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Enzymes are proteins that increase the rate of chemical reaction by lowering their activation energy. The enzyme glucose oxidase is one of the most widely used enzyme as an analytical reagent due to its ability to identify the presence of glucose, its low cost and good stability. This report discusses the role of enzymes concentration in biological reactions and the catalytic activity of glucose oxidase on D-Glucose. The activity was studied by spectrophotometry and the results were first tabulated and then plotted. The results of this experiment indicate that the enzyme concentration has no major affect on the rate of
Data from Table 1. confirms the theory that as the concentration of glucose increases so will the absorbance of the solution when examined with the glucose oxidase/horseradish peroxidase assay. Glucose within the context of this assay is determined by the amount of ferricyanide, determined by absornace, which is produced in a one to one ratio.1 Furthermore when examining the glucose standards, a linear calibration curve was able to be produced (shown as Figure 1). Noted the R2 value of the y = 1.808x - 0.0125 trend line is 0.9958, which is statistically considered linear. From this calibration curve the absorbance values of unknowns samples can be compared, and the correlated glucose concentration can then be approximated.
We then took 1ml of the 1% solution from test tube 1 using the glucose pipette and added it to test tube 2, we then used the H2O pipette and added 9ml of H2O into test tube 2 creating 10ml of 0.1% solution
Living organisms undergo chemical reactions with the help of unique proteins known as enzymes. Enzymes significantly assist in these processes by accelerating the rate of reaction in order to maintain life in the organism. Without enzymes, an organism would not be able to survive as long, because its chemical reactions would be too slow to prolong life. The properties and functions of enzymes during chemical reactions can help analyze the activity of the specific enzyme catalase, which can be found in bovine liver and yeast. Our hypothesis regarding enzyme activity is that the aspects of biology and environmental factors contribute to the different enzyme activities between bovine liver and yeast.
Catalase is a common enzyme that is produced in all living organisms. All living organisms are made up of cells and within the cells, enzymes function to increase the rate of chemical reactions. Enzymes function to create the same reactions using a lower amount of energy. The reactions of catalase play an important role to life, for example, it breaks down hydrogen peroxide into oxygen and water. Our group developed an experiment to test the rate of reaction of catalase in whole carrots and pinto beans with various concentrations of hydrogen peroxide. Almost all enzymes are proteins and proteins are made up of amino acids. The areas within an enzyme speed up the chemical reactions which are known as the active sites, and are also where the
The affects of pH, temperature, and salt concentration on the enzyme lactase were all expected to have an effect on enzymatic activity, compared to an untreated 25oC control. The reactions incubated at 37oC were hypothesized to increase the enzymatic activity, because it is normal human body temperature. This hypothesis was supported by the results. The reaction incubated to 60oC was expected to decrease the enzymatic activity, because it is much higher than normal body temperature, however this hypothesis was not supported. When incubated to 0oC, the reaction rate was hypothesized to decrease, and according to the results the hypothesis was supported. Both in low and high pH, the reaction rate was hypothesized to decrease, which was also supported by the results. Lastly, the reaction rate was hypothesized to decrease in a higher salt concentration, which was also supported by the results.
One of the most primitive actions known is the consumption of lactose, (milk), from the mother after birth. Mammals have an innate predisposition towards this consumption, as it is their main source of energy. Most mammals lose the ability to digest lactose shortly after their birth. The ability to digest lactose is determined by the presence of an enzyme called lactase, which is found in the lining of the small intestine. An enzyme is a small molecule or group of molecules that act as a catalyst (catalyst being defined as a molecule that binds to the original reactant and lowers the amount of energy needed to break apart the original molecule to obtain energy) in breaking apart the lactose molecule. In mammals, the lactase enzyme is present
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
The Effect of Temperature on the Activity of the Enzyme Catalase Introduction: The catalase is added to hydrogen peroxide (H²0²), a vigorous reaction occurs and oxygen gas is evolved. This experiment investigates the effect of temperature on the rate at which the enzyme works by measuring the amount of oxygen evolved over a period of time. The experiment was carried out varying the temperature and recording the results. It was then repeated but we removed the catalase (potato) and added Lead Nitrate in its place, we again tested this experiment at two different temperatures and recorded the results. Once all the experiments were calculated, comparisons against two other groups were recorded.
Enzymes react differently under different conditions and concentrations, being the most productive at the enzymes specific optimum condition and concentration. The enzyme sucrase, extracted from yeast, breaks down the complex sugar sucrose into the simple sugar glucose. Testing for sucrase’s optimum environment, multiple reactions were ran using varying amounts and concentrations of sucrose and sucrase at different pHs and temperatures. The product was then treated with Benedicts solution to visually observe what amount of glucose was present after the reaction was ran; negative results being little to no glucose present and positive results being glucose present. The varying levels of colors created by the Benedicts test were recorded as 1 (negative) blue; 2 green; 3 yellow; 4 (positive) orange; and 5 (positive) red. After running the reactions to determine the optimum temperature and pH, 37 degrees Celsius was determined to be the optimum temperature while pH 2.0 was determined to be the optimum pH. This means that under these conditions the enzyme will help produce the most product from the substrate. After finding the optimum conditions the two different concentrations of sucrose were ran for ten minuets taking an initial sample and then subsequent samples every minuet, under those conditions, one concentration at 2.5% sucrose and again at 10% sucrose. The 10% sucrose had the most positive results because there were sufficient active sites to bind with most of the sucrose present producing glucose more efficiently than the 2.5% sucrose. As with the 2.5% sucrose all of the sucrose was bond to the active sites of sucrase and there were ...
Investigating the Effect of Substrate Concentration on Catalase Reaction. Planning -Aim : The aim of the experiment is to examine how the concentration of the substrate (Hydrogen Peroxide, H2O2) affects the rate of reaction. the enzyme (catalase).
Investigating Factors that Affect the Rate of Catalase Action Investigation into the factors which affect the rate of catalase action. Planning Aim: To investigate the affect of concentration of the enzyme catalase on the decomposition reaction of hydrogen peroxide. The enzyme: Catalase is an enzyme found within the cells of many different plants and animals. In this case, it is found in celery.
At the time of conducting the experiment, the intention was to analyse the effect that an increase in catalase concentration had on the amount of oxygen (O2) produced if the hydrogen peroxide (H2O2) concentration was constant. It was proposed that when the catalase increases in concentration at the increments of 0.5%, 1%, 2%, and 4% and the hydrogen peroxide remained at a fixed concentration, the oxygen production would rise gradually. It was suggested that this would occur due to the collision theory ("BBC - GCSE Bitesize: Collision Theory") and the greater number of active sites thus an increase in accessibility allowing enzyme- substrate complex’s to be formed. According to the data gathered from the experiment, it can be implied that the hypothesis was supported as the data indicates an incline in oxygen
Introduction / Background Information. This is an experiment to examine how the concentration of the substrate Hydrogen Peroxide (H2O2) affects the rate of reaction of the enzyme Catalase. In this experiment I will be using yeast as a source of catalase. Enzymes are catalysts which speed up specific reactions. Enzymes such as catalase are protein molecules, which speed up a specific reaction within the cell.
The results of this experiment showed a specific pattern. As the temperature increased, the absorbance recorded by the spectrophotometer increased indicating that the activity of peroxidase enzyme has increased.At 4C the absorbance was low indicating a low peroxidase activity or reaction rate. At 23C the absorbance increased indicating an increase in peroxidase activity. At 32C the absorbance reached its maximum indicating that peroxidase activity reached its highest value and so 32 C could be considered as the optimum temperature of peroxidase enzyme. Yet as the temperature increased up to 60C, the absorbance decreased greatly indicating that peroxidase activity has decreased. This happened because at low temperature such as 4 C the kinetic energy of both enzyme and substrate molecules was low so they moved very slowly, collided less frequently and formed less enzyme-substrate complexes and so little or no products. Yet, at 23 C, as the temperature increased, enzyme and substrate molecules
In order to perform their vital functions, our cells require a continual input of energy. Aerobic cellular respiration is the process in which our cells, in the presence of oxygen, break down glucose and turn it into usable high-energy ATP molecules. It is a highly complex process that involves many individual processes and it takes place predominantly in the mitochondria.