production and reaction velocity increased with increasing catalase concentration‚ however‚ the 33% percent catalase concentration showed a drop of 0.175 mL O2/s compared to the 25% catalase concentration (figure 1.2). The velocity of 25% catalase was 0.275 mL/s‚ 33% was 0.1 mL/s‚ 50% was 0.435 mL/s‚ and 75% catalase was 0.575 mL/s (figure 1.1). The 50% catalase concentration produced the most O2 overall however the 75% catalase concentration had the fastest initial reaction velocity. Experiment III: O2
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competitive inhibitor‚ thereby impeding the forward reaction. In this experiment‚ o-diphenol oxidase‚ an enzyme that causes the browning in fruits‚ was extracted from banana and reaction rate of this was established with various concentrations of catechol‚ the substrate‚ using the Michaelis-Menten‚ Lineweaver-Burk‚ Hanes-Woolf and Eadie-Hofstee plots. The plots were generated using the slope of absorbance readings against time plots. Absorbance can be used to detect reaction rate as this notes color
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phenol in the absence or presence of cellobiase….. Methods: Activity #1 The materials used for this activity are as follows: 1.5 mM substrate‚ enzyme‚ Stop solution‚ buffer‚ DPTPs‚ 15 ml conical tubes‚ cuvettes‚ marker‚ beaker‚ distilled water‚ spectrophotometer‚ stop watch. First four 15 ml conical tubes were labeled: “Stop solution“‚ “1.5 mM Substrate”‚ “Enzyme”‚ and “Buffer”. Then‚ seven cuvettes were located and five of them were labeled “E1-E5” and the other two were labeled “Start” and
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them to bind to a reactant‚ called a substrate at an active site. Enzymes are flexible‚ and therefore can change it’s shape to better accommodate its substrate; this is the induced fit model (D. Fraser‚ 50). When an enzyme binds to a substrate‚ it is called the enzyme substrate complex‚ where the substrate is then converted into different products. As an enzyme is not a part the reaction‚ it remains unchanged and therefore can continue binding to other substrate molecules‚ catalysing the same reaction
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quantify the concentration of the Bovine Serum Albumin (BSA) then constructing a standard curve graph and to use the spectrophotometer to perform an enzyme assay using different concentration of the BSA. Experiment 5 also verifies the Beer-Lambert Law‚ which is the linear relationship between absorbance and concentration of an absorbing species. Absorbance formula is shown in fig. 1.1. However‚ the Beer-Lambert Law is not obeyed at high concentration as solution with high concentration may alter the
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structure of phosphatase‚ which alters its active site‚ and thus changes its efficiency to catalyze the reaction. We measured the rate of reaction‚ by using a chromogenic substrate‚ PNPP‚ and a spectrometer to determine the amount of product produced in 15 min and also using our normal curve created of known PNP concentrations
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Steady-state rate equations Reactions of two substrates Inhibition of enzyme activity pH dependence Biological regulation of enzymes Computational Systems Biology Simple Enzyme Kinetics 3 Computational Systems Biology Basics • • An essential feature of enzyme-catalyzed reactions is saturation: at increasing concentrations of substrates the rate increases and approaches a limit where there is no dependence of rate on concentration (see slide with limiting rate Vmax) •
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(Phenolase). 2. To determine the level of specificity of Phenolase using the following substrates: Caffeic Acid‚ Catecol‚ Guaicol‚ Pyragallol and Tyrosine. 3. To determine the effect of ascorbic acid on Peroxidase. 4. To determine the level of specificity of Peroxidase using the following substrates: Caffeic Acid‚ Catecol‚ Guaicol‚ Pyragallol and Tyrosine. 5. To calculate the effect of the substrate acetaldehyde concentration on a Xanthine Dehydrogenase catalyzed reaction. 6. To determine the effect of heat
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reversible inhibitors: competitive‚ uncompetitive‚ and noncompetitive. They can be plotted on double reciprocal plot. Competitive inhibitors are molecules that look like substrates and they bind to active site and slow down the reactions. Therefore‚ competitive inhibitors increase Km value (decrease affinity‚ less chance the substrates can go to active site)‚ and VMAX stays the same. On double reciprocal plot‚ competitive inhibitor swifts the x-axis (1/[s]) to the right towards zero compared to the slope
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in which each enzyme can only speed up a specific reaction. There are molecules that enzymes work with called substrates. substrate bind to an area of an enzyme called active site. There is specificity between the enzyme and substrate that react with. When a specific substrate binds to the active site of an enzyme‚ the active site undergoes slight conformational change to keep the substrate long enough to be converted to a product. So‚ the activity of enzymes can be determined by measuring the number
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