PK – Lab Report Name: ____________________ Section: ___________________ Experimental Errors and Uncertainty Data: The data table that follows shows data taken in a free-fall experiment. Measurements were made of the distance of fall (Y) at each of the four precisely measured times. Time‚ t (s)|Dist‚ y1 (m)|Dist‚ y2 (m)|Dist‚ y3 (m)|Dist‚ y4 (m)|Dist‚ y5 (m)||σ|t2| 0|0|0|0|0|0|0|0|0| 0.5|1.0|1.4|1.1|1.4|1.5|1.3|.2|.25| 0.75|2.6|3.2|2.8|2.5|3.1|2.8|.3|.56| 1.0|4.8|4
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Abstract The purpose of this lab was to test if ethanol affects the reaction involving hydrogen peroxide and catalase. Tests were performed by putting chicken liver‚ ethanol solution (diluted ethanol solution for other trials) and hydrogen peroxide in a test tube with a side arm‚ and having a rubber tube lead the oxygen gas into a gas collection tube. Results from the tests showed a negative correlation‚ this means that the more diluted the solution of 95% ethanol was‚ the less oxygen gas collected
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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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we studied enzyme catalase‚ which accelerates the breakdown of hydrogen peroxide into water and oxygen. The purpose was to isolate catalase and measure the rate of activity under different conditions. The laboratory was also conducted in association with a second laboratory that measured the effects of an inhibitor on the enzymes. Changes in temperature and pH along with Substrate Concentration and Enzyme Concentration were the conditions tested in the experiment. Each lab was assigned to a
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Effects of Enzyme Catalysis of H2O2 by Catalase Report by: Timmy Lin (#269164729) October 17‚ 2011 Mr. Rienzi AP Biology Problem: Measuring the effects of Catalase enzymes on hydrogen peroxide decomposition. Measuring the rate of the reaction when hydrogen peroxide and Catalase are mixed at the same ratio for different time (10‚ 20 30 60 120 180 360 seconds). Background: Enzymes are biological catalysts that carry out cellular metabolic processes with the ability to enhance the rate
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Assessment of Catalase Function Lab Introduction The purpose of this lab report was to test and measure the rate of substrate destruction by an enzyme‚ we tested the destruction of hydrogen peroxide by the enzyme catalase. Hydrogen peroxide is a poisonous by product of metabolism that can damage cells if it is not removed. Catalase is an enzyme that speeds up the breakdown of hydrogen peroxide into water and oxygen gas. H2O2 + catalase → H2O + O2 A catalyst is a substance that lowers the
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Purpose Understanding how catalase activity is affected by pH is the purpose of this experiment. Introduction Enzymes play an important role in daily life because of the chemical reactions. Almost chemical reactions require the presence of enzymes to promote the metabolic process. They are known as the incredibly efficient and highly specific biological catalysts. Most enzymes are protein with the ability to enhance the rate of reaction between molecules. To catalyze a reaction‚ the enzymes
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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 my hypothesis: At pH buffer 7 the enzyme (catalase) will work most efficiently
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From the graphs‚ it is evident that an increase in both catalase concentration and substrate concentration resulted in a higher rate of reaction or‚ as observed in the kPa graphs‚ a higher volume of O2(g) formed at the end of the 5 minute trial. Interestingly‚ it should also be noted‚ as it was mentioned in the Figure 2‚ that the trend for the 6mL of 3% H2O2(aq) was more of a linear trend than an exponential decay‚ steadily rising until the end of the 5 minute trial. From this‚ it can be inferred
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trend O2 production and reaction velocity increased with increasing catalase concentration‚ however‚ the 33% percent catalase concentration showed a drop of 0.175 mL O2/s compared to the 25% catalase concentration (figure 1.2). The velocity of 25% catalase was 0.275 mL/s‚ 33% was 0.1 mL/s‚ 50% was 0.435 mL/s‚ and 75% catalase was 0.575 mL/s (figure 1.1). The 50% catalase concentration produced the most O2 overall however the 75% catalase concentration had the fastest initial reaction velocity. Experiment
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