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Enzymatic Reaction Lab

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The purpose of this experiment was to analyze the effects of the variables: temperature, pH, and enzyme concentration, on the enzymatic reaction rate of catalase and the level at which its products are released, measuring the rate of absorption using the indicator solution guaiacol and a spectrophotometer to develop a hypothesis of the ideal conditions for these reactions. My hypothesis is that the extremes in concentration, temperature and pH will negatively affect the Au rate. This experiment used 11 solutions contained in cuvettes. Each cuvette, once mixed, is placed in spectrophotometer and then a reading taken every 20 seconds. Cuvettes 1, 8, and 10 are used as blanks to zero out the spectrophotometer. They all lack the enzyme to help determine the absorption of just the enzyme. …show more content…

Cuvette 8 contains hydrochloric acid solution and is used as the zero for cuvette 9. Cuvette 10 contains Sodium hydroxide solution and acts as the zero for cuvette 11.Cuvette 2 is used as the control in each variable test. Cuvettes 2, 3, and 4 tested the variable of enzyme concentration. They were all kept at 23 degrees Celsius and a pH of 7. Cuvette 2 contained 1 mL of catalase, resulting in an absorption rate of .001 Au. Cuvette 3 contained 2 mL of catalase .producing an Au rate of .0012. Cuvette 4 held 4 mL pf catalase and had an Au rate of .0023. The visible pattern is that as the amounts of enzymes increase the absorption rate will also increase. Cuvettes 5, 6, and 7 test the variable of temperature. Cuvette 5 was put into a freezer at 0 degrees Celsius. The resulting Au rate was .0004. Cuvette 6 was placed in a bath of warm water at 35 degrees Celsius, reaching an Au rate of .001. Cuvette 7 had am Au rate of .00001, and was kept at 85 degrees Celsius. The suggested pattern is that the extremes reduce the Au

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The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.

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Dependent Variable amount of product (glucose and fructose) produced 2. Independent Variable temperature 3. Controlled Variables pH, amount of substrate (sucrose) present, sucrase + sucrose incubation time Effect of Substrate Concentration on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2.

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The Melibiose (MEL), Arabinose ARA, nitrate reduction, and catalase tests were all positive, and the oxidase test was

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55 degrees celcius Table 6: Effect of Sucrose Concentration on Sucrase Activity Optical Density 35 g/L 30 g/L 25 g/L 20 g/L 15 g/L 10 g/L 5 g/L 0 g/L 1 1.007 0.974 0.950 0.926 0.849 0.734 0.515 0.003 2 1.002 1.011 0.947 0.937 0.834 0.766 0.496 0.002 3 0.980 0.998 0.944 0.932 0.838 0.754 0.495 0.001 average 0.996 0.994 0.947 0.932 0.840 0.751 0.502 0.002 Effect of Sucrose Concentration on Sucrase Activity 5. State how sucrase activity changes with increasing sucrose concentration. First sucrase activity increases greatly. After 10 g/l sucrase activity continues to increase but at a slow rate until it reaches 30 g/l. At 30 g/l to 35 g/l sucrase activities mostly stayed the same

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1764 Words | 8 Pages

Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.

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(NH4)2CO3 was added to the solution. Then the tube was placed into warm water. Once the tube was cooled, the tube was centrifuged and 0.5 mL of 6M acetic acid was added to the precipitate. This was done to see if the precipitate turned cloudy. The solution was clear and not cloudy.

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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.

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Practical Activity Outline: Predicting the Effect of pH on the Activity of Amylase Arlecia Johnson Enzyme to use: Amylase is the easiest enzyme to find, it is in your saliva! Source: Saliva Animal: Human being The substrate: Starch, because amylases action starch and starch is also very easy to find in carbohydrate foods. Method and type of treatment A. Position a drop of solutions of iodine in test tubes (each with one drop) and place them in a row, in a test-tube rack.

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3mL of the liquid in each of the vials were added into cuvettes and measured in the spectrophotometer. Before each time point the photo spectrometer was zeroed using a cuvette with 3mL of distilled water. If any of the results were considered unusual the machine was zeroed again and the sample was retested. The results from the spectrophotometer test were recorded in a table. The experiment was repeated six times to gain a sample size of six.

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These factors include the pH and the temperature of the solution (1). Most enzymes have a preferred temperature and pH range (2). The preferred temperature for catalase falls between the ranges of thirty five to fifty degrees Celsius (4). Temperatures that are too high denature the enzyme and halt the enzyme’s activity (2). Catalase denatures starts to denature at fifty five degrees Celsius (2).

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In this experiment students were able to see enzyme activity and learn about how the bacterial amylase and the fungi amylase react at different temperatures when mixed with starch. We were able to see when the enzyme is catalyzing using iodine. As stated in the Results, the only temperature tested which showed a lighter coloration was 55 degrees. The lighter coloration is due to enzyme activity, which means that starch was being catalyzed by amylase and turned into maltose. Maltose gives the light coloration in the mixtures, which is the reason why at lower temperatures the colors of the spots were dark brown, and as time passed by they became slightly lighter.

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Along with being found in plants, they are also present in liver cells, kidney cells, leukocytes and erythrocytes. For the concentration of enzyme experiment, the hypothesis was if the concentration of an enzyme increases, then the enzyme activity will increase as well. The hypothesis was proven to be true, because there are more enzymes to react with substrates. For the enzyme—factors affecting, the hypothesis concluded was if the temperature increases, than the enzyme activity will increase. This however was proven wrong, because enzymes become unstable at higher temperatures.

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603 Words | 3 Pages

Introduction: In this lab, of water in a hydrate, or a substance whose crystalline structure is bound to water molecules by weak bonds, is determined by heating up a small sample of it. By heating, the water of hydration, or bound water, is removed, leaving only what is called an anhydrous compound. Based on the percent water in the hydrate, it can be classified as one of three types: BaCl2O ⋅ 2H20, with a percent water of about 14.57%, CuSO4

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INTRODUCTION: Arginase is an enzyme- enzymes are biological catalyst which drives a reaction at the speed of life. Arginase is a hydrolase, hydrolases catalyze hydrolysis reactions, this is determined via the E.C number (Nelson and Cox 2008). Arginase has the EC number is 3.5.3.1 (Schomburg 2015). The enzyme ‘commission number’ is the arithmetical classification that is used for enzymes which indicates the chemical reaction they catalyze.

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