Investigating the effect of changing substrate concentration on the activity of the enzyme catalase The aim of this experiment is to examine how the concentration of a substrate (hydrogen peroxide) affects the rate of reaction of an enzyme catalyse (found in liver cells) Research Question: how does changing the concentration of the substrate affect the rate of reaction of the enzyme catalyse? Hypothesis: As the concentration of the substrate increases‚ so does the rate of reaction until the reaction
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however‚ without enzymes‚ these reactions could possibly take several years to complete. An enzyme is a macromolecule‚ generally a protein‚ that lowers the activation energy of a reaction without being changed by the reaction‚ and this causes the reaction to occur much faster than usual (Campbell et al.‚ 2014). The act of speeding of a chemical reaction is called catalysis‚ and molecules that perform this are called catalyst. Enzymes act as catalysts‚ and there a many types of enzymes that perform many
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purpose of this experiment is to study how enzyme activity is affected by environmental conditions. Researchers tested the level of potato extract enzyme activity with 1-11 pH‚ varying temperature‚ catechol solution‚ hydroquinone solution‚ and different measurements of catechol. In Figure 1A and 1B‚ pH levels were tested with potato extract to see how pH would affect the amount of Benzoquinone is formed in the potato. Although it was hypothesized that enzymes would form Benzoquinone better in acidic
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Discussion The primary purpose of this experiment was to determine the optimum temperature range for the activity of the enzyme lactase. Extreme temperatures can have a detrimental effect on enzymes; very hot temperatures can cause the denaturation in the enzyme‚ which is the loss of protein structure. This causes a change in the shape of the enzyme leading to its inability to perform its function. As previously stated‚ the alternate hypothesis read: the optimal temperature range for lactase activity
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The Effect and Rate of the Enzyme Amylase on Starch Abstract Assessing reaction speed of the enzyme amylase can be measured by the amount of glucose and maltose produced during given time intervals. I hypothesized that‚ if the reaction time is longer‚ then the amount of amylase will be larger. Enzymes are specific in their match of substrates they will breakdown – similar to a key and its lock. Since amylase is the only enzyme that breaks down starch‚ the procedure was effective and gave clear
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Group No. 10 Date Started: June 11‚ 2013 Tongco‚ Val Justin DM. Date Finished: June 18‚ 2013 Santos‚ Erickson S. Vasquez‚ Jona Candace P. Wong‚ Victor Lorenzo E. Experiment 1 Use of Micropipettor and Spectrophotometer Introduction In scientific experiments‚ correct measurements are required to achieve precise and accurate data. Precision is the degree to which several measurements provide answers very close to each other. Accuracy describes the nearness of a measurement to the
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The enzyme tyrosinase was successively extracted by combining a homogenate of a potato and sodium sulfate with ammonium sulfate. Tyrosinase was successfully extracted by taking advantage of solubility properties of certain proteins. A standard curve was generated indicating dopachrome absorbance values through the use of a spectrophotometer and a computer graphing program. A spectrophotometer was used to measure either the amount of light that passed through a solution (transmittance) of the amount
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LABORATORY REPORT Activity: Enzyme Activity Name: Daniel Franco Instructor: Professor Jennifer Frere Date: 03.08.2015 Predictions Sucrase will have the greatest activity at pH 6 Sucrase will have the greatest activity at 60 °C (140 °F) Sucrase activity decreases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity Dependent Variable amount of product (glucose and fructose) produced Independent Variable pH Controlled Variables temperature‚ amount of
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conditions and enzyme function. *There are many environmental factors these may include temperature because if its too cold the enzyme would still work but it would work slowly and if its too hot the enzyme will become denatured. As the temperature increases‚ the kinetic energy of the molecules increase so they move around more meaning that there are more collisions between the enzymes and substrates molecules and therefore more reactions. pH is a factor because the different types of enzymes work best
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certain environmental factors affect the enzyme activity rate. For the first experiment‚ where we tested the increase in concentration of enzyme with the substrate‚ we found that higher concentration of enzyme increases the rate of reaction of the enzyme. This is because more enzyme molecules are present‚ which allow more substrate molecules to get into the active sites of the enzyme (Sattler W& Esterbauer H). When calculating the absorbance of different enzyme concentration‚ it was noticeable that
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