BIO150 LAB REPORT - the fastest enzyme (catalase) PDF

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FAKULTI SAINS GUNAANUNIVERSITI TEKNOLOGI MARACAWANGAN PERAK KAMPUS TAPAHBIO150 – METABOLISM & CELL DIVISIONSCIENTIFIC LAB REPORTNAME:STUDENT ID: 2020451586GROUP: ASEXPERIMENT TITLE: THE FASTEST ENZYME: CATALASELECTURER: MS. HUSNA ZULKIPLIDATE OF SUBMISSION:---------------------------------------...

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FAKULTI SAINS GUNAAN UNIVERSITI TEKNOLOGI MARA CAWANGAN PERAK KAMPUS TAPAH BIO150 – METABOLISM & CELL DIVISION

SCIENTIFIC LAB REPORT NAME: STUDENT ID: 2020451586 GROUP: EXPERIMENT TITLE: THE FASTEST ENZYME: CATALASE LECTURER: MS. HUSNA ZULKIPLI

DATE OF SUBMISSION: -------------------------------------------------------------------------------------------------------------------------- Declaration of Academic Honesty Academic honesty or academic integrity is a very important virtue that all students should uphold at all times. I declare that the lab report submitted is not plagiarised and is entirely my own work, and that no part of it has been copied from any work produced by other person(s)/ source(s) or provided by any other student(s). I understand that issuing a false declaration can result in severe penalties and I am willing to be penalized if any form of copying is found valid.

INTRODUCTION

Enzyme is a substance found in living organisms that acts as a catalyst, regulating the rate at which chemical reactions happen while remaining unchanged by the process. Majority of these biochemical reactions do not take place simultaneously, instead they are regulated by enzymes. Enzymes catalyze all types of cell metabolism. Enzymes help to break down large molecules to smaller molecules, DNA replication and to break down toxins in the liver.

Several factors influence enzyme activity, including substrate concentration and the presence of inhibiting molecules. When all active sites of the enzyme molecules are engaged, the rate of an enzymatic reaction increases with increasing substrate concentration, reaching maximum velocity. Thus, the rate at which the active sites transform substrate to product influences the rate of enzymatic reaction.

Catalase is a natural enzyme found in nearly all organisms that are exposed to oxygen. Catalase protects living cells from oxidative damage, which may happen when cells or other molecules in the body interact with oxidative compounds. Byproducts of the reactions, such as hydrogen peroxide, may be toxic to the body. To avoid this, the catalase enzyme assists in the elimination of these harmful compounds by converting hydrogen peroxide (H₂O₂) into inert water and oxygen.

The aim of this experiment was to look into the relationship between substrate concentration and the enzymatic reaction rate. Seeing as catalase enzymes are present in the liver, kidney, and potato, they are used in this experiment. Liver and kidney is linked to the organ's function in cleansing the body of various toxins. However, the liver contains the highest concentration of catalase enzyme as it functions to detoxify substances in the body. Plants, on the other hand, contain catalase enzymes. Catalase enzymes are required in photorespiration even though plants do not break down toxins.

Objective : To determine the relationship between the rate of catalase enzyme reaction and the concentration of hydrogen peroxide .

Problem statement : Will the rate of catalase enzyme reaction increase when the concentration of hydrogen peroxide increases ?

Hypothesis : The rate of catalase enzyme reaction will increase as the concentration of hydrogen peroxide increases.

Apparatus : 10ml test tube and rack, 10ml graduated cylinder, 100ml beaker, dropper, ceramic square, scalpel, tongs, rubber stoppers, wooden splinter, pestle and mortar, spatula, wire gauze, bunsen burner.

Material : Liver, kidney, potato, hydrogen peroxide.

Procedure :

Part A: 1. 2ml of hydrogen peroxide was poured into test tubes. 2. 1cm cube of liver was cut and dropped into a test tube of hydrogen peroxide. 3. Rubber stopper was inserted and the test tube was swirled gently. 4. Reaction in the test tube was observed and recorded. 5. Presence of oxygen was tested using a glowing wooden splinter. 6. Step 2-5 was repeated using 1 cm cube of kidney and potato respectively.

Part B: 1. 1cm cube of liver was grinded and transferred into a test tube of hydrogen peroxide. 2. Rubber stopper was inserted and the test tube was swirled gently. 3. Reaction in the test tube was observed and recorded. 4. Presence of oxygen was tested using a glowing wooden splinter. 5. Step 1-4 was repeated using 1 cm cube of grinded kidney and grinded potato respectively.

Part C: 1. 1cm cube of liver was boiled in a beaker for 3 minutes and dropped into a test tube of hydrogen peroxide. 2. Rubber stopper was inserted and the test tube was swirled gently. 3. Reaction in the test tube was observed and recorded. 4. Presence of oxygen was tested using a glowing wooden splinter. 5. Step 1-4 was repeated using a 1 cm cube of boiled kidney.

RESULTS

PART A : Material

Observations

Presence of oxygen

Cube of liver

Colourless gas bubble are

Glowing wooden splinter

released at a slow rate

lit up

Colourless gas bubble are

Glowing wooden splinter

released at a slow rate

lit up

Colourless gas bubble are

Glowing wooden splinter

released at a slow rate

lit up

Material

Observations

Presence of oxygen

Ground liver

Colourless gas bubble are

Glowing wooden splinter

released at a fast rate

lit up

Colourless gas bubble are

Glowing wooden splinter

released at a fast rate

lit up

Colourless gas bubble are

Glowing wooden splinter

released at a fast rate

lit up

Material

Observations

Presence of oxygen

Boiled liver

Colourless gas bubble

Glowing wooden splinter

were not released

did not lit up

Colourless gas bubble

Glowing wooden splinter

were not released

did not lit up

Cube of kidney

Cube of potato

PART B :

Ground kidney

Ground potato

PART C :

Boiled kidney

DISCUSSION

As an organism, oxygen is essential to us. Oxygen plays a critical role in respiration, the energy-producing process that powers most living organisms' metabolisms. To remain alive and for our bodies to generate energy, we humans, like many other animals, need oxygen in the air we breathe. However, oxygen is a double edged sword. Despite its importance to us, it also creates hydrogen peroxide as a waste product of the biochemical process. Hydrogen peroxide is a chemical that may break apart to yield hydroxyl radicals that targets crucial biochemicals in our systems such as proteins and DNA.

Fortunately, catalase enzymes are present in our body. The purpose of catalase in living cells is to protect them from oxidative damage when cells or other molecules in the body come in contact with oxidative compounds. Catalase enzymes may aid in the decomposition of hydrogen peroxide in this scenario. The hydrogen peroxide can be converted into harmless byproducts such as water and oxygen.

2H₂O→ 2H₂O + O₂

The corresponding equation gave us a vision of why colorless gas bubbles were produced when different materials were placed into a test tube containing hydrogen peroxide.

In part A, 1cm cube of liver, kidney and potato were inserted into three separate test tubes containing hydrogen peroxide. The colorless gas bubbles were released slowly by all three of them. at a slow rate. The only difference between the samples is the amount of colorless gas bubbles produced as they interacted with hydrogen peroxide. For instance, the liver released a large amount, the kidney released a moderate amount and lastly the potato released a small amount of colourless gas bubbles. The concentration of catalase enzyme in each material determines the colorless gas bubbles released. As a result, the liver produces the most colorless gas bubbles when compared to the kidney and potato since it contains the highest concentration of catalase enzyme. A larger amount of catalase enzyme reduces activation energy and thus accelerates the rate of the reaction. This is due to the liver's function as the detoxifying organ in our bodies.

In part B, ground liver, ground kidney and ground potato were inserted into three different test tubes. All of them released the colourless gas bubbles at a faster rate than part A where the gas bubbles were released at a slower rate with the differences in the amount of colourless gas bubbles released . This is due to the fact that the surface area of the materials is greater when grounded compared to cubed materials. Higher surface area speeds up the reaction by reducing the amount of energy required to break down the molecules. As a result, the reaction will be quicker. In contrast, the amount of colorless gas bubbles produced in A is the same for all three materials studied.

In part C, 1cm cube of boiled liver and boiled kidney was inserted into two different test tubes containing hydrogen peroxide. Unlike in part A and B, materials in part C did not release any colourless gas bubbles when exposed to hydrogen peroxide. In simple terms, the reaction did not occur between the boiled materials and the hydrogen peroxide. This is because the substance was previously boiled in a beaker at temperatures over 60℃, which is above the optimal temperature for enzymes. The optimal temperature for an enzyme to function is 37℃, where the kinetic energy in the substrate and enzyme is ideal for the maximum number of effective collisions.The shape of the enzyme changes at temperatures above 60℃, and it is no longer complementary to its basic substrate. As a result, after the enzyme has been denatured, there is no reaction between the boiled materials and hydrogen peroxide.

Furthermore, oxygen is present in all of the materials in parts A and B but not in part C. The colourless gas bubbles produced by the reaction between materials and hydrogen peroxide is proven to be oxygen. This is due to the fact that the glowing wooden splinter was lit up as it was put into the test tubes of materials for part A and B. However, when placed into the test tubes of materials for part C, the glowing wooden splinter did not light up. As a result, there is no oxygen in part C because the reaction between materials and hydrogen peroxide did not occur because the enzyme was denatured.

Other factors that may affect the result of this experiment must be kept constant. For instance, temperature and enzyme concentration. We must use the same amount of samples throughout the whole experiment so that we can get an accurate answer with a small margin of errors.

CONCLUSION

The aim of this experiment was fulfilled. The relationship between hydrogen peroxide concentration is proportional to the enzymatic reaction rate of catalase. When the concentration of hydrogen peroxide increases, the enzymatic reaction rate of catalase will increase as well. Therefore, the hypothesis is accepted.

REFERENCES

1. Essays, UK. (November 2018). Effect of Enzyme Catalase on Hydrogen Peroxide. Retrieved from https://www.ukessays.com/essays/biology/differentconcentrations-of-enzyme-effect-o n-reaction-rate-biology-essay.php?vre

2. Helmenstine, Anne Marie, Ph.D. (2019, February 1). Peroxide Definition and Facts. Retrieved from https://www.thoughtco.com/definition-ofperoxide-60549

3. UCAR Center for Science Education. (2014). Oxygen. https://scied.ucar.edu/learning-zone/air-quality/oxygen

4. Joe Schwarcz Phd. (2017, January 18). Hydrogen Peroxide: the body’s best defence system. McGill Office for Science and Society. https://www.mcgill.ca/oss/article/general-science-you-asked/hydrogen-peroxide-bodys -best-defence-system#:~:text=In%20this%20case%20oxygen%20is,an%20enzyme% 20found%20in%20liver.&text=To%20protect%20itself%2C%20the%20body,it%20can %20form%20hydroxyl%20radicals

5.

Science Buddies, & Svenja Lohner. (2016, November 10). Exploring Enzymes. SCIENTIFIC AMERICAN. https://www.scientificamerican.com/article/exploring-enzymes/...