method 1. Collect all equipment, and set out the water bath at temperatures ranging from 20?C, 40?C, 60?C, and 80?C.Test with the thermometer to check if the temperatures are set to the required ranges. 2. Measure 5ml of milk solution with graduated pipette into 8 different test tubes. Add 4 drops of each type of trypsin ( 4 drops of calf trypsin and 4 drops of fungal trypsin) and mix with test tube containing 5ml of milk solution. 3. Shack well and place each type of trypsin mixed with milk into the various water bath with different temperature ranges.( So in each water bath 1 calf trypsin and 1 fungal trypsin would be placed in) 4. Check every 5mins to check, and record the temperatures each time you check. When the temperatures start to drop down remove the test tubs. 5. Repeat at least 3 times and record you final results, compare the temperatures ranges for each trypsin and milk solution in various water baths . 6. plot a graph of temperature against time and comment on your graph. predicted graph OF results when the temperature start going down because it has denatured the graph will look like this Effect of temperature

Investigating the Best Temperatures betweem Calf Trypsin and Fugal Trypsin 7.5 of 10 on the basis of 1236 Review.