ipl-logo

Catechol Oxidase Lab Report

542 Words3 Pages
bulb-icon

Recommended: Effect of enzyme concentration on kinetics

The different possible substrates for avocado catechol oxidase have very different Km’s and Vmax’s (Table 1). The Km’s range from 0.7 to 95, and the Vmax’s range from 0.58 x 105 to 17 x 105. The enzyme’s own substrates catechol has a Km of 6.5 and a Vmax of 5.4 x 105. Some of the substrates are better suited for catechol oxidase than others. For example, dopamine has a Km of 95 and a Vmax of 11 x 105. Both of these values are fairly high and would not make an effective substrate for catechol oxidase since the enzyme has a low affinity for the substrate. An example of a good alternative substrate would be 4-methylcatechol that has a low Km of 1.1 and a Vmax of 3.4 x 105. The enzyme now has a high affinity for the substrate and therefore requires less substrate to meet its Vmax. The substrate for the sweet potato catechol oxidase is N-phenylthiourea. In comparison to the possible substrates for catechol they both have hydrogen acceptor sites that can be used to hydrogen bond in the active site of the enzyme. Along with hydrogen bonding there may be some ionic bonding between some metal atoms in the active site of the enzyme and the substituents coming off of the benzene ring. …show more content…

However, the Vmax values for the avocado are much higher than the values for the banana or the mushroom. It would appear that the avocado and banana are more closely related because the enzyme showed similar affinity for the alternative substrates. This makes sense because on the tree of life mushrooms and green plants split long before monocots and dicots split. Meaning that monocots and dicots are more closely related than they are to mushroom. In this study, the avocado comes from a dicot and the banana comes from a

Show More
Related
1117 Words | 5 Pages

The temperature in our experiment was not very high which didn’t result in denaturation of peroxidase. The temperature seemed to be a constant that didn’t affect the experiment. If the temperature was higher in pH 3 and low in pH 10, then it would cause pH 3 to denature even more which would make the pH 3 total about 4.0. Substrate concentration basically means the amount used for the substrate. The substrate in our experiment was 0.1% hydrogen peroxide.

Read More
247 Words | 1 Pages

An enzyme can not be considered a reactant because, like catalysts, the enzyme is never used up in the reaction and is reused again in another chemical reaction. In this lab, the source of hydrogen peroxidase was the potato solution. The substrate that the hydrogen peroxidase acts upon is the hydrogen peroxide.

Read More
1090 Words | 5 Pages

ABSTRACT To catalyze a reaction, an enzyme will grab on (bind) to one or more reactant molecules. In this experiment we examined how increasing the volume of the extract added to the reaction would affect the rate of the reaction. The enzyme used was horseradish peroxidase which helps catalyze hydrogen peroxide. Using different pH levels, the absorbance rate of the reaction was measured to see at which condition the enzyme worked best. The rates of absorption were calculated using a spectrophotometer in 20 second intervals up to 120 seconds.

Read More
506 Words | 3 Pages

Throughout this work, a correlation between the enzyme activity and temperature existed. The data for both showed that at the temperature extremities the lower the enzyme activity was; except for the bacterial enzyme at 0°C. At high temperatures, an enzyme denatures or changes shape, making it difficult or impossible for a substrate to bind, and at low temperatures, the frequency and rate of reaction decreases causing for a halt in product formation (Pitzer et.al., 2012). Thus, showing that enzymes need to be in their optimal environments to work properly. Bacillus lincheniformis and Aspergillus oryzae are both organisms that live that in medium temperature environments.

Read More
461 Words | 2 Pages

Amount of catalase enzyme added b. 0.5 cm3 c. cm3 d. 10 cm3 test tubes. The catalase enzyme was added to each test tube, so the reaction was possible. 4. Height of Oxygen Bubbles b. cm c. 10 cm3 test tubes, 0.5 cm3 catalase enzyme, 4 cm3 of H2O2, and Certain Temperature (10 degrees C, 20 degrees C, 30 degrees C, 60 degrees C) The test tube is where the dependent variable that is measured.

Read More
1389 Words | 6 Pages

Conclusion In conclusion, the reason why this lab was conducted to examine the effects of Hydrogen Peroxide coming into contact with a catalase solution, in this experiment it was Calf Liver. As a result of the contact, oxygen gas was formed. Therefore, the collected data suggested the rate of reaction of the catalyse increases as the volume of Hydrogen Peroxide increases. This can be seen through the linear trend line that moves up in a positive direction, which shows that the relationship between the rate of reaction and the volume of hydrogen peroxide is positive.

Read More
1860 Words | 8 Pages

Most enzymes work best at body temperature of 37 (degrees Celsius). PH is another factor that affect the rate of enzymes activity. Enzymes function slowly in lower pH like in the pH of 1 or 2. Potato are high catalase when is being placed in a pH of 2 solution and hydrogen peroxide is added to it there will be some fizzing but not a good one. If the potato is placed in a pH of 13 and hydrogen peroxide is added there wouldn?t be any fizzing or little fizzing meaning that high pH either denature the catalase or substrate can not bind to the active site of an enzymes because its changes its shape.

Read More
750 Words | 3 Pages

Introduction: Enzymes are biological catalysts that increase the rate of a reaction without being chemically changed. Enzymes are globular proteins that contain an active site. A specific substrate binds to the active site of the enzyme chemically and structurally (4). Enzymes also increase the rate of a reaction by decreasing the activation energy for that reaction which is the minimum energy required for the reaction to take place (3). Multiple factors affect the activity of an enzyme (1).

Read More
1303 Words | 6 Pages

Enzymes are biological catalysts made of proteins that accelerate chemical reactions by lowering their activation energy therefore increasing the activity rate of the enzyme and more substrates turned into products. The ‘Catalase’ enzyme that was used during this experiment was obtained from peroxisome found in celery which are organelles found in bacteria, plant, and animal cells. It is involved in the breaking down of certain substances and the diminish of reactive oxygen species and that includes hydrogen peroxide (H2O2) which can be a byproduct of the metabolism of oxygen. Hydrogen peroxide is toxic to the cell and so the catalase enzyme is utilised to break down H2O2 to form oxygen molecules and water free of free radicals.

Read More
971 Words | 4 Pages

Enzymes consist of an active site, this active site is unique to the substrate which it binds to. The active site is a tertiary structure which defines what substrate can bind to the active site. The active site is therefore highly specific. The structure and function of enzymes are compared to the lock and key hypothesis, where the lock is the enzyme and the key being the substrate. Another theory which has been presented is the induced fit hypothesis, where the tertiary structure in the active site changes slightly when bonded to the substrate to strengthen the bond between the active site and the substrate.

Read More
560 Words | 3 Pages

The results of the effect of substrate concentration on catalase activity (Figure 3.)  also matched the expectations of the experiment. It was assumed that when the maximum velocity was reached, all of the available enzyme had been converted to the enzyme-substrate intermediate. We can tell from the figure that the maximum velocity reaches approximately 100 O2/min before all of the enzyme had been converted to the enzyme substrate complex (Worthington Biomedical Corporation).

Read More
328 Words | 2 Pages

The Metarhizium genus consists of cosmopolitan fungi that infect a wide range of arthropod hosts. The infection is a complex process enclosing several steps, typically culminating in host death. During infection, Metarhizium spp. form different infection-specialized cellular structures and secrete a set of hydrolytic enzymes that helps to breach the chitin-rich host cuticle and to access the host hemolymph. Amongst these secreted enzymes there are chitinases.

Read More
1046 Words | 5 Pages

Without enzymes, the pathways of metabolism would become congested because the chemical reactions would take a very long time. Heat can increase the rate of reaction by allowing reactants to attain the transition state more often, but wouldn’t work well in biological systems. High temperatures denature proteins and will kill them, so instead organisms use catalysis to speed up the reactions. The way an enzyme catalyzes a reaction is by lowering the E_A barrier to enable the reactant molecules to absorb energy to react the transition state even at moderate temperatures. Enzymes can’t make endergonic reactions exergonic.

Read More
1563 Words | 7 Pages

Catalase (CAT) activity 255 With slight modifications, catalase activity was assayed according to the method of Aebi 256 (41) by monitoring the disappearance of H2O2 at 240 nm. The 3 ml reaction

Read More
1973 Words | 8 Pages

1.Introduction: An enzyme is a large protein that acts as a biological catalyst which changes the rate of a reaction. It provides an active site which is an environment where a reaction can take place this is made up of amino acids. The structure and shape of the substrate, the structure and shape of an enzyme and the substance upon which the enzyme works all have to match exactly. This enables the substrate to bind, but it can 't do this if the shapes of the two are different. The Aim of Enzyme Catalase Experiment is making a series of experiments involving the enzyme Catalase which has been performed in order to determine some of the enzyme 's properties.

Read More

More about Catechol Oxidase Lab Report

Open Document