INTRODUCTION Enzyme is a biological catalyst that acts on a molecule called substrate and it also significantly speed up a chemical reaction by lowering the activation energy. In order to learn about the enzyme and its behaviour‚ this lab practical is conducted to examine the kinetic of the enzyme alkaline phosphatase. As illustration‚ when alkaline phosphatase is added to a substrate called p-Nitrophenyl phosphate (colourless in alkaline solution)‚ a series of reaction takes place and eventually
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It is hypothesized that as the substrate concentration increases‚ the rate of reaction will increase respectively‚ until the enzyme reaches its optimum point of saturation‚ after which any increase in the substrate concentration will no longer affect the rate of reaction. The independent variable in this investigation is the varying concentrations of the substrate (Hydrogen Peroxide: 1%‚ 3%‚ 5% and 6%)The dependent variable was the rate of enzyme catalase activity‚ which was measured by the volume
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Investigating the Enzymatic Activity of Catecholase through Temperature‚ pH‚ Enzyme Concentration‚ and Substrate Concentration University of Alabama at Birmingham Burgess‚ B.N. Introduction: Background Enzymes are macromolecules that act as catalysts in living organisms by speeding up chemical reactions without being changed or destroyed by the reaction (Campbell and Reece‚ 2008). Enzymes are able to speed up the rate of a chemical reaction by decreasing the activation energy during the reaction
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Lab - Formal Report – August 8‚ 2007 ABSTRACT This investigation examined what would happen to the rate of an enzyme-catalyzed reaction if the concentration of substrate changed. We hypothesized that if the concentration increased‚ then the reaction rate would also increase. To test our question‚ we varied a combination of substrate and buffer‚ totaling 6mL‚ with a constant amount of 2 drops of catalyst. The enzyme catalyst‚ peroxidase‚ increased the rate of the reaction. The results of
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just 6 amino-acids. Substrate in active site Enzyme Structure Enzymes are proteins‚ and their function is determined by their complex structure. The reaction takes place in a small part of the enzyme called the active site‚ while the rest of the protein acts as "scaffolding". This is shown in this diagram of a molecule of the enzyme trypsin‚ with a short length of protein being digested in its active site. The amino acids around the active site attach to the substrate molecule and hold it in
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lead to different products without their contribution. Enzymes are biocatalysts that usually show high affinity to a specific substrate under particular environmental conditions. The binding of the substrate and catalysis take place at a specific small region‚ around 10 amino acids‚ in the enzyme known as active site which usually represents a hydrophobic cleft where substrate molecules are being attached in the optimal orientation using the full range of possible intermolecular forces. Some enzymes
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reaction with the use of a catalyst. Catalyst – any substance that increases rate of reaction upon addition to a certain reaction Page 3 Enzymes Act on substrates in a reaction Highly specific Breaks down complex macromolecules‚ synthesizes compounds essential for the cell Active site Enzyme-substrate complex Speeds up reaction rates Page 4 http://www.cas.muohio.edu/~wilsonkg/old/gene2005/syllabus_F03_23.jpg Page 5 Enzymes Require cofactors for
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"ase" to the name of the substrate. Example: Dehydrogenases are enzymes that remove hydrogen. Induced-fit Theory The shape of the enzyme must match the shape of the substrate. Enzymes are therefore very specific; they will only function correctly if the shape of the substrate matches the active site. Enzyme and substrates An enzyme-substrate complex forms when the enzyme’s active site binds with the substrate like a key fitting a lock. Enzyme-substrate complex The product is
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darkest in their respective treatments‚ the spectrometer would be needed. Starting with the palest and moving to the darkest‚ all absorbance was measured at 460 nm. Once all these readings are found‚ divide by 0.0078 to calculate the benzoquinone concentration (µm). Mean and standard deviation were both calculated using Microsoft Excel
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Enzymes are specific-type proteins that act as a catalyst by lowering the activation energy of a reaction. Each enzyme binds closely to the substrate; this greatly increases the reaction rate of the bounded substrate. Amylase enzyme‚ just like any other enzyme‚ has an optimum PH and temperature range in which it is most active‚ and in which the substrate binds most easily. The purpose of this experiment was to determine (1) the reaction rate of an amylase enzyme in starch and (2) the environmental
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