• Join over 1.2 million students every month
  • Accelerate your learning by 29%
  • Unlimited access from just £6.99 per month

Biology Foundation - Effect of Temperature on the Action of an Enzyme As a method of investigating the effect of temperature on enzyme action, what are the shortcomings of this experiment?

Extracts from this document...

Introduction

Biology Foundation - Effect of Temperature on the Action of an Enzyme As a method of investigating the effect of temperature on enzyme action, what are the shortcomings of this experiment? What could be done to improve it? Suggest further experiments you might carry out to examine the effect of temperature on the inactivation of the enzyme. Enzymes have a specific three-dimensional shape. They are large molecules, usually much bigger than their substrates, but only a relatively small part of the enzyme actually comes into contact with the substrate. This area of the enzyme is called its active site. Each enzyme can catalyse only one particular reaction, because an enzyme can only react with a specific substrate molecule. In this case, Amylase can only catalyse the hydrolysis of starch into smaller disaccharide maltose molecules. This is because amylase can only react with starch molecules specifically in the way cellulase 'breaks down' cellulose specifically. ...read more.

Middle

The rate of enzyme-catalysed reactions reaches a peak at a particular temperature. This is the optimum temperature for the reaction. Any increase in temperature also causes the atoms making up the enzyme molecule to vibrate more. Eventually this vibrating causes the breaking of the hydrogen bonds and other bonds that hold the enzyme molecule in its tertiary structure, with its specific shape. Its three-dimensional shape alters, including the active site, which will no longer fit the substrate molecule. The enzyme is Denatured. This is a permanent change that cannot be reversed by cooling. Addressing the issue of the shortcomings of this experiment, it could be said that at what point is denaturing irreversible? Just prior to this point, is it reversible? In order to investigate this further it could be said that the experimental reactants should be maintained at the given temperature throughout the experiment to ensure any potentially reversible denaturation is maintained throughout the course of the experiment. ...read more.

Conclusion

This is due to changes in the enzyme Active Site and as temperature is increased, this will eventually lead to denaturing. This can be explained by taking the example of the reaction leading up to 85o C. The rate of reaction slows down due to the Carbon, Hydrogen, Oxygen and Nitrogen atoms vibrating furiously due to increased heat equals increased kinetic (movement) energy which leads to the Active Site not maintaining its integrity and consistency and after time not holding its shape. While it can still catalyse, the reaction is not efficient. When the temperature increases to 85o C the active site has been destroyed hence the reaction ceases i.e. the albumen in eggs is runny when the egg is cold however after being boiled the albumen become hard and white. This is a classic example of denaturing. Stan Howell - Biology Foundation - Amylase Practical 1 ...read more.

The above preview is unformatted text

This student written piece of work is one of many that can be found in our GCSE Patterns of Behaviour section.

Found what you're looking for?

  • Start learning 29% faster today
  • 150,000+ documents available
  • Just £6.99 a month

Not the one? Search for your essay title...
  • Join over 1.2 million students every month
  • Accelerate your learning by 29%
  • Unlimited access from just £6.99 per month

See related essaysSee related essays

Related GCSE Patterns of Behaviour essays

  1. THE EFFECT OF BILE SALT ON THE ACTION OF THE ENZYME LIPASE

    Furthermore, once you decrease the concentration of bile salt the less powerful the activity of the lipase. This is a result of a diluted solution of bile restricting the degree of emulsification on the lipids therefore, lipids surface area does not increase dramatically leading to a slower reaction as the

  2. The effect of aspirin on the action of bovine liver catalase

    Analysis The results and graph produced from this investigation show that aspirin reduces the rate of the bovine liver catalase-aided breakdown of hydrogen peroxide into oxygen and water. Increasing the concentration of aspirin results in greater inhibition of the reaction.

  1. Investigation On The Enzyme Trypsin

    For this reason I expect my graph to look something like this: Method In order to perform my investigation, I used the following apparatus: � Trypsin (pH 7, 3% concentration) � Photographic Film (gelatine source) � Water Bath set at 50�C � Thermometer � Test Tubes � Wooden Splints � Syringe � Stopwatch (accurate to 1 second)

  2. Coursework: Effect of Temperature on the Rate of Reaction between

    into the reacting solution so it took more time for the full production to take place as more particles needed to collide and react.. 3rd attempt This graph shows the 3rd attempt of the experiment. It shows that as the temperature increases, the rate of reaction (time)

  1. To investigate the effect of varying the masses of white sugar and yeast and ...

    you open the bottle you see 'streams' of gas running from the sides. In bread dough the nitrogen gas bubbles trapped in the dough during mixing provide the nucleating sites; The oxygen from the air has been used up by the yeast in respiration.

  2. To investigate the effect of temperature on the breakdown of starch by amylase, and ...

    black/brown 3 black/brown brown 3.30 brown brown Temperature 37� C time in minutes colour 1st experiment colour 2nd experiment 0 black black 0.30 black/brown black/brown 1 brown brown Because this reaction was so quick I took results at more regular intervals of 10 seconds.

  1. Rates of Reaction- Hydrolysis of Urea by Urease

    According to research urease can still function at a minimal temperature of 20�C and between 10�C and 30�C the rate of reaction doubles. However the theories which will be evaluated is theory A, B and C. Theory A is based on a previous experiment which demonstrated that the optimum temperature

  2. Investigating the effect temperature has on

    * Conical flask 100cm3 (x1) containing the reaction. * Stopwatch (x1) Timing the time it takes for the cross to disappear. * Piece of card with a black cross drawn on it * 25 cm3 measuring cylinder (x2) to measure the thiosulphate and distilled water. * Goggles Important for safety when handling chemicals such as hydrochloric acid.

  • Over 160,000 pieces
    of student written work
  • Annotated by
    experienced teachers
  • Ideas and feedback to
    improve your own work