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Enzyme Catalyzed Reaction Lab Report

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The purpose of this unit was the kinetic analysis of Alcohol dehydrogenase under ideal conditions and in the presence of an inhibitor. In a normal reaction, the reactant is converted to the product, whereas in an enzyme-catalyzed reaction, the substrate reversibly binds with the enzyme to form the enzyme-substrate complex, which is then converted to the product and the free enzyme. The rate of the reaction is the concentration of substrate consumed or the concentration of product formed, therefore, the rate of an enzyme-catalyzed reaction is the velocity at which the product is formed from the substrate over time. There are many factors that influence enzymatic reactions, but two major ones are the enzyme and substrate concentrations. The ideal conditions for studying enzyme activity are at zero order reaction conditions as the rate of the reaction would be indicative of solely the characteristics of the enzyme. An important aspect of enzyme-catalyzed reactions is saturation, where at low substrate reactions, the rate of the reaction increases as the substrate concentration is increased. Eventually, there will reach a point where the enzyme is performing at the maximum activity so the reaction rate is no longer dependent on the substrate concentration …show more content…

Furthermore, NADH has an absorbance max at 340 nm, which allows for the reaction to be followed by the increase in A340 as NAD+ is reduced. From this experimental data, the initial velocity of the reaction can be obtained as this is the rate of the reduction reaction, the slope of the absorbance vs. time curve. Subsequently, this can be converted to the concentration per time using the Beer-Lambert equation. From the values obtained, the Michaelis-Menten and Lineweaver-Burk plots can be created, which would allow for the determination of the KM, Vmax, and

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Nevertheless, the effects caused by the breakage of bonds will eventually lead to a decrease in the rate of reaction. As seen in the data, the reaction rate increased from 0.088 to 0.101 throughout the interval of -5℃ to 20℃ then decreased to 0.037 throughout the interval 20℃ to 56℃. This can be explained by the fact that 20℃ is the optimal temperature, therefore the active site of the enzyme is complementary to the substrate, causing the rate of reaction to be

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1117 Words | 5 Pages

The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.

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By using a spectrophotometer to measure absorbance at 420 nm, the rate of enzyme activity after all reactions have come to a stop can be

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Using two test tubes, label one “s” for substrate and the other “e” for enzyme. The substrate tube should contain 7 mL of distilled water, 0.3 mL of hydrogen peroxide, and 0.2 mL guaiacol and the enzyme tube should contain 6 mL of distilled water and 1.5 mL of peroxidase. Combine the materials of the substrate and enzyme tubes, mix the two using a clean transfer pipette, transfer a portion into a cuvette so that the cuvette is about half-full then cover the top of the cuvette with Parafilm and then place it in the spectrophotometer and record absorbance. Remove the cuvette and repeat recording absorbance at 1, 2, 3, and 4 minutes. Be sure to mix the cuvette and clean its surface with Kimwipes before each reading.

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Introduction: Enzymes are biological catalysts that increase the rate of a reaction without being chemically changed. Enzymes are globular proteins that contain an active site. A specific substrate binds to the active site of the enzyme chemically and structurally (4). Enzymes also increase the rate of a reaction by decreasing the activation energy for that reaction which is the minimum energy required for the reaction to take place (3). Multiple factors affect the activity of an enzyme (1).

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Enzymes are catalysts that accelerate chemical reactions by decreasing the amount of activation energy needed, during reactions enzymes are not consumed allowing the enzyme to be reused (Eed, 2013). Each individual enzyme has a groove on its own surface, this groove is known as the active site (Robinson, 2016). On the active site a reactant, also known as a substrate, interacts with the enzyme in order to cause a reaction that could take days or years to happen occur significantly faster (Robinson, 2016). There are many factors that affect how efficient enzymes are, such as pH, temperature, and both enzyme and substrate concentration (Eed, 2013). Another factor is charge, however its affect tends to be negligible and the actual shape of the

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191 Words | 1 Pages

Enzymes are a type of globular protein that function within the human body as catalysts for other biochemical reactions. Catalysts are agents within a specific reaction that are able to quicken the reaction process without being altered themselves. Substances that these enzyme catalysts are able to convert into products are labelled as substrates. In order for the enzyme to catalyse the specific biochemical reaction, the substrate must bind to a special region on the surface of the globular enzyme (known as the active site). However, the shape and chemical properties of the active site and the substrate must match each other in order for the reaction to proceed.

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730 Words | 3 Pages

Enzyme speed chemical reactions by lowering the activation energy, activation energy is the energy require for chemical reactions to take place. Enzyme is the ES complexes that lower the activation energy. There are two ways to form product in enzyme, one is two substrates to form one product in one active site or one substrate break down into two products. If two substrate molecules need to be joined to form one product, two substrates need to attached to the enzyme holds them close together, reducing any repulsion between the substrate molecules so they can bond more easily to form one product. If the enzyme is catalysing a breakdown reaction, it means one substrate breakdown into two products, one substrate molecule fitting into the active

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1515 Words | 7 Pages

Under some conditions, substrate will bind to the active site of an enzyme and form an enzyme-substrate complex. The enzyme would fasten the chemical reaction and the substrate will

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Speeding up reactions is a very important function of enzymes because it can reduce time and cost for procedures. Also, without enzymes, these reactions would take place too slowly to keep organisms alive. There

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Enzymes are resourceful catalysts for biochemical reactions, like all catalysts enzymes tend to speed up reactions. Enzymes use alternative reaction pathway of lower activation energy. They take part in the reaction, and as a result their able to provide alternate pathways. Throughout the reaction enzymes remain unchanged because they cannot experience any permanent changes Enzymes consist of active sites, which are parts of the enzyme molecule that have the ideal shape and functional groups to bind to one of the reacting molecules.

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INTRODUCTION Enzymes are biological catalyst that alters the chemical reaction rate without itself being altered which reacts with the substrate and converts the enzyme substrate complex into different molecules – product. Enzyme plays the consequential role in functioning of life process such as for growth, digestion of nutrients, excretion of metabolic waste, energy provider to brain and muscles and thus directly or indirectly involved in every biological processing of life. Apart from numerous life functioning role, enzymes are also used in industry-oriented procedure such as for drug delivery in biomedical research, production of biodiesel in energy sector, production of jams and syrups in food industry, treatment of sewage in waste management

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1150 Words | 5 Pages

The data received in the experiment only somewhat supported my hypothesis. My group tested how changing the pH of the hydrogen peroxide substrate would affect enzyme activity and the rate of reaction. Our hypothesis was that the solution with a pH closest to the pH of hydrogen peroxide, which is fairly acidic, would have the fastest rate of reaction. After conducting the experiment, we found that an acidic pH of 2 resulted in the reaction having a reaction rate of 0 sec-, while when conducted with a substrate pH of 7, the reaction proceeded at the fastest rate of 0.051 sec-. These results show that a pH of 7—a more neutral solution—actually caused the enzyme to work the best, as opposed to the predicted acidic substrate.

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ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells.

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2446 Words | 10 Pages

An enzyme can be regarded as a catalyst for a biochemical reaction, or more simply, a biological catalyst. Its sole purpose is to increase the rate of a reaction, or speed up the reaction via provision of an alternative reactive pathway, which entails a lower activation energy. Enzymes participate in the reaction itself, enabling the occurrence of an alternate pathways of reaction, but they do not attain permanent changes to their structure or nature, and as a result remain unchanged preceding a reaction. It is then understood, that they can amplify the rate of a reaction, but are unable to effect upon the equilibratory position. Enzymes, unlike chemical catalysts are highly specific in terms of the reactions that they catalyse.

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