The purpose of this lab was to observe and understand the effects of changes in temperature‚ pH‚ enzyme concentration‚ and substrate concentration on the reaction rate of an enzyme-catalyzed reaction. Another purpose of the lab was to explain how environmental factors affect the rate of enzyme-catalyzed reactions. Hypothesis: I believe that if there is an increase in enzyme concentration‚ an increase in temperature‚ or an increase in pH‚ then the intensity of the reaction will increase‚ which
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energy must be exceeded first. Enzymes are described as the lock and key complex. They have an active site which is specific to a binding site on a substrate molecule. When this happens the substrate changes shape therefore the product is formed. ‘The enzyme-catalyzed reaction is as follows: E + S=ES=EP=E + P where E is enzyme‚ S is substrate and P is product.’[2] Factors that affect enzyme activity are: 1. Temperature- at low temperatures the rate of reaction is low this is due to the
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different temperature conditions‚ we can record the rate of reaction by taking a sample out and test it with iodine solution to see if there is any remaining starch present. We have to use the enzyme amylase because enzymes will only work on a specific substrate i.e. amylase will work on starch because of its special shape of active site. This is known as the enzymes specificity’. The enzyme amylase is used for hydrolysing starch and glycogen to form glucose and maltose. This enzyme is found in human saliva
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enzyme used in this experiment was the β-galactosidase purified from E. coli. This enzyme hydrolyzes lactose and turns it into galactose and glucose. Since it is difficult to assay the activity of β-galactosidase‚ we will be using the artificial substrate‚ o-nitrophenyl-β-galactoside (ONPG) instead of lactose. ONPG is an analog of lactose and an advantage of using ONPG is that it is easy to determine the amount of ONPG cleaved by using spectrometric assay (1). The β-galactosidase hydrolyzes ONPG
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rate of a chemical reaction. In this study‚ we performed two different experiments that investigated the effect of varying substrate concentration‚ and the effect of temperature on the rate of Enzyme-Catalase reaction. In experiment one (i.e. the effect of varying substrate concentration on the rate of enzyme-catalase reaction) we tested the hypothesis HA as substrate concentration increases‚ so will reaction rate until all active sites are bound. In experiment two (i.e. The effect of temperature on
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inhibition the inhibitor increases during the same period. There are two types of reversible inhibition namely competitive and non-competitive inhibition. A competitive inhibitor binds to the active site of the enzyme and thus competes with the substrate for the active site. They are able to do this because they have a similar structure to that of the enzyme. Once the enzyme is bound to the enzyme know further reaction can take place until it dissociates from the molecule hence it is often termed
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enzyme 2. When an enzyme catalyzes a reaction: A a. Substrate(s) bind in the active site b. Products bind in the active site c. The shape of the enzyme remains unchanged d. The enzyme is consumed by the reaction 3. Which of the following would interfere most with the ability of an enzyme to catalyze a reaction? A a. Reduced concentration of substrate available b. Reduced concentration of product available c. Increased concentration of substrate available d. A change in the pH 4. Feedback mechanisms
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of Catalase Concentration 1. Obtain four 50ml beakers 2. Llabel beakers 100‚ 75‚ 50‚ and 0 units/ per ml 3. Prepare 40ml of enzme for each of the concentrations 40ml of original enzyme + 0ml cold distilled water =100units/ml 30ml of original enzyme + 10ml cold distilled water=75units/ml 20ml of original enzyme + 20ml cold distilled water=50units/ml 0ml of original enzyme + 40ml cold distilled water=0units/ml 4. Save undiluted enzyme for parts C-E 5. Place concentrations in ice bath 6
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peroxide into water and oxygen gas. Enzyme activity is affected by many factors such as temperature‚ pH‚ concentration of enzyme and substrate‚ and lastly is the presence of inhibitor. Inhibitors act to slow down or even stop the action of the enzymes. Inhibitors are generally categorized as competitive and non-competitive. Competitive inhibitors bind to the active site of the enzyme rendering the substrate unable to bind to the enzyme and hindering the reaction to take place. Non-competitive inhibitors
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of breaking bonds within the monomers of substrate‚ the molecule upon which the enzyme is acting. When the substrate and the enzyme bind‚ the substrate-enzyme complex is formed. The substrate binds to the enzyme’s active site‚ which is the part of the protein in which the enzyme fits. Scientists have introduced multiple models that attempt to illustrate exactly how the enzyme and substrate fit together (See figure 1). In the lock and key model‚ the substrate and enzyme fit together perfectly. In the
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