Effect of temperature on enzyme activity In this experiment… Independent variable: Temperature of the amylase Dependent variable: Enzyme activity which is measured by the time for disappearance of starch Controlled variables: Volume of amylase; volume of starch solution; concentration of amylase; concentration of starch solution Prediction of results i) At low temperature‚ the rate of amylase activity is very low. ii) At optimum (=best) temperature‚ the rate of amylase activity is the
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Experiment 4 – Effect of Temperature on Enzyme Activity Aim To study the effects of temperature on the activity of amylase enzyme on starch solution. Introduction Enzymes are widely known as biological catalyst. Almost all cellular reactions are controlled and guarded by enzymes. Virtually every metabolic reaction which takes place within a living organisms are catalyzed by enzymes. Enzymes are complex three-dimensional globular proteins. Some of the enzymes are built up off proteins and
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Enzyme Catalase Activity in Reaction with the Substrate Hydrogen Peroxide Abstract We performed these experiments to observe the effects of enzymes on the rate of reactions. We tested and compared the activity of the enzyme catalase on the substrate H2O2 in various states and percentages‚ and observed the absorption values of the enzyme-substrate relationship at different concentrations. Our results show that the more substrate available‚ the quicker the reaction will happen except in one test
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Substrate concentration and yeast catalase Aim: To see how the substrate concentration in hydrogen peroxide affects the rate of an enzyme controlled reaction using yeast catalase. Introduction: An enzyme is a biological catalyst made of protein. Enzymes are protein molecules found in living organisms and in this case I will use a yeast catalase. Catalase is an enzyme that catalyzes the reduction of hydrogen peroxide. Hydrogen peroxide is a poisonous by-product of metabolism‚ so it is very
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Method I generally followed most of my plan for the experiments‚ but to improve accuracy and reliability‚ I made one change. In my plan‚ I said that I was going to use 20cm³ of starch for each experiment. However‚ in my actual experiment I used 40cm³ of starch. This is because I thought I might not have had enough solution if I only used 20cm³ of starch. If this was the case‚ then I would have to stop the experiment half way through‚ which would have prevented me from obtaining accurate results
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Temperature Affecting Enzyme Activity Introduction The basic properties of life revolve around chemical reactions. Without the presence of enzymes some of life’s processes would not come so easily. Enzymes are basically proteins‚ which have specific shapes for different substrates. Enzymes change the rate in chemical reactions. It does this without having to change its own shape‚ which makes enzymes different from other proteins. A common enzyme that we have is catalase‚ which breaks down
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Copy button on the panel above to save your report) Activity: Name: Instructor: Date: Enzyme Activity Pam Campbell Id 0002337 Dr. Murphy Nmezi August 9‚ 2011 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 40 °C (104 °F) 3. Sucrase activity increases with increasing sucrose concentration until a plateau is reached. Materials and Methods Effect of pH on Enzyme Activity. 1. Dependent Variable. amount of product (glucose and
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Matthew Saldanha Bio DCP lab-Catalase experiment Aim: To investigate enzyme kinetics‚ using different concentration of the enzyme. Hypothesis: The assay system used in the lab consists of a filter paper disc coated with the enzyme and the dropped into a papercup of substrate (Hydrogen Peroxide). As the hydrogen breaks down the hydrogen peroxide into hydrogen and oxygen gas‚ the bubbles of oxygen gas collect underneath the filter and make it
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investigate the effect of substrate concentration Hydrogen Peroxide H O (in %) on the rate of reaction of the enzyme catalase (in 1/mean time). Prediction: As the substrate concentration (hydrogen peroxide) in % increases the rate of reaction in 1/mean rate increases until the solution becomes saturated with the substrate hydrogen peroxide. When this saturation point is reached‚ then adding extra substrate will make no difference. The rate steadily increases when more substrate is added because
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the three different Substrate Concentrations (3%‚ 1% and 0.3%) as which one was the fastest to react‚ I hypothesized that the reaction would occur the fastest with the 3% hydrogen peroxide (the highest amount of concentration) because the higher the concentration the more faster the reaction occurs and helps produce or break up the enzyme. After testing all three of my substrate concentrations with 10 trials each‚ my data showed (first graph) that the 3% substrate concentration had the fastest average
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