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    Stallings Period 2 January 26‚ 2013 Enzyme Catalysis Lab Report Background: Enzymes are catalyst‚ which affect the rate of a chemical reaction. One consequence includes the cell to carry out complex chemical activities at relatively low temperatures. In these reactions the substrate binds reversibly to the active site. The cause of this is a decrease in the energy needed to activate the reaction of the substrate molecule to from products. Every enzyme is particular for a reaction for the reason

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    Catalase Lab

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    Purpose The purpose of this catalase lab is to design simple experiments to demonstrate how various factors affect the rate of enzyme activity. This lab shows how the enzyme decomposes in hydrogen peroxide. Methods and Materials Refer to handout attached to the back of lab Observations Table 1: The mL of oxygen produced with increase of catalase 30secs 60secs 90secs 120secs 150secs 180secs Disks: 2 17ml 16ml 21ml 26ml 31ml 35ml Disks: 4 8ml 19ml 27ml 35ml 44ml 53ml

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    Matthew Saldanha Bio DCP lab-Catalase experiment Aim: To investigate enzyme kinetics‚ using different concentration of the enzyme. Hypothesis: The assay system used in the lab consists of a filter paper disc coated with the enzyme and the dropped into a papercup of substrate (Hydrogen Peroxide). As the hydrogen breaks down the hydrogen peroxide into hydrogen and oxygen gas‚ the bubbles of oxygen gas collect underneath the filter and make it

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    Liver Enzyme Lab Report

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    LAB 1: What temperature does the enzyme actually work properly in? (Hypothesis) If the temperature is below 40 but above 20‚ then the liver will show bubbles. If the temperature is raised higher than the optimum temperature‚ then an extreme decline in enzyme activity would occur following by the quick denaturing of the enzyme‚ rendering it is permanently useless. Also about 37°C is body temperature. The liver that was at 25°C had a huge amount of bubbles (a 4 on the scale) and the 0°C

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    Catalase Lab

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    From performing the pH experiment it has proven that pH buffer 7 is the optimum pH for catalase in potatoes. This is because the height of the bubbles was the highest of all three tests (pH 3‚ pH 7‚ pH 9) reaching an average height of 0.433 cm. See graph 3. While pH buffer 3’s average height was 0.233 cm only reaching a maximum height of 0.3 cm in Trial 3 and pH buffer 9’s average height being 0.333 cm only reaching a maximum height of 0.4 cm again in Trial 3. See table 1. Therefore this supports

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    Catalase Test Lab Report

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    sample of the agar plate and the slide was viewed under the microscope. Once‚ the microscopic visual was captured‚ a catalase test followed. Next‚ for further data‚ MSA results were recorded‚ along with antibiotic observations of demo plates. Lastly‚ with the information gathered‚ it was identified that the unknown sample was Streptococcus salivarius. Introduction: In this lab‚ the exploration of an unknown gram positive bacteria was conducted. What is known about gram positive microorganisms

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    Enzyme Lab Report

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    Investigating the effect of changing substrate concentration on the activity of the enzyme catalase The aim of this experiment is to examine how the concentration of a substrate (hydrogen peroxide) affects the rate of reaction of an enzyme catalyse (found in liver cells) Research Question: how does changing the concentration of the substrate affect the rate of reaction of the enzyme catalyse? Hypothesis: As the concentration of the substrate increases‚ so does the rate of reaction until the reaction

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    Catalase Test Lab Report

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    the shape. The next step according to the result‚ will be a catalase test.

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    Enzyme Lab Report

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    Enzyme action is the simple mechanism by which enzymes catalyse chemical reactions. This begins with the binding of the substrate to the active site on the enzyme. The binding of the substrate to the enzyme causes changes in the distribution of electrons in the chemical bonds of the substrate. This then causes the reactions that lead to the formation of products that are then released from the enzyme surface to regenerate the enzyme for another reaction cycle. The active site has a unique shape that

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    Potato Catalase Lab Report

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    potato catalase for exactly 5 seconds. It was next dried on a paper towel for 5 seconds‚ and finally placed at the bottom of the first beaker‚ which contained hydrogen peroxide solution. The timer was then started. The timer stopped when the paper disk floated up to the top of the beaker. This was performed 3 times. After this‚ two negative controls were tested. The first negative control used a denatured catalase instead of the potato extract. The

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