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Importance of enzymes
Effect of substrate concentration on enzymes
Substrate effects on enzymes
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Recommended: Importance of enzymes
Introduction
Enzymes are macromolecules that act as a catalyst, and it’s a chemical agent that accelerates the reaction without being consumed by the feedback or the results (Campbell and Reece, 2005). After the adjustment by the enzymes, the chemical movement through the pathways of metabolism will become awfully crowded because many chemical reactions are taking a long time (Campbell and Reece, 2005). There are two kinds of reactions in nature. The first one is Catabolic reaction and the second one is Anabolic reaction. Catabolic reactions are large molecules that are broken up into smaller molecules (Ahmed, 2013). Anabolic reactions are small molecules that join to make larger molecules, like polymerization (Ahmed, 2013). If you put all the reactions together, catabolic and anabolic is called Metabolism (Ahmed, 2013).
Basically enzymes are protein molecules that can be composed of one or more multiple polypeptide (Ahmed, 2013). Enzymes can also have non-protein parts that are called cofactors and they are attached to them (Ahmed, 2013). “If the cofactors are organic nature they are called coenzymes” (Ahmed, 2013). For a catalytic of an enzyme to extend its speed of the reaction varies, depending of the factors such as temperature, pH, concentration of substrate, concentration of enzyme and so on (Ahmed, 2013). Enzyme has five properties: first one is Enzyme bind to substrate, second one is Enzyme are substrate specific, third one is substrate binds an enzyme at the active site (Ahmed, 2013). The last two properties are “Enzymes are not consumed in a reaction” and “Enzyme work best on optimum temperature and pH” (Ahmed, 2013). Any particular study will have changes in the rate of the reaction because of the differe...
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...act with the factors and it cause them to react greatly as we expect them to react.
References
Albery John W. and Knowles Jeremy R. (1976). “Evolution of Enzyme Function and the Development of Catalytic Efficiency.” Biochemistry. Vol. 15, No. 25.
Ahmed, S. 2013. Principles of Biology Lab manual. U.S.A., Hobbes End publication: page 21-30 (Ahmed, 2013).
Chul-Won Park and Zipp Erik (2000). “The effect of Temperature and pH on Enzymes Kinetics.” Introduction to Biochemical Engineering. Web (Chul-Won Park, 2000).
Cleland W. W. (1975) “Partition Analysis and the Concept of Net Rate Constant as Tools in Enzyme Kinetics.” Biochemistry. Vol. 14, NO. 14 (Cleland 1975).
Reece Jane B., Urry Lisa A., Cain Michael L., Wasserman Steven A., Minorsky Peter V., and Jackson Robert B. (2005). “Chapter 8: An introduction to Metabolism”. Campbell Biology. Ninth Edition. Pp152-157.
After conducting this experiment and collecting the data I would have to say that the optimal temperature for enzyme activity would have to be room temperature which in my experiment was thirty-four degrees Celsius. I came to this answer because the glucose test strip showed that at room temperature there was more glucose concentration that at either of the other temperatures. Due to temperature extremes in the boiling water the enzymes could no longer function because the breakdown of lactose stopped. The cold water also hindered the breakdown of the lactose but as the water warmed the enzymes were more active which can be seen in the results for the cold water at 20 minutes B. Describe the relationship between pH and the enzymatic activity of lactase.
Each group shared their findings with the class. The metabolic rates of the mouse were conducted by the instructor and distributed. We also did not use the Winkler method to measure the O2 levels. We used a measuring device instead.
Enzymes are proteins that increase the speed of reactions in cells. They are catalysts in these reactions which means that they increase the speed of the reaction without being consumed or changed during the reactions. Cofactors are required by some enzymes to be able to carry out their reactions by obtaining the correct shape to bind to the other molecules of the reaction. Chelating agents are compounds that can disrupt enzyme reactions by binding to metallic ions and change the shape of an enzyme. Catechol is an organic molecule present under the surface of plants. When plants are injured, catechol is exposed to oxygen and benzoquinone is released because of the oxidation of catechol. Catecholase aids in the reaction to produce
In this experiment as a whole, there were three individual experiments conducted, each with an individualized hypothesis. For the effect of temperature on enzyme activity, catalase activity will be decreased when catalase is exposed to temperatures greater than or less approximately 23 degrees Celsius. For the effect of enzyme concentration on enzyme activity, a concentration of greater or less than approximately 50% enzymes, the less active catalase will be. Lastly, the more the pH buffer deviates from a basic pH of 7, the less active catalase will be.
Background information:. Enzyme Enzymes are protein molecules that act as the biological catalysts. A Catalyst is a molecule which can speed up chemical reactions but remains unchanged at the end of the reaction. Enzymes catalyze most of the metabolic reactions that take place within a living organism. They speed up the metabolic reactions by lowering the amount of energy.
Enzymes are biological catalysts - catalysts are substances that increase the rate of chemical reactions without being altered itself. Enzymes are also proteins that fold into complex shapes that allow smaller molecules to fit into them. The place where these substrate molecules fit is called the active site. The active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of residues that form temporary bonds with the substrate and residues that catalyse a reaction of that substrate. (Clark, 2016)
Enzymes have the ability to act on a small group of chemically similar substances. Enzymes are very specific, in the sense that each enzyme is limited to interact with only one set of reactants; the reactants are referred to as substrates. Substrates of an enzyme are the chemicals altered by enzyme-catalysed reactions. The extreme specific nature of enzymes are because of the complicated three-dimensional shape, which is due to the particular way the amino acid chain of proteins folds.
Enzymes as mentioned before help speed up reactions, they generally work by bonding to a substrate, this bonding occurs at the active site. This link then forms a different molecule which will benefit its respective process. Every enzyme has its own optimum pH level to work under, if too low the enzyme will be very slow. However if too high the enzyme will then denature and be obsolete. This is why it is important to know the optimum pH level for whatev...
= == In relative terms enzymes are biological catalysts; control the rate of chemical reaction, different temperatures and pH’s affect their optimum rate of reaction in living organisms. In detail; enzymes are globular proteins, which catalyse chemical reactions in living organisms, they are produced by living cells – each cell has hundreds of enzymes. Cells can never run out of enzymes as they or used up in a reaction.
In this lab, it was determined how the rate of an enzyme-catalyzed reaction is affected by physical factors such as enzyme concentration, temperature, and substrate concentration affect. The question of what factors influence enzyme activity can be answered by the results of peroxidase activity and its relation to temperature and whether or not hydroxylamine causes a reaction change with enzyme activity. An enzyme is a protein produced by a living organism that serves as a biological catalyst. A catalyst is a substance that speeds up the rate of a chemical reaction and does so by lowering the activation energy of a reaction. With that energy reactants are brought together so that products can be formed.
Enzymes are biological macromolecule that acts as catalysts and increase the rate of a chemical reaction. Without enzymes, life, as we know about it, would not exist. Enzymes function by deceasing the activation energy and stabilizing the transition state of a chemical reaction without altering the thermodynamic of reaction (#1 Boyer). At the molecular level, enzymes catalyze these reactions by binding to the substrate or reactants to form an enzyme-substrate complex. The reaction takes place while the substrate is bound to the enzyme and converting the substrate to the new product. The new product is then released from the enzyme substrate complex, and the enzyme is then free to bind with more substrate. E+S → ES → E+P (#1 Boyer). Based on
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
Purpose: This lab gives the idea about the enzyme. We will do two different experiments. Enzyme is a protein that made of strings of amino acids and it is helping to produce chemical reactions in the quickest way. In the first experiment, we are testing water, sucrose solution, salt solution, and hydrogen peroxide to see which can increase the bubbles. So we can understand that enzyme producing chemical reactions in the speed. In the second experiment, we are using temperature of room, boiling water, refrigerator, and freezer to see what will effect the enzyme.
Enzyme kinetics deals with the rate of enzyme catalyzed reactions. This provide information about several important aspects such as:-
Coenzymes are a type of cofactor and they are bound to enzyme active sites to help with their accurate functioning. Coenzymes which are directly concerned and altered in the course of chemical reactions are measured to be a kind of secondary substrate. This is as they are chemically changed as a result of the reaction unlike enzymes. However unlike the primary substrates, coenzymes can be used by a amount of different enzymes and as such are not specific. For example hundreds of enzymes are able to use the coenzyme NAD.