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Factors Affecting The Rate Of Enzymes Activity Biology

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Enzymes are accelerators made within the human organic structure. Catalysts of course, lower the activation energy required for reactions. The lower the activation energy is, the faster the rate of reaction is, and hence enzymes speed up reactions in the organic structure by take downing the activation energy required. ( Diet-Health.net )

There are many factors that contribute to the rate of reaction of an enzyme. Factors include: concentration of the enzyme, temperature, pH degree, concentration of the substrate, and inhibitors. This lab shows the affects these factors have on the rate of reaction between catalase, an enzyme found in murphies, and H peroxide, the substrate.

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The specific enzyme that was studied during this lab was catalase. Catalase is a of course happening enzyme that is found in many populating beings such as workss and the human organic structure. Catalase breaks down H peroxide, a really harmful oxidising agent for cells ( Catalase ) . A individual catalase molecule can interrupt down 1000000s of H peroxide molecules in a given minute.

Catalase breaks down H peroxide into H2O and O. Hydrogen peroxide is a natural waste merchandise which forms when the organic structure breaks down fatty acids and converts that into energy. Hydrogen peroxide besides forms when white blood cells break down and kill bacteriums in the organic structure. Catalase is besides helpful in prevent the formation of C dioxide bubbles in the blood. Catalase can assist interrupt down other harmful chemicals in the organic structure such as intoxicant, phenol, and methanal ( VitaminStuff.com ) .

As mentioned before, enzymes play a important function in organic chemical science. Catalase is one of the most accepted enzymes found in life beings. This lab provides the clear and apprehensible information of the enzyme being studied, catalase, and proves the affects of the factors that contribute to an enzyme ‘s rate of reaction.

Part 1: Change in Enzyme Concentration

Table 1:

Enzyme concentration & A ; composings

Distance ( centimeter )

Time ( s )

Rate of Change ( cm/s )

Other observations

100 % concentration ( 10 milliliter murphy juice )

8 centimeter

3.02 s

2.65 cm/s

– bubbles appeared

80 % concentration ( 8 milliliter murphy juice, 2 milliliter distilled H2O )

8 centimeter

5.06 s

1.58 cm/s

– fewer bubbles than old composing

60 % concentration ( 6 milliliter murphy juice, 4 milliliter distilled H2O )

8 centimeter

6.28 s

1.27 cm/s

– fewer bubbles than old composing

40 % concentration ( 4 milliliter murphy juice, 6 milliliter distilled H2O )

8 centimeter

7.5 s

1.07 cm/s

– fewer bubbles than old composing

20 % concentration ( 2 milliliter murphy juice, 8 milliliter distilled H2O )

8 centimeter

19.65 s

0.41 cm/s

– no bubbles appeared

Graph 1:

Analysis 1:

Harmonizing to the observation graph 1, the major tendency shows that as the concentration of the catalase, which is in the murphy juice, additions there is besides an addition in the rate of reaction. As the concentration of the catalase decreased, the rate of reaction besides decreased.

Part 2: Change in Temperature

Table 2:

Temperature ( A°C )

Distance ( centimeter )

Time ( s )

Rate of Reaction ( cm/s )

10.0

8.00

5.85

1.38

21.0

8.00

4.83

1.66

35.0

8.00

2.99

2.68

50.0

8.00

4.21

1.90

80.0

8.00

5.52

1.45

Graph 2:

Analysis 2:

Observation graph 2 shows the relationship between the environmental temperature and the rate of reaction. Harmonizing to the observation chart the optimum temperature was 35°C. The optimum temperature being the temperature at which the enzyme reacted the fastest. Any temperature higher or lower than 35°C, the catalase molecules did non respond as fast.

Part 3: Change in pH Degree

Table 3:

Sum of H2O2 ( milliliter )

Sum of Distilled Water ( milliliter )

Sum of pH Buffer ( milliliter )

pH Level

Vertical Distance Travelled by Filter Paper Towards Meniscus

Time taken by filter paper phonograph record to travel to meniscus ( s )

Upward speed of Filter Paper Disc ( cm/s )

10 milliliter

5 milliliter

7 ( Control )

8.15

6.6

1.23

10 milliliter

5 milliliter

2

7.98.15

16.65

0.47

10 milliliter

5 milliliter

4

8.15

7.05

1.16

10 milliliter

5 milliliter

9

8.1

10.4

0.78

10 milliliter

5 milliliter

12

7.85

8.14

0.96

Graph 3:

Analysis 3:

Harmonizing to graph 3, the optimum value was the pH degree of 7. At the pH degree of 7, the rate of reaction was the fastest, any pH degree higher or lower than that of 7 the enzyme ‘s rate of reaction would diminish. This relationship was much like that of the temperatures, anything above or below the optimum value the rate of reaction lessenings.

Part 4: Change in Substrate Concentration

Table 4:

Concentration of

H202 of Distilled Water

Test

Time of catalase to go from the underside of the trial tubing to the top ( s )

Distance of underside of trial tubing to substrate ( centimeter )

Rate of alteration of the catalyzed reaction ( cm/s )

15 milliliter of H202

3 %

1

5.89

8.0

1.36

2

6.86

8.0

1.17

Entire

6.38

8.0

1.27

13 milliliter of H202 2.6 %

1

8.13

8.0

0.98

2

7.11

8.0

1.13

Entire

7.62

8.0

1.01

10 milliliter of H202 2 %

1

8.65

8.0

0.87

2

12.8

8.0

0.63

Entire

10.73

8.0

0.75

7.5 milliliter of H202 1.5 %

1

9.43

8.0

0.84

2

12.53

8.0

0.64

Entire

10.98

8.0

0.74

5 milliliter of H202 1 %

1

10.37

8.0

0.77

2

12.88

8.0

0.62

Entire

12.63

8.0

0.70

Graph 4:

Analysis 4:

Harmonizing to graph 4, as the concentration of the substrate ( hydrogen peroxide ) increases the rate of reaction besides increases. This relationship was much like that of the alteration in enzyme concentration.

Part 5: Addition of an Inhibitor

Table 5:

Experiment Number

Sum of Inhibitor ( Cu ( II ) sulfate beads )

Time ( s )

Distance ( centimeter )

Rate of alteration ( cm/s )

1

0

4.13

8.0

1.94

2

1

4.68

8.0

1.71

3

5

5.57

8.0

1.44

4

10

6.66

8.0

1.20

5

15

8.57

8.0

0.93

Graph 5:

Analysis 5:

Harmonizing to graph 5, as there was an addition in the beads of Cu ( II ) sulfate ( the inhibitor for this lab ) there was a lessening in the rate of reaction. This was due to the fact that the Cu ( II ) sulfate blocked the active site of the catalase.

Evaluation: Decision

For each portion of the lab, there were hypothesis made in the beginning of the experiments. Each experiment was done and observed and a decision was reached on whether the hypothesis for the experiment made sense and was proven.

Part 1: Change in Enzyme Concentration

Hypothesis: If there was an addition in the concentration of the catalase, so there would be an addition in the rate of reaction.

This hypothesis was proven to be true. As there was an addition in the concentration of the enzyme, the catalase, there was an addition in the rate of reaction. This was due to the fact that there were more catalase enzymes available for the substrates to adhere to and shortly respond with. The concentration of the substrate was maintained at the of course available concentration, there were no alterations made. That meant that there were more active sites available to the substrates to adhere to. The more the active sites there were, the more substrates were being reacted at the same clip, hence diminishing the clip it took to to the full respond with all the substrate molecules.

Table 2: Change in temperature

Hypothesis: If the temperature of the environment environing the reaction increases the rate of reaction will besides increase, until it reaches the optimum point, the point at which the rate of reaction will get down to diminish.

The hypothesis was proven to be true every bit good. The rate of reaction did increase until it reached the optimum point. At the optimum point ( 35°C ) the rate of reaction was the highest, which meant the most figure of H peroxide molecules were responding with the enzymes during the experiment at that specific temperature. In other words, the optimum point was when the enzymes worked the best. As the temperature rose, the molecules possessed more kinetic energy. The more kinetic energy there was, the more the molecules moved and collided with one another, increasing the rate of reaction, until it reached the optimum point. Once the temperature started to increase higher than 35°C the catalase started to denature, which meant the form of the enzyme would get down to differ. The denaturing catalase decreased the rate of reaction because there were n’t every bit many healthy normal catalase molecules to keep the rate or even increase it.

Part 3: Change in pH Degree

Hypothesis: If the pH degree of the substrate increased so the rate of reaction will besides increase until an optimum pH degree is reached. Anything above or below the optimum pH degree the enzyme will denature.

This hypothesis was besides proven to be true. The optimum pH degree was 7, impersonal, for the catalase. This meant at pH 7, the most enzyme-substrate reactions were taking topographic point at that specific clip. Enzymes work within a little pH scope, hence pH degrees tend to hold a great impact on the enzyme-substrate activity ( Nelson Biology 12 ) . Any pH degree above or below 7 started to denature the enzyme, decelerating down the rate of reaction. Denaturing enzymes meant that the form of the overall enzyme had changed. This meant that at the pH degrees of 2, 4, 9 or 12 the form of the active site for the substrate to bond to would alter, decelerating down the procedure. At the pH degree of 7, catalase ‘s activity was the greatest.

Part 4: Change in Substrate Concentration

Hypothesis: If the concentration of the substrate ( hydrogen peroxide ) increases the rate of reaction besides increases.

This hypothesis was proven to be true. This relationship was much like that of the concentration of the catalase. As the concentration of the substrate increased the rate of reaction besides increased because there were more hydrogen peroxide molecules available to respond with the catalase. However, at one point ( the point of impregnation, which was n’t achieved in this lab ) the rate of reaction would be changeless. That meant at a given point during the experiment, all of the active sites of the catalase would be occupied with a H peroxide molecule and the rate of reaction would neither increase nor diminish. Strictly looking at the experiment observed, the rate of reaction was increasing as the substrate concentration was increasing because there were more substrates available to respond with an enzyme at a specific clip.

Part 5: Addition of an Inhibitor

Hypothesis: If the add-on of an inhibitor increased so that means the rate of reaction would diminish.

This hypothesis was besides proved correct. The Cu ( II ) sulfate acted as an inhibitor for the experiment. When added, the Cu ( II ) sulfate attached itself to the active site of the catalase molecules, doing the rate of reaction to diminish. The Cu ( II ) sulfate was meant to barricade the active site, which it did successfully, therefore the lessening in the rate of reaction. This meant, the more Cu ( II ) sulfate was added the lower the rate of reaction would be. This is because this inhibitor stalls the reaction clip because there are less reactions taking topographic point at that minute in clip, due to the fact that the active sites are blocked off from the H peroxide molecules.

Evaluation: Beginnings of Mistake

Throughout this lab there were many mistakes made that were uncontrolled and/or unaccounted for. These mistakes were non human mistakes, which were tried to be reduced to the minimum if non none. Some beginnings of mistake included: the trial tubing measurings, mistakes sing the filter paper phonograph record and the inconsistent concentration of the catalase.

The trial tubings were meant to be all the same form and keep the same sum. However this was non the instance for every individual trial tubing. To the human eyes the sum in the trial tubing might look the same but in world the sum might change. This is due to the fact that the trial tubing from the interior do non all have the same form, after all trial tubings are human made and there is a opportunity of major human mistake during that procedure every bit good. The trial tubes non being consistent meant that there was room for mistake in measurings. Even though the volume of the catalase and the H peroxide were measured out exactly, the measurings that were made utilizing a swayer were non. This was due to the fact that the trial tubings were non all the same, and that the human oculus is non precise in analysing such measurings. This meant there were infinite mistakes throughout the lab.

For many procedures the filter paper phonograph record, which was dipped in the murphy juice, did non ever drop to the underside of the trial tubing. Even with the aid of forceps and plastic pipettes, which were used to help the filter paper phonograph record to the underside of the trial tubing, the filter paper phonograph record did non make the underside. This was because the catalase that was absorbed into the filter paper phonograph record automatically started responding with the H peroxide. They were really inconsistent, some filter paper phonograph record took a longer clip to be pushed to the underside and others merely sank, and since clip was a major facet to the lab this caused many mistakes.

Catalase concentration was besides a beginning of mistake. There were many murphies that were land and made into potato juice for the intent of this lab. Naturally, they would transport different concentration of catalase because of the different ways they were grown. There might be a murphy that had many foods while it was still maturating in the field and a murphy that hardly got any foods. The concentration of the catalase used in one portion of the lab would be higher or lower than the concentration of the catalase used in another portion because of the different murphies used. This affected the lab because, like observed before, the higher the concentration of the catalase the higher the rate of reaction there will be. In the hereafter, if merely one murphy was land and made into potato juice would assist command this facet of the lab.

These were merely three chief mistakes observed during this lab. There were many more, sing the separate subdivisions of the lab.

Evaluation: Following Stairss

Throughout this lab there were many processs that could hold been done otherwise or to a different point. Another lab could hold been carried out with another natural enzyme which could hold been comparable to the factors and affects of catalase. Besides, the impregnation degree was undiscovered for the enzyme ( in footings of concentration, and the inhibitors ) . Both are processs that could hold been carried to obtain a better apprehension of enzymes.

Another illumination lab would hold been helpful if done, because so the factors and the affects these factors had on the rate of reactions could hold been compared for a better apprehension. There is another of course happening enzyme that portions features with catalase. This enzyme is called amylase. Amylase is a accelerator that hydrolysis ‘ polyoses starch into disaccharide malt sugar. Amylase can be found in the spit, produced in the salivary secretory organs and the pancreas. If amylase is added to starch solution, the amylum will shortly interrupt down to organize malt sugar ( Enzyme Lab ) . Both catalase and amylase are natural happening enzymes found in the human organic structure and they are great for comparing with one another. If the same lab was done with amylase this lab would assist others understand a little more in the similarities and differences between enzymes.

One other suggestion would be to transport out the experiments to the full potency. After reading and analyzing enzymes, it is clear that there are impregnation points for the substrate concentration and the affects of an inhibitor ( Nelson Biology 12 ) . Impregnation points refer to the point at which there is no addition or lessening in the rate of reaction between the catalase and H peroxide. The experiment that required the addition in the substrate concentration could hold been ( and should hold been ) carried out until the point of impregnation was observed. This is when the rate of reaction corsets at a changeless because all the active sites are occupied by H peroxide molecules and no other reactions can happen. This could hold besides been possible with the inhibitor portion of the lab. At one point no reactions would happen because the inhibitors would hold been barricading all the possible active sites for the H peroxide to respond with. This is besides referred to as a impregnation point. If these impregnation points were observed, there would ‘ve been a better apprehension of the affects the different factors had on the enzyme.

For future labs, both these procedures should be considered, if non acted upon. With both procedures there is the handiness to foster the apprehension of enzymes and their capablenesss in life beings.

Work Cited

“ CATALASE -ANTIOXIDANT BENEFITS, INFORMATION ON SUPPLEMENTS, ARTICLES, LINKS, NEWS, ADVICE. ” VITAMINSTUFF – A RESOURCE FOR VITAMINS, HERBS, ANTIOXIDANTS, AND ALTERNATIVE MEDICINE. N.p. , n.d. Web. 1 Mar. 2010. & lt ; hypertext transfer protocol: //www.vitaminstuff.com/catalase.html & gt ; .

“ Catalase – An Extraordinary Enzyme. ” Catalase Home Page ( Index page for hypertext transfer protocol: //www.catalase.com ) . N.p. , n.d. Web. 1 Mar. 2010. & lt ; hypertext transfer protocol: //www.catalase.com/cataext.htm & gt ; .

“ Enzyme Lab – Ex. 4. ” Welcome to Eve. N.p. , n.d. Web. 1 Mar. 2010. & lt ; hypertext transfer protocol: //eve.kean.edu/~breid/enzyme/enzyme.html & gt ; .

“ Enzymes – Enzyme – Biological Catalysts – Diet and Health.net. ” Diet and Health.net. N.p. , n.d. Web. 1 Mar. 2010. & lt ; hypertext transfer protocol: //www.diet-and-health.net/Supplements/Enzymes.html & gt ; .

“ Protein Digestion: A Trip Through the Gut. ” Oracle ThinkQuest Library. N.p. , n.d. Web. 1 Mar. 2010. & lt ; hypertext transfer protocol: //library.thinkquest.org/11226/main/c14txt.htm & gt ; .

“ Substrate – definition from Biology-Online.org. ” Life Science Reference – Biology Online. N.p. , n.d. Web. 1 Mar. 2010. & lt ; hypertext transfer protocol: //www.biology-online.org/dictionary/Substrate & gt ; .

“ catalase: Definition from Answers.com. ” Answers.com: Wiki Q & A ; A combined with free online lexicon, synonym finder, and encyclopedias. N.p. , n.d. Web. 1 Mar. 2010. & lt ; hypertext transfer protocol: //www.answers.com/topic/catalase & gt ; .

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Cite this Factors Affecting The Rate Of Enzymes Activity Biology

Factors Affecting The Rate Of Enzymes Activity Biology. (2017, Jul 12). Retrieved from https://graduateway.com/factors-affecting-the-rate-of-enzymes-activity-biology-essay/

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