The experimental results were different from the hypothesis because while the enzyme appeared to not work as well‚ I expected a more significant change. Most of the time‚ there was only a millimeter of difference of the foam between the two samples while I expected a greater difference such as 10 millimeters. Enzymes speed up chemical reactions and at the active site‚ a substrate can be broken down or two substrates can form a larger molecule. Hydrogen peroxide is broken down by peroxidase into water
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Kenneth Hampton | | |Restriction Enzymes: | |A study in Reactions and Mapping | | | |November 7‚ 2008 | ABSTRACT This experiment will study the
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Enzyme Lab Report Introduction The objective of this experiment was to determine if changes in pH or temperature affected the activity of enzymes‚ specifically the enzyme sucrase. Enzymes are protein molecules that act as biological catalysts to increase the speed of the reaction or to lower the activation energy of that reaction. However‚ the activity of an enzyme can be affected by physical factors such as pH and temperature because these factors alter the structure of the enzyme (Freeman‚ 2011)
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relationship between substrate concentration and initial reaction rate provided that substrate concentration is much greater than enzyme concentration. Enzymes are essential to life as they are required for many vital metabolic reactions to occur. To adequately explain the properties of enzymes‚ it is assumed that an enzyme-controlled reaction takes place through an enzyme-substrate complex by the lock and key mechanism. It is hypothesized that a greater concentration of product is achieved through
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Enzyme Lab Report Introduction: Enzymes are proteins that enable chemical reactions. In the enzyme lab‚ the effects of concentration‚ temperature and pH on the functionality of the enzyme catalase. The enzyme lab was also about measuring reactions by capturing the oxygen that was generated by the reaction. Materials and Methods: Experiment 1‚ 2‚ & 3 Experiment 1 examined the effects of concentration on catalase activity. Experiment 2 examined the effects of concentration in temperature
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Stallings Period 2 January 26‚ 2013 Enzyme Catalysis Lab Report Background: Enzymes are catalyst‚ which affect the rate of a chemical reaction. One consequence includes the cell to carry out complex chemical activities at relatively low temperatures. In these reactions the substrate binds reversibly to the active site. The cause of this is a decrease in the energy needed to activate the reaction of the substrate molecule to from products. Every enzyme is particular for a reaction for the reason
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and measure the enzyme activity of β-galactosidase in the different concentrations of o-Nitrophenylgalactoside (ONPG) using a spectrophotometer. The spectrophotometer was also set at 420nm‚ a wavelength which is best for recording the absorbance values for the experiment. From the results‚ 0.9mM ONPG solution has the highest absorbance and 0.1mM ONPG solution has the least. Also‚ 0.5mM ONPG solution has the highest rate of enzyme activity and it is the most efficient as the enzyme activity of the
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Hypothesis: If pH is increased or decreased past the enzyme’s optimum pH‚ the number of products produced by the enzyme will decrease because the enzyme will become denatured. Variables: The Independent variable is the pH of the environment. The uncertainty of pH is ± 1. pH is a unitless value. The Dependent variable is the number of products produced. The uncertainty of this this measurement is ± 1 product. In order for this experiment to be controlled‚ many variable were identified and held constant
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two Title: Enzyme Function Purpose: To observe the role of enzymes in chemical reactions and to determine the kinds of cells that contain more of the enzyme catalase. Prior Knowledge: Enzymes are proteins that assist the chemical reactions of a cell by lowering the amount of activation energy needed to start the reactions‚ thereby enabling the cell to carry out the reactions at a faster rate; enzymes that lower the activation energy are therefore called catalysts. Moreover‚ the enzyme itself is
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Acetylcholinesterase and Butyrylcholinesterase substrate selectivity and various acting cholinesterase inhibitors Introduction Cholinesterases are a group of enzymes present in mammals which breakdown certain neurotransmitters by hydrolyzing the ester bonds within a molecule (Rang & Dale‚ 2007). There are two major types of enzymes‚ acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Though similar in structure‚ they differ in distribution‚ function and substrate specificity. AChE is
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