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The Effect of Enzyme Concentration On Enzyme Activity

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Introduction

THE EFFECT OF ENZYME CONCENTRATION ON ENZYME ACTIVITY AIM: To investigate the effect of a reduction in enzyme concentration on the rate of reaction, in this case the breakdown of protein by protease enzyme. The protein substrate in this reaction will be trypsin milkprotein (casein). PREDICTION: I believe thath a higher enzyme concentration results in protein trypsin to be broken down faster/ a faster rate of reaction. The protein solution would turn clear quicker when enzymes are more concentrated. The site of the reaction occurs in an area on the surface of the protein (protease) called the active site. At low enzyme concentration there is great competition for the active sites and the rate of reaction is low. As the enzyme concentration increases, there are more active sites and the reaction can proceed at a faster rate. Therefore i believe as the protease concentration is reduced, the rate of reaction, as well as the trypsin mlk protein, is also reduced. FACTORS AFFECTING THE RATE OF REACTION: Temperature - enzmes work best at an optimum temperature. Below this, an increase in temperature provides more kinetic energy to the molecules involved. ...read more.

Middle

-glassware for diluting enzyme -milk powder solution -test tube holder -waterproof pen -ruler -standard acidific trypsin solution 19% -5cm3 pipettes 50cm3 beaker -glassware for dilution of the enzyme METHOD: 5cm3 protein solution was pipetted into a test tube and mixed thoroughly. The stop clock was then immediately started and the time taken for the protein solution to clear was recorded. This was repeated two more times for accuracy. These exact procedures were repeated with different enzyme concentrations, ensuring that the conditions are unchanged. The different enzyme concentrations were used: 1% - 5cm3 enzyme solution STRONGER 0.5% - 2.5cm3 and 2.5cm3 water 0.25% - 1.25cm3 enzyme and 3.75cm3 water 0.10% - 0.5cm3 enzyme and 4.5cm3 water WEAKER RESULTS: CONCLUSION: The results i have obtained have shown that a decrease in concentration of enzymes results in an increase in the timetaken for the solution to clear. In other words, as the concentration of protease decreases, the amount of active where the reaction takes place also decrease, therefore causing a lower rate of reaction - the time taken for the trypsin milk protein to be broken down is slower. ...read more.

Conclusion

Here, a flask could be used to mix the two solutions together. When adding the two solutions together, the flask would be inverted a reasonable amount of times, approximately six. The amount of times it is inverted must stay constant throughout each experiment to avoid unfairness. Inverting must be done slowly to allow time of proper mixing between the two solutions, also so the solution can reach both ends of the flask each time inverting. Carrying this process ut can result in a much better chance of a fully mixed standard solution. Other factors in which error could have occured are inaccurate measuring - here, i can only read measurements accurately to the nearest millametre, when to start timing - here, starting the clock must be done immediately after mixing the solutions, and some solutions may have taken longer to mix, and the clock therefore being started at different times during each experiment, and temperature of the surroundings - temperature can affect the rate of reaction. If the temperature of the surroundings changes, this can cause a temperature change in the solution. As stated earlier, enzymes work best at an optimum temperature. Below this, the rate of reaction increases, and above this, the rate of reaction decreases, both causing inaccurate results. ...read more.

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4 star(s)

This is a well written and structured report.
1. The report needs to have an introduction section that covers relevant background information
2. The report does not include the data that has been collected
3. The conclusion needs to attempt to explain the patterns that have been found
4. The evaluation needs to suggest further research opportunities
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Marked by teacher Luke Smithen 17/09/2013

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