The catabolic enzyme alpha-amylase is active in some parts of the digestive system but not in others. What property of aqueous solutions controls its level of activity and how? If this property was out of the normal range in the areas of the digestive system where the enzyme is normally active, how would the catabolism of the substrate of alpha-amylase be affected?
The catabolic enzyme alpha-amylase is active in some parts of the
Alpha-amylase is a protein having enzymatic activity and enzyme commission (EC) number 3.2.1.1. Enzyme is a catalytic molecule that increases the rate of any chemical reaction without being used up in it. It can be any protein molecule or in some cases, it can be an RNA molecule. An enzyme binds with the substrate or reactant of a reaction and releases the end products.
Alpha-amylase breaks the alpha bonds present in polysaccharides like glycogen and starch. The end products of these cleavage reactions are maltose and glucose. In humans, alpha-amylase is prominently found in saliva and pancreatic juice.
The salivary amylase begins the digestion of polysaccharides in mouth and gets inactivated in the stomach due to the presence of gastric juices. When the chyme reaches the duodenum, digestion of polysaccharides again resumes by the effect of pancreatic amylase.
The major factors affecting the activity of alpha-amylase are:
pH: Alpha-amylase works best at pH 7.0. Drop in the pH of an aqueous solution subsequently reduces its activity and the enzyme gets completely inactivated at pH 3.0-3.3.
Temperature: The optimum temperature for the activity of alpha-amylase is 37°C which is the normal human body temperature. Increase or decrease in the temperature reduce, inactivate or denature the enzyme.
Certain anions: Chloride and bromide anions play a crucial in the activity of alpha-amylase. Presence of iodide, phosphate and sulfate also affect its activity but only to certain extent. Presence of these anions prevents inactivation of alpha-amylase and the enzyme can work even at reduced activity.
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