• 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. 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.

  2. The effects of temperature on the action of the enzymes catalyse.

    I will use the mashed up form as it will be a faster reaction as there is more area to react on, as we have to consider the time span. The same volume of hydrogen peroxide in each part of the Investigation.

  1. Factors Affecting Enzyme Activity

    The reason fro the reaction possibly taking place at all is that light decomposes hydrogen peroxide meaning that the hydrogen peroxide being exposed to the light in the laboratory may cause some gas to be collected in the gas cylinder.

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

    to bind to, this causes collisions with uninhibited active sites to be less frequent. Increasing the concentration of aspirin made the most difference between 0gdm-3 and 10gm-3 where the rate of reaction fell by 0.64mm3s-1, between these points the relationship between aspirin concentration and rate of reaction is shown on the graph as an almost straight line (see fig 3).

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

    The substrate (milk) is held in the active site by temporary bonds forming a structure, which is referred to as the enzyme-substrate complex. The energy needed to allow such a reaction to continue, is called the activation energy. Indeed, to increase the rate of reaction and the formation of new

  2. 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)

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

    This shows that the rate of reaction has decreased compared to the start/lowest temperature (explained in 1st attempt). There is only one main anomalous that stands out the most at 35 degrees. This could be due to the container or data logger not being cleaned so it added more particles

  2. Rates of Reaction- Hydrolysis of Urea by Urease

    of urease was 50�C, however Theory B opposes this finding, stating that urease activity does not stop increasing until a temperature of 71�C, thereafter, temperatures greater than 71 �C would denature the enzyme. Theory C states that the optimal pH of urease is approximately 7; therefore meaning that urease would

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