Enzymatic Reaction Lab

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

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.

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.

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.

For example, between pH 5 and 7, there is an almost 500 mL difference, even though they are only 2.0 away on the pH scale. This shows even small changes in pH can have a large difference in the rate of reaction. Evaluation of Conclusion: The data and conclusion does match with previous background research. Background research suggests that reaction rate increases with pH until a point where optimum pH is reached, after which the enzyme is denatured and no longer can perform its function. This research was also shown in the data, even though the point at which the enzyme denatured was not

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.

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

1.1 Abstract The purpose of quantitative analysis of protein using a spectrophotometer is to measure the concentration of proteins in a given sample. The experiment is conducted by laboratory method (Biuret Test) and using spectrophotometer to analyze the absorbance of reactants at 540 nm, hence determining the concentration of the proteins in a given sample. The purpose of stopped enzyme assay to study B-galactosidase is to determine the effect of temperature and concentrations of substrate on enzyme activity.

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).

Introduction In class, a series of experiments were performed that pertained to the enzyme known as catalase, which converts hydrogen peroxide into oxygen. Due to peroxide being toxic to the tissues of both plants and animals, both possess the enzyme catalase, which breaks into two non-toxic compounds: water and oxygen gas. Enzymes are proteins that react to certain substrates to create a product, and continue doing so afterwards. Methods and Materials To test reactions between catalase and hydrogen peroxide, groups of three to four people were formed.

Uncontrolled Environmental conditions Atmospheric conditions The controlled variable Concentration of amylase was kept under control by measuring the amount of amylase used and also it was made sure the percentage of amylase used was 1%. The Amount of amylase/starch used were kept to 5cm3 at all times. Materials needed Beakers Bunsen burner Test tube Thermometer Stopwatch Test plate Glass rod Starch Amylase solution Water bath Iodine solution. Test tube holder Labels Marker Procedure First 5 test tubes were taken and labeled with numbers from 1 to

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.

⋅ 5H2O, which has about 36.0%, and CuCl2 ⋅5H20 (21.17%). Materials: Ring stand, ring clamp, evaporating dish, Bunsen burner, clay triangle, crucible tongs, electronic balance, sample of hydrated salt. Methods:

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.

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.