Enzyme Lab Report
Influence of Concentration on the Activity of Amylase
Title
Influence of Concentration on the Activity of Amylase
Abstract
Does more or less concentration speed up the reaction rate of amylase in starch? In this experiment diluted solutions of amylase were created and then tested using a starch solution, I2KI for reaction times. The answer to the question was proved to be that more concentration of amylase speeds up the reaction time.
Introduction
The enzyme, amylase is found in the saliva of most animals and in humans. Amylase hydrolyzes starch, a plant's reservation of carbohydrates. Amylase causes a chemical reaction in the polysaccharide starch that breaks down the glucose molecules into maltose. When diluted with a solution of I2KI, starch will change to a dark purple while doing the same to maltose, there would be no color change. The question posed, does more or less concentration speed up the reaction rate? Group 11 predicts that the more concentrated solution of amylase (1>5), the reaction rate will be faster; therefore test tube 1 will have the quickest reaction rate. The rate of disappearance of starch in amylase can be shown by diluting amylase in a 1:1 ratio but using Tube 1 to create Tube 2, Tube 2 (a mix of 1 and 2) to create Tube 3 and so on for 5 Tubes.
Materials
test tube rack
10 standard test tubes wax pencil test plate flask of distilled water beaker of distilled water
5mL graduated cylinder
1 calibrated 1mL pipette
2 calibrated 5mL pipette disposable pasteur pipettes pipette bulb buffer solution
I2KI solution
1% starch solution
1% amylase solution
Methods
The lab group prepared amylase dilution in the first set of test tubes (1-5). 5mL amylase was added to a test tube already containing 5mL distilled water creating the first tube to have .5% amylase. Next 5mL of amylase from test tube 1 was added to the 5mL of distilled water in test tube 2, giving test tube 2 a dilution of .25%. This was
Title
Influence of Concentration on the Activity of Amylase
Abstract
Does more or less concentration speed up the reaction rate of amylase in starch? In this experiment diluted solutions of amylase were created and then tested using a starch solution, I2KI for reaction times. The answer to the question was proved to be that more concentration of amylase speeds up the reaction time.
Introduction
The enzyme, amylase is found in the saliva of most animals and in humans. Amylase hydrolyzes starch, a plant's reservation of carbohydrates. Amylase causes a chemical reaction in the polysaccharide starch that breaks down the glucose molecules into maltose. When diluted with a solution of I2KI, starch will change to a dark purple while doing the same to maltose, there would be no color change. The question posed, does more or less concentration speed up the reaction rate? Group 11 predicts that the more concentrated solution of amylase (1>5), the reaction rate will be faster; therefore test tube 1 will have the quickest reaction rate. The rate of disappearance of starch in amylase can be shown by diluting amylase in a 1:1 ratio but using Tube 1 to create Tube 2, Tube 2 (a mix of 1 and 2) to create Tube 3 and so on for 5 Tubes.
Materials
test tube rack
10 standard test tubes wax pencil test plate flask of distilled water beaker of distilled water
5mL graduated cylinder
1 calibrated 1mL pipette
2 calibrated 5mL pipette disposable pasteur pipettes pipette bulb buffer solution
I2KI solution
1% starch solution
1% amylase solution
Methods
The lab group prepared amylase dilution in the first set of test tubes (1-5). 5mL amylase was added to a test tube already containing 5mL distilled water creating the first tube to have .5% amylase. Next 5mL of amylase from test tube 1 was added to the 5mL of distilled water in test tube 2, giving test tube 2 a dilution of .25%. This was
References: Reece, J.; Urry, L.; Cain, M.; Wasserman, S.; Minorsky, P.; Jackson, R. Campbell Biology, San Francisco, CA: Pearson Benjamin/Cummings, 2011. Munaim, S. Symbiosis: Investigating Biology, Schenectady, NY: Pearson Learning Solutions, 2011.