They allow molecules to use less energy to create the reaction. However, when the temperature reaches a certain value, the structure of the enzyme vibrates so energetically that some of the bonds holding the enzyme molecule in its precise shape begin to break. This experiment can be improved by increasing the amount of rennin; this will speed up the experiment. An explanation of the independent and dependent variables involved. For example: The rate of reaction for rennin will be fastest at pH 2, at 37°C and at high substrate concentration. Introduction An enzyme is a biological catalyst. Pertaining to alternative sources of rennin, this includes the production of rennin from vegetables which are suitable for vegetarians as well as molds where rennin is being precipitated out.
The curve goes through the origin because at 0°C, the molecules do not have enough kinetic energy to move and collide with the other molecules causing a reaction to occur. This shows that the rennin did not have enough kinetic energy to work when the substrate was at room temperature and it had denatured when the substrate was at 60ºC. Your plan should have a clear and helpful structure to include: 1. In your results you can use a combination of past and present tense. I'm just completing my bio assignmnet which is prac write up.
The primary structure is the sequence of amino acids that make up a polypeptide chain. At 40ºC, 55ºC and 55ºC, the first readings obtained were quite dissimilar to the replicates. The most widely used fermentation-produced chymosin is produced either using the fungus or using. A polypeptide or protein molecule may contain several hundred amino acids. Alternative Title: chymosin Rennin, also called chymosin, protein-digesting that curdles by transforming caseinogen into insoluble casein; it is found only in the fourth stomach of cud-chewing animals, such as cows.
The rate of reaction will be measured by the amount of hydrogen gas H2 released. Chymosin secretion is maximal during the first few days after birth, and declines thereafter, replaced in effect by secretion of as the major gastric protease. I would also vary the types of milk used in this experiment. They are biological catalysts that speed up chemical reactions in the body. Therefore, the enzyme and substrate molecules will meet more often and the rate at which the product is formed will increase. Take 2mls from the beaker with a 1:1 dilution and place it in a test tube labelled 2. Repeat steps 3 to 5 for test-tube B, C, D and E, placing each in the 5, 25, 35 and 45 degree celsius water baths respectively.
The milk in the anomaly at 50ºC may have been slightly under the actual temperature so the enzyme would be less denatured as it was closer to the optimum temperature. Milk Milk is an almost complete food. As the temperature ascends to beyond the optimum temperature required, there are an increased amount of permanent bonds made. Consequently, there were fewer points on the graph which give less accurate overall curves. Place test-tube A, containing only rennin solution, into the 0 degree celsius water bath for 10 minutes before adding 2cm3 of milk into Test-tube A using a clean graduated pipette. Chymosin is also similar to pepsin in being most active in acidic environments, which makes sense considering its mission. As the temperature increases, the enzyme and substrate molecules gain more kinetic energy, so they move around at a greater speed.
§ 1ml of rennin should be added to the test tube and the stopwatch should be started. To provide extensional evidence for this experiment, different levels of pH should be used, such as the optimum pH that is about 2. Method This is everything you did, in the order that you did it in. They should be clearly set out. Watch baths should also be maintained in a constant temperature to avoid inaccuracy.
After 70 degrees the enzymes must have denatured meaning the shape of the active sites must have changed permanently. Rennin secretion is maximal during the first few days after the animal's birth but it declines thereafter replaced by the secretion of pepsin as the major gastric protease. For an enzyme to catalyse a reaction the small substrate molecules must temporarily bind to the active sites of the enzymes were the bonds in the substrate are broken and the products released. When the enzyme—substrate solution is subjected to a high level of alkalinity or acidity this causes the enzyme in the solution to denature, hence increasing the rate of reaction. Introduction:Enzymes are made up of proteins which are produced within living cells and act as catalysts which speed up chemical reactions. As a result of this the rate of reaction decreases. When this substrate fits into the active site, it forms an enzyme-substrate complex.
Aim Your aim is what you are trying to find out by conducting an experiment. Â· Repeat the above steps using bungs 2 and 3, still with the 5% Rennin solution. In animals that lack rennin, milk is coagulated by the action of as is the case in humans. Then both of the test tubes with the rennin and milk will be heated with a Bunsen burner to the desired temperature. Stir the solution to mix well. Â· Label 3 stopwatches with a china graph pencil: 1, 2 and 3.
Drop 3 drops of rennin to one test tube. Hypothesis: I believe the rate of reaction will speed up as the temperature increases until it reaches about 37oC, which is the body temperature, where it will begin to slow down and stop reacting. These include baking, cheese making and treating leather. However, the molecules vibrate so energetically that certain bond that make up the secondary and tertiary structure begin to break and so the shape of the enzyme is no longer exact. Evaluation The results seem fairly reliable; conversely the replicates obtained were not always similar to the initial values acquired.