Iycee Charles de Gaulle Summary The Effect On Catalase And Lipase Biology Essay

The Effect On Catalase And Lipase Biology Essay

Enzyme is a biological accelerator, which is usage to rush up a chemical reaction by take downing the activation energy barriers. The maps of the enzyme are straight related to its construction, and therefore, denaturation will happen if its form is altered. There are optimum conditions where it supports enzymes in its most active construction, such as the best temperature, pH, and concentration of enzymes and substrates that will bring forth the most reaction rate. These fluctuations of environmental factors are use to carry on experiments to analyze the effects it have on catalase and lipase.Most enzymes are protein, which is a supermolecule with a alone three dimensions configuration that acts as a accelerator.

A accelerator is a chemical agent that speeds up a chemical reaction by take downing the activation energy, the initial energy needed to drive a reaction, barriers without being consume in the procedure. An enzyme can take down the activation energy when catalyzes a reaction by enable the reactant molecules called substrates to absorb adequate energy to make the passage province with minimal thermic aid.Since enzymes are proteins, they are really sensitive to their environmental factors, such as temperature, degree of pH, and concentration of enzyme and substrate in an enzyme-substrate mixture, that may impact the enzymes or its reaction rate.

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This is because of its specific amino acerb sequence that gives each enzyme a certain form, which is the ground that the map of an enzyme is straight related to its construction. The construction of the enzyme allows merely a specific substrate to adhere into its active site, an country where substrates bind to the enzyme, so that the contact action may happen. Its construction is so critical that little alterations in it will do the enzyme to be less efficient and cut downing the reaction rate. Extreme change will do denaturation in an enzyme, where it can no longer map. However, there are optimum conditions where it favors the most active form for each enzyme to work the best under.Each enzyme has a different optimum temperature and optimum pH degree where they work best in that produce the most merchandise molecules by holding the greatest reaction rate due to the figure of molecular hits and transition of reactants. Most enzyme ‘s optimum pH is of the scope 8 and optimum temperatures is about 37.

5A°C because it is the mean internal temperature of a human organic structure. As the temperature rise, the enzyme reaction rate will besides increase until a certain temperature and above that temperature, the reaction rate will diminish. This is due to heat doing molecules move quickly and do the substrates to clash with the active sites more frequently to change over reactants to merchandises. However, excessively much heat will do the bonds in the enzyme to interrupt and change its form, which will do the enzyme to be denatured.

The same thought is apply to the pH degrees ; if a solution that is intensely acidic or basic will do the bond in enzyme to interrupt, change its form, and go denaturized ( Campbell et al. , 2008 ) .Concentration of enzyme and substrates besides affect the reaction rate but it does non impact the construction of the enzyme.

If the substrate concentration is changeless, so the reaction rate is besides changeless. But if the substrate concentrations addition, so the reaction rate will increase until it reaches a point where the enzymes are saturated, intending the enzymes are all presently working on substrates and it is limited by the figure of enzymes. Besides, when the substrates are changeless and the enzymes concentration additions, so the reaction rate will besides increase.In this experiment, the existent experiment analysing catalase and the simulation experiment analysing lipase will be usage to measure the consequence given by fluctuation in environmental factors. Catalase is enzymes that convert the harmful by-product of metamorphosis, H peroxide, into O and H2O and is found in all life cells. The enzyme catalase binds to the substrate, H peroxide, and catalyst the chemical reaction to bring forth H2O and O. Whereas, lipase is enzymes that breaks down lipoids or other fats into absorbable signifier and is found in the pancreas or the little bowel.

The enzyme lipase binds to its substrate, fats, and catalyzes the reaction to divide it into glycerin and fatty acids. Catalase is predicts to work best in the temperature of 37.5A°C, under the pH of 8, and when the the enzyme concentration and substrate concentration is high. While, lipase is predicts to work best in the temperature of 37.5A°C, under the pH of 5, and when the substrate concentration is high.

Methods:For this experiment over enzymes, we used catalase, which were extracted from a yeast solution, to show how the enzyme-catalyzed reactions rates were affected by different enzyme concentrations, substrate concentrations, temperatures, and pH. The rate of chemical reaction was measured by the force per unit area of O that was produced.To accurately mensurate the addition of force per unit area of O2, we connected the completed agreement of Vernier Gas Pressure Sensor to the Vernier LabPro interface, which was so connected to the laptop that carried the Logger Pro computing machine package plan. From the Logger Pro plan, we opened the file “ 06B Enzyme ( Pressure ) ” from the Biology with Computer booklet. Once all of the equipment was setup and running, we obtained a clean, big trial tubing and collected the enzyme. The enzyme was placed at the underside of the trial tubing and the trial tubing was dried. The stopper valve was in a closed place before the gum elastic stopper was inserted and tightly secured onto the trial tubing.

We so drew the diluted H2O2 into a syringe and connected it to the gum elastic stopper assembly. Following, we open the valve of the setup to shoot the peroxide solution, which was instantly closed and the cod button was clicked on the Logger Pro plan. Throughout this 3 minute informations aggregation procedure, we made certain that the gum elastic stopper was still integral to guarantee accurate informations reading. Once it had ended, we clicked store latest tally in the Logger Pro package.

Then, we removed the gum elastic stopper assembly, discarded the contents of the trial tubing, and cleaned and dried the trial tubing and the gum elastic stopper. When the informations collected for the set of experiment had finished, we clicked on the graph where it began to increase and dragged it over to where the graph expression non-linear, so clicked the Linear Fit icon one time the wanted country was highlighted, and recorded the equation of the line and its incline to find the rate of the reaction into the informations tabular array. We used these same procedures for the general processs for all sets of the experiments.To prove the consequence of enzyme concentration, we used 15 millilitres of H2O and 15 millilitres of 3 % H2O2 in this experiment. We obtained one bead of enzyme solution at the underside of the clean, big trial tubing, as stated in the general processs. Then we drew up six millilitres of the substrate solution and continued to follow the general processs to get the rate of reaction.

The remainder of experiments on enzyme concentration used the same methods as stated but merely changed from one bead of enzyme to two, three, four, and so five beads of enzyme solution. We so recorded the information for this set of experiments in table one.Then to prove the consequence of substrate concentration, we used one millilitre of H2O and five millilitres of 3 % H2O2 in this experiment. Three beads of enzyme solution are obtained and placed at the underside of the trial tubing. We so drew up six millilitres of the substrate solution and continued to follow the general processs to get the rate of reaction. The same methods are applied for the remainder of the experiments on substrate concentration, except that the one millilitre of H2O with five millilitres of 3 % H2O2 are to be replaced by two, three, four, and five millilitres of H2O with four, three, two, and one millilitre of 3 % H2O2, severally, for each experiment. We so recorded the information for this set of experiments in table two.Furthermore, to prove the consequence of temperature on the enzyme reaction rate, we used three millilitres of H2O and three millilitres of 3 % H2O2.

We drew up the solutions into the syringe and placed it in ice H2O for three proceedingss ; the temperature of ice was so recorded merely in this experiment. Then we placed the trial tubing that contained three beads of enzyme solution into the Erlenmeyer flask that was half filled with ice H2O, where it was chilled for three proceedingss. When the syringe was done acclimated for three proceedingss in ice H2O, it was removed and connected to the gum elastic stopper and we continued to follow the general processs to get the rate of reaction. For the remainder of the set of experiments on temperature, we repeated the same methods except the ice H2O are replaced by room temperature, 30A°C H2O bath, 40A°C H2O bath, 50A°C H2O bath, and 60A°C H2O bath with each experiment. We so recorded the information for this set of experiments in table three.Finally, to prove the consequence of pH on the enzyme reaction rate, we used three millilitres of the pH 3 solution and three millilitres of 3 % H2O2. We so obtained three beads of enzyme and placed it at the underside of the trial tubing, such as stated in the general processs, drew up the solutions into the syringe, and continued to follow the general processs to get the rate of reaction. The same methods were used to transport out the remainder of the set of experiments on pH, except the pH 3 solutions was substituted by the solutions of pH 5, pH 7, pH 9, and pH 11.

We so recorded the information for this set of experiments in table four.Consequences:Figure 1. Consequences of the existent experiment on the consequence of substrate concentration on the reaction rate of the enzyme catalase, utilizing computing machine package Logger Pro to measure on a three proceedingss interval per test. As the substrate addition in the solutions, the reaction rate of catalase lessenings.Figure 2.

Consequences on the consequence of substrate concentration in the simulation of the enzyme lipase, utilizing the plan “ Enzyme Investigation. ” The effects are based on the changeless variables of temperature at 37.5A° C, pH of 9, and the enzyme concentration of 1 ten 10-6 moles per litre.Figure 3.

Consequences of the existent experiment on the consequence of temperature on the reaction rate of the enzyme catalase, utilizing the computing machine package Logger Pro and measure each experiment on a three proceedingss interval. The effects are base on the changeless variables of 0.5 milliliter of substrate concentration and 3 beads of enzyme solutions. As indicate, catalase ‘s optimum temperature is 30A° C.Figure 4. Consequences on the consequence of temperature on the rate of reaction in the simulation of the enzyme lipase, utilizing the plan Enzyme Investigation.

The reaction rates of lipase changing from different temperature are based on the changeless variables of pH of 9, substrate concentration of 0.01 moles per litre, and the enzyme concentration of 1 ten 10-6 moles per litre. As indicate, lipase ‘s optimum temperature is between 37-38A° C.Figure 5. Consequences of the existent experiment on the consequence of pH on the reaction rate of the enzyme catalase, utilizing the computing machine package Logger Pro and measure each experiment on a three proceedingss interval. The reaction rate of catalase changing from pH degree of 3 to 11 are based on the changeless variables of 3mL of 3 % H2O2 and 3 beads of enzyme concentrations.Figure 6.

Consequences on the consequence of pH on the rate of reaction in the simulation of the enzyme lipase, utilizing the plan “ Enzyme Investigation. “ The reaction rate of lipase changing from pH degree of 1 to 14 are based on the changeless variables of temperature at 38A° C, substrate concentration of 0.01 moles per litre, and the enzyme concentration of 1 ten 10-6 moles per litre.Figure 7. Consequences of the existent experiment on the consequence of enzyme concentration on the reaction rate of the enzyme catalase, utilizing the computing machine package Logger Pro and measure each test on a three proceedingss interval. As indicate, the more beads of enzymes is provide into the solutions of 15 milliliter of H2O and 15 milliliter of 3 % H2O2, the reaction rate additions.Discussion:As discussed in the Introduction, the optimum conditions for most enzymes are in the environment of around human organic structure temperature, which is 37.

5A° C, and with the pH degree of around 8 because enzymes work best in a somewhat basic solution. Besides, additions in enzyme concentration should ever increase the rates of reaction ; this is verified through the existent experiment of catalase, which is illustrated in figure 7. While additions in substrate concentration will besides give a rise to the rate of reactions, it will bit by bit come to a point where it reaches the impregnation point and “ any farther addition in substrate concentration produces no important alteration in reaction rate, ” which is demonstrate in figure 2 ( Royal Science of Chemistry ) .In old anticipations, the enzymes catalase and lipase are both thought to hold optimum temperatures around 37.5A° C.

The optimum pH of catalse is 8, while lipase is 7. Figure 4 suggests that the anticipation for lipase optimum temperature is right. The rates of reaction for the enzyme lipase continue to increase as the temperature rise until it reach its highest at 37.5A° C, so the reaction rate Begin to drop after 38A° C until it come to a halt at 60A° C. This is due to the increasing temperature, increases enzyme reaction rate up until the point where the enzymes is denatured when the temperature continues to lift above its optimum temperature, as explained in the debut. For catalase nevertheless, the anticipations prove false for the figure 3 suggests that the optimum temperature for catalase is 30A° C and non at 37.

5A° C. The reaction rate begins to drop after 30A° C, due to denaturalization of enzyme.On the other manus, the anticipations for the optimum pH conditions of both catalase and lipase prove false. In figure 5, it suggests that the optimum pH conditions of catalase are at 11, non 8, and is continue to lift as the solution is going more basic. The information suggests that catalase works best in a really basic solution and non merely somewhat basic as predicted, but it does demo that the reaction rate is diminishing as the solution gets acidic. As predicted, catalase does non work good in acidic solution and as it gets excessively acidic, catalase will get down to be denatured ( Vasquez et al, 2008 ) . Figure 6 suggests that the optimum pH degree for lipase is at 9, and non 7.

As the solution continue to be more acidic or basic, the reaction rate get down to decelerate and decreases until it comes to a halt when lipase is wholly denaturized and stop operation.The anticipation that the addition in substrate concentration will besides increase in the reaction rate of catalase is indicate by figure 1 as false. Figure 1 show that the reaction rate lessenings as the substrate concentration additions. This may be due to the enzymes had already make the concentrated point.

Figure 2, nevertheless, verify that the anticipations of addition in substrate concentration besides increase the reaction rate for lipase.