Investigating the effect of pH on amylase activity
The aim of the experiment is to determine the effects of different pH and the rate of reaction on fungal amylase and starch.
The enzyme amylase is found in the human body, it catalyses the hydrolosis of internal glycosidic bonds in polysaccharides, the breakdown of starch into sugars. Amylase is present in human saliva, where it initiates the chemical process of digestion. Enzymes work best at an optimum pH of 7 which is the bodies normal pH. The pH affects the charge of the amino acid at the active site. PH changes affect the structure of an enzyme molecule and therefore affect its ability to bind with its substrate molecules. Changes in pH affect the ionic bonds and hydrogen bonds that hold the enzyme together, which naturally affects the rate of reaction of the enzyme with the substrate. On top if this, the hydrogen ions neutralise the negative charges of the R groups in the active site so that the substrate and the active site do not attract and therefore do not react.
Amylase is an enzyme. Since enzymes are proteins, their secondary and tertiary structures are affected by temperature and pH. The enzymatic activity is closely associated with the structure of the enzyme, so any change in the secondary or tertiary structure leads to a change in enzyme activity. (3)
Amylase is a digestive enzyme found in saliva and in pancreatic secretions to the small intestine. The function of amylase is to catalyze the hydrolysis of carbohydrates, such as the polysaccharide, starch, to the disaccharide maltose. Maltose is subsequently hydrolyzed to glucose by another digestive enzyme, maltase. These glucose molecules are the starting point of glycolysis. Glycolsis is the first process organisms employ to harvest energy, (ATP), from ingested carbohydrates. In cellular respiration, glycolosis is the initial step in energy production as it converts glucose to two pyruvate molecules....
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