The?progress?of?enzyme-catalysed reactions?can be investigated by:
Measuring the?rate of formation of a product?using catalase
Measuring the?rate of disappearance of a substrate?using amylase
Investigating catalase activity
In this investigation, the rate of?product formation?is used to measure the rate of an enzyme-controlled reaction:
Hydrogen peroxide?is a common but?toxic?by-product of metabolism
This means it must be?broken down?quickly
Catalase?is an enzyme found in the cells of most organisms that?breaks hydrogen peroxide down into water and oxygen
Hydrogen peroxide and catalase are combined and the?volume of oxygen generated?is measured in a set time
The?rate of reaction?can then be calculated
Experimental set-up for investigating the rate of formation of a product using catalase
Investigating amylase activity
In this investigation, the rate of?substrate disappearance?is used to compare rates of reaction under different conditions:
Amylase?is a digestive enzyme that?hydrolyses starch into maltose and glucose
Amylase functions best at pH 7 and 37oC (all enzymes operate best under specific conditions)
Amylase and starch are combined?and this reaction mixture is then?tested for starch?at regular time intervals
This can be done by taking samples from the reaction mixture at each time interval and adding each sample to some?iodine in potassium iodide solution?(starch forms a?blue-black?colour with this solution)
In this way, the time taken for starch to be broken down can be measured
The investigation can be repeated under a variety of conditions?(eg. by altering pH or temperature) and the?reaction rates can then be compared
Experimental set-up for investigating the rate of disappearance of a substrate using amylase