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Effects of Copper Sulphate on the rate of reaction between Trypsin and Milk Protein

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Introduction

EFFECTS OF COPPER SULPHATE ON RATE OF REACTION BETWEEN TRYPSIN AND MILK PROTEIN AIM In this investigation I will aim to discover the effect different concentrations of copper sulphate will have on the rate of reaction between trypsin and milk. PREDICTION I predict that the lower the concentration of copper sulphate that reacts with the trypsin and milk, the faster the reaction rate will be. I predict this because copper sulphate is a toxin and the general effects of toxins on enzymes, is that toxins reduce the strength of the enzyme as toxins (i.e. heavy metals such as copper sulphate) denature enzymes and therefore the enzyme cannot digest the product as fast, and the rate of reaction will inevitably drop. PLAN APPARATUS * Trypsin * Milk (from powder) * Copper Sulphate at 7 concentrations (1M, 0.1M, 0.01M, 0.001M, 0.0001M, 0.00001M and 0.000001M) * Distilled Water * Marker pen and white paper * Test tube rack * Test tubes (x7) * Stopwatch * Syringe I will not perform a preliminary experiment as this particular investigation is extremely time consuming and I do not have enough time to be able to complete a preliminary experiment and a main experiment. The experiment will be set up so that there are three people working in our group and we will each be testing one concentration of copper sulphate to maximise productivity in order to obtain the largest number of results we can. ...read more.

Middle

The trypsin digests the milk protein casein causing the milk to become translucent, hence, allowing us to be able to spot the black cross behind the test time as time goes on, as more milk protein will have been digested by the trypsin. The distilled water results were the control results and this conclusively proves to us that copper sulphate solution does decrease the rate of reaction between trypsin and milk protein. This is because the rate of reaction with only distilled water being added to the solution of trypsin and milk is 1.1 x 10^-2 min^-1, whereas as soon as a weak concentration of copper sulphate is introduced that reaction rate decreases to 9.6 x 10^-3 min^-1, and this reaction rate carries on decreasing as the copper sulphate concentration increases, coherently proving that copper sulphate solution decreases the rate of reaction between milk protein and trypsin. The rate of reaction is decreasing as the concentration copper sulphate solution is increasing, but at a decreasing rate. That is for a given and constant change in the concentration of copper sulphate, the difference between the rates of reactions increase at an accelerating rate. This is easily spotted on the graph as the curve greatly increases in steepness as the concentration of copper sulphate solution increases by a constant value which saw no such acceleration in difference between results at the lower concentrations. ...read more.

Conclusion

2) I would mark a black cross on a plain piece of paper and hold it behind a test tube with 3cm cubed of milk in it. 3) I would heat the trypsin in a boiling tube and when it is at the correct temperature (I would test the effects at every 5 degrees Celsius, i.e. I would test the trypsin with the milk at 20 degrees, 25 degrees etc...) I would add the trypsin to the milk and start the stopwatch. 4) I would then wait until the milk had become translucent so that the black cross behind the test tube was visible and I would then stop the stopwatch 5) I would perform three repeats for every given temperature. Then record my results and analyse them in order to draw a conclusion. I feel that if this experiment were to take place then the conclusion drawn would be that as the temperature of trypsin was round the 20 degrees mark the reaction rate would be quite low and as the temperature of trypsin increases the reaction rate would increase. I would expect the reaction rate to hit a peak at around 30 - 40 degrees Celsius and then start to decrease and eventually the effects of trypsin would be non existent after the trypsin has reached 50 degrees Celsius as after this temperature, enzymes are denatured and no longer function as they would normally. ?? ?? ?? ?? SUNIL SUTARIA 11DL ...read more.

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