Enzyme Practical
Introduction
Enzymes are a protein serving as a catalyst, a chemical agent that changes the rate of the reaction without being consumed by the reaction. Enzymes are proteins made up of long chains of amino acids. These form complex shapes. The enzymes are all individually working; they have different specific structures and jobs. One maybe very large and the other small, the specific shape of the active site on an enzyme are unique and prepare it to mix with a certain substrate. Without enzymes, the process of metabolism would be too slow. The reactant an enzyme acts on is referred to as the enzymes substrate. The enzyme will combine with or to its substrate. While the two are joined, the substrate is converted to its product by catalytic action on the enzyme (Steane, 2006).
A very widespread enzyme, which is necessary for the proper function of the human body, is amylase. It is mainly involved in the process of digestion since it catalyses the hydrolysis of amyloses (e.g. starch) to produce maltose and glucose. It is usually found in two forms: α-amylase and β-amylase. They both have a similar function but they work in a different way. In the human body, α-amylase is found in saliva and pancreatic juices with an optimum pH around 7. Industrially it is manufactured from bacteria such as Bacillus (Travens, 2007)
Enzymes are made mostly of proteins, but they also have some non-protein components. These non-protein components must be included in order for the enzyme to act as a catalyst (Wiley, 2008) and then the non-protein component is called a cofactor. Cofactors can include potassium, magnesium, or zinc ions however not relevant to the experiment but just more depth to enzymes.
Enzymes are affected by different factors: temperature, Ph. Each of the factors has different variant factors. Temperature, fluctuation between higher and lower temperatures will affect the rate of reaction. Whereas Ph. level will affect with its variant acidity or alkaline which will lower or raise the reaction process.
The factor that is being experimenting is through temperature changes around the enzymes, the reaction rate between the motions of the molecules increases. However when the temperature raises too high the enzymes becomes denatured. Therefore the experiment must be carefully controlled.
The reaction occurs between an enzyme and its substrate more frequently due to heat (this is thoroughly tested by using starch) of which when reacting with the amylase changes the starch polymer into a monomer (Cheung, 2004). This is a substrate also a polysaccharide of glucose molecules. Leading on from the heat hypothesis when an enzyme is denatured it no longer can bind to catalyse the reaction and become non-functional.
Method and materials
The method and materials are not inputted to this report as these were in the hand-out at the beginning of the lesson.
Results
Results are attached in Annex A
The graph also shows that around 80 degree Celsius the motion between the inner molecules become too frequent and break down the enzyme this results in the enzyme being denatured. . As the amount of time increases from 60-130 seconds the reaction is seen to increase and occurs at a faster rate. The enzyme began to decrease when temperature increased too much.)
Discussion
The results support my original hypothesis of how the temperature affects the amylase reaction rate.
Within each test tube experiment there are possibilities’ of mistakes. Temperatures being shown can be wrong or differ from reality, Temperatures were not monitored when bringing up to 5 minutes of prep time. Temperature can change by 0.1 of a degree
