Amylase Activity on Starch
The Effect and Rate of the Enzyme Amylase on Starch
Abstract
Assessing reaction speed of the enzyme amylase can be measured by the amount of glucose and maltose produced during given time intervals. I hypothesized that, if the reaction time is longer, then the amount of amylase will be larger. Enzymes are specific in their match of substrates they will breakdown – similar to a key and its lock. Since amylase is the only enzyme that breaks down starch, the procedure was effective and gave clear results of sugar produced. With help from the stain reagent benzoic acid – I visibly saw the production of sugar molecules. However, I was only able to determine which of the Tubes experimented had the most or least sugar present, by color intensity. By operating a spectrophotometer, I was able to create a standard curve, which gave the absorbance values of glucose/maltose concentrations in the Tubes tested. From that, using the standard curve results and calculations (7.8 x 10^16) I then determined the µmoles of sugar present in each Tube. Finding that, in at least 2 minutes, enzyme amylase will have broken down enough starch to obtain 0.26 µmoles of sugar.
Introduction
Enzymes are proteins that act as catalysts. Enzymes break down big molecules like starch into small molecules like glucose, so that they diffuse through cell walls in our body into the blood stream. It has to be the correct enzyme - amylase is the only enzyme that will break down starch. Starch is a polymer composed of a series of glucose monomers. Amylase hydrolyzes starch into glucose and disaccharide maltose (Lab pg62). The lock and key theory is a possible explanation of why, only one type of enzyme can breakdown starch. The analogy is that, the enzyme is the lock and the key is the substrate, only the correct key (substrate) fits into the keyhole (active site) of the lock (enzyme). Utilizing a stain reagent (benzoic acid) that does not react with starch and deactivates the enzyme amylase, will
Abstract
Assessing reaction speed of the enzyme amylase can be measured by the amount of glucose and maltose produced during given time intervals. I hypothesized that, if the reaction time is longer, then the amount of amylase will be larger. Enzymes are specific in their match of substrates they will breakdown – similar to a key and its lock. Since amylase is the only enzyme that breaks down starch, the procedure was effective and gave clear results of sugar produced. With help from the stain reagent benzoic acid – I visibly saw the production of sugar molecules. However, I was only able to determine which of the Tubes experimented had the most or least sugar present, by color intensity. By operating a spectrophotometer, I was able to create a standard curve, which gave the absorbance values of glucose/maltose concentrations in the Tubes tested. From that, using the standard curve results and calculations (7.8 x 10^16) I then determined the µmoles of sugar present in each Tube. Finding that, in at least 2 minutes, enzyme amylase will have broken down enough starch to obtain 0.26 µmoles of sugar.
Introduction
Enzymes are proteins that act as catalysts. Enzymes break down big molecules like starch into small molecules like glucose, so that they diffuse through cell walls in our body into the blood stream. It has to be the correct enzyme - amylase is the only enzyme that will break down starch. Starch is a polymer composed of a series of glucose monomers. Amylase hydrolyzes starch into glucose and disaccharide maltose (Lab pg62). The lock and key theory is a possible explanation of why, only one type of enzyme can breakdown starch. The analogy is that, the enzyme is the lock and the key is the substrate, only the correct key (substrate) fits into the keyhole (active site) of the lock (enzyme). Utilizing a stain reagent (benzoic acid) that does not react with starch and deactivates the enzyme amylase, will