Investigating the Effect of Lipase Concentration on the Breakdown of Fat in Milk
Investigating the Effect of Lipase Concentration on the Breakdown of Fat in Milk
INTRODUCTION:
Enzymes are proteins which can catalyse chemical reactions without changing themselves. The enzyme lipase breaks down the fat in dairy products such as full-cream milk for people who are lactose intolerant. Lipase acts on its specific substrate, lipids produces fatty acids. If enzyme concentration increases, random collisions between the substrates and active sites of enzyme increase due to the increasing amount of active sites which allow more collisions to happen, so the rate of breakdown of lipids to simpler substances will increase. During the experiment, sodium carbonate solution and pH indicator phenolphthalein will be added ahead of lipase enzyme; when the pH is below 8.2, phenolphthalein will turn from pink to colourless. Sodium carbonate solution is added in order to turn the solution alkaline and the indicator pink then back to colourless after lipase is added to catalyse the chemical reaction and speed up the breakdown of lipids into fatty acid in the milk. Fatty acid produced then is going to neutralise the solution with sodium carbonate solution added previously; phenolphthalein will finally turn from pink back to colourless.
AIM:
In this experiment I will investigate the effect of increasing enzyme concentration on the activity of the enzyme lipase that will be allowed to act on the same amount of milk and the time taken for the phenolphthalein to turn from pink to white compared.
HYPOPTHESIS:
With higher lipase concentrations, there will be more active sites in the solution to be fit in by the substrates, which means more collisions between the active sites and the substrates and quicker breakdown of lipids in the milk within shorter period of time. At enzyme concentration of 1% or 2%, reactions can happen at a relatively slower pace, with lipids broken down and phenolphthalein turning from pink to white over a relatively longer time
INTRODUCTION:
Enzymes are proteins which can catalyse chemical reactions without changing themselves. The enzyme lipase breaks down the fat in dairy products such as full-cream milk for people who are lactose intolerant. Lipase acts on its specific substrate, lipids produces fatty acids. If enzyme concentration increases, random collisions between the substrates and active sites of enzyme increase due to the increasing amount of active sites which allow more collisions to happen, so the rate of breakdown of lipids to simpler substances will increase. During the experiment, sodium carbonate solution and pH indicator phenolphthalein will be added ahead of lipase enzyme; when the pH is below 8.2, phenolphthalein will turn from pink to colourless. Sodium carbonate solution is added in order to turn the solution alkaline and the indicator pink then back to colourless after lipase is added to catalyse the chemical reaction and speed up the breakdown of lipids into fatty acid in the milk. Fatty acid produced then is going to neutralise the solution with sodium carbonate solution added previously; phenolphthalein will finally turn from pink back to colourless.
AIM:
In this experiment I will investigate the effect of increasing enzyme concentration on the activity of the enzyme lipase that will be allowed to act on the same amount of milk and the time taken for the phenolphthalein to turn from pink to white compared.
HYPOPTHESIS:
With higher lipase concentrations, there will be more active sites in the solution to be fit in by the substrates, which means more collisions between the active sites and the substrates and quicker breakdown of lipids in the milk within shorter period of time. At enzyme concentration of 1% or 2%, reactions can happen at a relatively slower pace, with lipids broken down and phenolphthalein turning from pink to white over a relatively longer time