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To investigate the amount of O2 released at different of concentration of enzyme catalyse in (Yeast).

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Introduction

To investigate the amount of O2 released at different of concentration of enzyme catalyse in (Yeast) Scientific background: Introduction: Many chemical reactions take place inside a cell. The speeds at which the cell reactions take place are controlled by catalyst called enzymes, or we can say enzymes are biological catalyst. Enzyme speed up the rate of reaction without it self being used. Some enzymes, such as pepsin and trypsin, which bring about the digestion of meat, control many different reactions, whereas others such as urease are extremely specific and may accelerate only one reaction. Enzymes are large proteins that speed up chemical reaction. In their round structure, one or more polypeptide chains twist and fold, bringing together a small number of amino acids to form the active site, enzyme active site is the method of key and lock this means the active site is lock if the shape of substrate do not match exactly. This ensures that the enzyme is not specific for that chemical reaction. There are thousand of enzymes in living organisms, and they are specific, this means that each enzyme catalyses a certain chemical reaction. An enzyme has an active site, which has a unique shape into which only a substrate of same unique shape can be fit. ...read more.

Middle

Method: There are many ways in which the amount of Oxygen released could be affected. I have chosen the concentration of enzyme. 10 ml of 4 % yeast has been taken and accepted it as 100 percent to calculate the different concentration. First the dilute yeast has been made. Five different concentration of yeast that are 100%, 80%, 60%, 40% and 20% are made as I have shown on the table of yeast concentration. To collect out data I measured the amount of O2 produced from the reaction, by letting it pass through a tube and let it displace the water in the measuring cylinder. The experiment carried out three times for each concentration with 3ml of yeast and hydrogen peroxide. The step bellow followed for recording the O2 released during the reaction. a. The 3 ml of hydrogen peroxide taken in small syringe. b. 3 ml of yeast has taken in a small syringe. c. Pure the yeast in test tube. d. Add 3 ml of hydrogen peroxide. e. The test tube closed immediately and the stopwatch started. f. The time keeps constant for 1 minute. g. The amount of O2 released from the reaction measured by the 100 ml Glass cylinder. ...read more.

Conclusion

Again when I see the graph it is not straight line. I have drawn the graph for the average of 3 experiments that I did for each concentration. There are a few different results that can be determined when I add straight line. I can say there are two anomalous average results, which are far from the straight line drawn. And I think it is not possible to take precise readings from the graph between the plotted points since insufficient readings. To do a more accurate experiment in the future. Several precautions or alteration can be made. For example for experiment of enzyme with hydrogen peroxide. I can use another enzyme like potato discs. And I can use more potato disc to provide more enzymes for decomposing H2O2.The average readings could be improved by repeating to reduce the average of anomalous results. The increase in rate of reaction is the reason of existing more catalyse enzyme that provide the more active site for decomposition of hydrogen peroxide. In this experiment 5 enzyme concentrations were considered. The formula for this chemical reaction is as follows. 2H2O2 H2O+ O2 My result supports the scientific knowledge that I have written about the enzyme and hydrogen peroxide. As concentration increase if provide more active site and the theory of key a lock apply here, because it is the same enzyme to work for decomposition of hydrogen peroxide to water and oxygen gas. 1 ...read more.

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