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Abstract on Impact of Temperature on Catalase Activity

An enzyme is primarily a protein that can be formed through catalyzing chemical reactions by fastening to a substrate. With this experiment, it is determined that using catalase as enzyme and hydrogen peroxide as the substrate could lead to break down. Concerning such, the experiment involves three sections within it. The first section depicts the hypothesis which indicates that, as soon as the substrate concentration has been increased, the reaction would also increase until every active site is bound to react. In the second section, it was been anticipated that as there is an increase in temperature, the rate of reaction has also increased until and unless the enzyme is denatured effectively. Now, in the third section, the hypothesis has affirmed that there is a decline in catalase activity concerning a significant change within the optimal temperature.

Besides, it has been noted that within the first section, the catalase was assorted with several substrate concentration. Subsequently, in the second part, it was been treated at diverse temperature to know its effectiveness and in the third section, hydrogen peroxide was treated with numerous pH buffers. Relating to such testing, the results supported every proving of the hypothesis that helps increase the substrate concentration with the same increment in the reaction rate of temperature. Whereas, regarding pH, increase and decrease in temperature slows down the rate of reaction remarkably. Thus, the enzymes stay inactive when the active sites are been filled, or when there is a significant increase in temperature, or when the pH has been changed from most favourable temperature. 

Introduction to Impact of Temperature on Catalase Activity

In scientific terms, enzymes are biological catalysts that help accelerate chemical reactions without being consumed any fraction of the enzyme. Also, despite the capability of metabolic pathways to help self-control, it has been noted that there is a decline in the quantity of activation energy needed to start a reaction, therefore, inclining the reaction rate (Kimbrough et al., 1997). This indicates that the experiment has permitted the utilization of enzyme catalase. The key role of catalase is breaking down H2O2 into H2O and O2. According to Rankan and Mallik, (1931), has revealed that Leow was the first person who had discovered the presence of catalase in living cells that he observed from a piece of tobacco leaf (Ranjan and Mallik, 1931). There is a prime requirement of various initial studies or research to associate the activity of enzymes with the capability of respiration. But, it was been anticipated that the purpose of catalase is to avert oxidation that is excessive, but not to support respiratory metabolism (Ranjan and Mallik, 1931).

The aim of conducting this specific research is to examine the impact of substance concentration, pH, and temperature on the activity of catalase. The null hypothesis was signified that an enzyme with a higher concentration with varying pH range and different temperatures shall have no impact on the catalase rate of reaction. Besides that, the hypothesis which was supposed to be an alternative indicates that as the substrate concentration inclined, the reaction rate will also increase until and unless every active site were bound and the activity of enzymes reaches an optimal temperature level. Thus, this will create the reaction rate at the highest. Furthermore, the pH hypothesis stated that the catalyst activity has been decreased concerning an alteration in the optimal level of pH. The catalyst speeds up the reaction as er the required quantity with the added substrate. Similarly, the enzymes operate at temperatures that are at the precise levels as they will be able to catalyze a reaction at specific temperatures, subsequently, initiate denaturing and turn out to be inactive (Aronson et al., 1956). On the other hand, supposedly if the level of pH is too low or too high, there are chances that the enzymes become denatured too and which may lead to losing its specific structure.

Methodology of Impact of Temperature on Catalase Activity

Concerning the experiment, the source of catalase was the celery. Besides that, hydrogen peroxide was been utilized as the substrate to formulate results. Relating to this, 5 grams of celery was chopped finely as it will help increase the area of the surface to occur reaction. Then, 20 ml of the universal buffer with p7 was added to a meniscus. Later, 3 drops of detergent were added to the universal buffer considerably. The prime objective of adding detergent in the solution was to use it as an indicator to signify the products that will occur by the reaction such as H2O and O2 through bubbles formation. It is important to gently mix the detergent with the universal buffer while preventing from foam formation considerably. On the other hand, the foam formation was being prevented to acquire exact and effective results because it was the only outcome of produced oxygen.

Subsequently, the celery was been chopped and added to the mixture that contains universal buffer along with detergent. The meniscus was smoothly tapped to ensure that the celery has been drowned absolutely within the solution. Besides, the volume of the baseline was recognized carefully. The extract of the catalase was mixed with 2 ml of H2O2 along with a pipette which was used to accurately measure the hydrogen peroxide. Thus, the foam formation was witnessed immediately after the mixture into the solution. However, it has been the visible foams were oxygen gas which was being produced by the process of hydrogen peroxide decomposition. On the other hand, the activity of the catalyst was monitored by volume measurement of oxygen which was generated by the reaction within the intervals of operation time of 5 minutes and 10 minutes considerably.

Now, post figuring out the basic process of using celery extract, the specific experiment was repeated various times by involving the following variations:

  • Different pH with 20% and 30%
  • The diverse concentration of hydrogen peroxide with 0%
  • Lower and higher temperature levels with 10% and 5%

Additionally, the different pH that was used was pH 4, pH 6, pH 7, pH 8, and pH 10 significantly. Every concentration was combined with the temperature of the room and the outcome has been noted accordingly. 

Within the second half part of the experiment or examination, a similar approach has been utilized; however, the substrate concentration was unchanged, while the temperature of catalase varied. It includes boiled catalase contains 70 degree Celsius, catalase in the bath with warm water contains 40 degree Celsius, catalase of room temperature comprise 19 degree Celsius, and ice catalase posses 0 degree Celsius. All these temperatures were used and each of them was pooled with the substrate and every data about the rate of reaction in ml was recorded accurately to ensure effectiveness.

Result of Impact of Temperature on Catalase Activity

The substrate concentration which comprised of 0% have not elicited any reaction, hence, there was no production of O2. Additionally, the concentration of substrate containing 5% has produced an average of 7.71 ml foam considerably. On the other hand, 10% created concentration has given an average of 15.57% ml foam. Whereas, the concentration that is contained 30% and 20% have formed 45 ml and 34.71 ml of average correspondingly. (Given in Table 1)

Besides that, the average quantity of foam which is required for the ice catalase was of 27.29 ml respectively. It has been noted that, when there is a rise in catalase temperature comparable to room temperature, it produces 27.71 ml of average. On the other hand, when the same catalase was treated in a warm water bath, it forms an average of 35.14 ml foam, and concerning the catalase which was boiled has provided an outcome of producing an average of 1.57 ml foam. (See table 2)

The pH 4 buffer has produced 6.9 ml average of foam. Whereas, pH 6 buffer has resulted in giving an average of 17.9 ml foam respectively. It has been understood that when there is an alteration of pH to pH 7, it has the result of producing 29.3 ml of average. Subsequently, the pH 8 and pH 10 buffers have produced 15.1 ml and 24.4 ml of average correspondingly. (See table 3)

Substrate concentration (H2O2)

Group 1: (No enzyme control)

Group 2

Group 3

Group 4

Group 5

Group 6

Group 7

Average

Standard Deviation

0%

0

0

0

0

0

0

0

0

0

5%

0

13

4

15

6

9

7

7.71

5.15

10%

0

27

12

23

13

11

23

15.57

9.34

20%

0

51

53

32

23

47

37

34.71

18.73

30%

0

56

73

42

31

64

49

45

24.19

(Table 1: Showing the impact of alteration in substrate concentration on the rate of reaction)

Temperature factor

Group 1: (No enzyme control)

Group 2:

Group 3:

Group 4:

Group 5:

Group 6:

Group 7:

Average

Standard deviation

Cold (0 degree celcius)

0

29

37

15

57

32

21

27.29

17.97

Room temperature (19 degree celcius)

0

14

42

22

28

25

63

27.271

20.19

Warm (50 degree celcius)

0

12

28

53

40

43

70

35.14

23.95

Boiled (70 degree celcius)

0

3

0

1

0

2

5

1.57

1.90

(Table: Impact of alteration in temperature on the rate of reaction)

pH buffer

pH 4

pH 6

pH 7

pH 8

pH 10

Group: 1

0

1

1

2

6

Group: 2

0

0

0

0

7

Group: 3

0

0

1

1

4

Group: 4

20

31

65

11

33

Group: 5

10

33

58

17

48

Group: 6

14

41

47

7

21

Group: 7

5

21

38

30

24

Group: 8

12

13

27

36

42

Group: 9

4

24

32

25

35

Group: 10

4

15

24

22

24

Average

6.9

17.9

29.3

15.1

24.4

Standard deviation

6.84

14.68

23.54

12.86

15.36

(Table 3: Indicating the result of alter in pH on the rate of reaction)

Discussion on Impact of Temperature on Catalase Activity

The main rationale of doing this research was to investigate the impact of wide-ranging substrate concentrations, temperatures of catalase, and ranges of pH on catalase commotion. The hypothesis has also been tested which indicates that when there is an increase in substrate concentration, the reaction rate will also augment until and unless every active site were bound. On the other hand, it was also focused to examine the hypothesis as to when the temperature increases, the reaction also increases until the enzymes were denatured. The catalase activity correspondingly decreases concerning the alteration in the optimal level of pH. The foam quantity in ml has been increased ranging from 0 to 45 due to an increase in substrate concentration extending from 0% to 30% respectively. This indicates that the conducted statistics support the hypothesis in experiment part 1 as the substrate concentration has caused the rate of reaction to incline drastically. As there is an increase in substrate concentration, more number of substrate molecules will likely to combine with additional enzyme molecules. Thus, it creates a high product quantity and increases the reaction rate.

Now, in experiment part 2, the data indicated an incline of reaction rate when there is an increase in temperature but subsequently declined when the temperature has been increased to 70 degree Celsius. The hypothesis reveals that the reaction rate must have accelerated as there was an increase in temperature until denaturing the enzymes. Since the enzyme has been heated extremely, making it inactive and less impacting the reaction speed (Aronson et al., 1956).

In experiment part 3, foam quantity in ml inclined from an average of 6.9 ml to 29.3 ml while changing the pH from pH 4 to pH 7. However, it significantly declined to 15.1 ml as changed from pH 7 to pH 8. This proves that pH impacts the breakdown of enzyme catalase of hydrogen peroxide.

Limitations might affect the results of the inability in controlling, inaccuracy in measurements, and contradiction due to human miscalculation. Concerning further experiments, ensuring exact group measurement and an individual to swirl the solutions will result in getting accurate data.

References for Impact of Temperature on Catalase Activity

Aronson, D., Fraser, M., & Smith, C. (1956). Enzyme Alteration by Ionizing Radiation. Radiation Research, 5(3), 225. https://doi.org/10.2307/3570404

Kimbrough, D., Magoun, M., & Langfur, M. (1997). A Laboratory Experiment Investigating Different Aspects of Catalase Activity in an Inquiry-Based Approach. Journal Of Chemical Education, 74(2), 210. https://doi.org/10.1021/ed074p210

Ranjan, S., & Mallik, A. (1931). A Study of the Catalase Reaction, with Special Reference to Respiration in Plants. New Phytologist, 30(5), 355-355. https://doi.org/10.1111/j.1469-8137.1931.tb07427.x

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