Proteins are polymer chains made of amino acids linked together by peptide bonds. In nutrition‚ proteins are broken down in the stomach during digestion by enzymes known as proteases into smaller polypeptides to provide amino acids for the body‚ including the necessary amino acids that cannot be biosynthesized by the body itself. Biosynthesis is an enzyme-catalyzed process in cells of living organisms by which substrates are converted to more complex products. Collagen is a group of naturally occurring
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CHAPTER 8 AN INTRODUCTION TO METABOLISM Metabolism‚ Energy‚ and Life 1. Explain the role of catabolic and anabolic pathways in cellular metabolism. Catabolic means the molecule is broken down into smaller parts. Anabolic means molecules are used to build bigger compounds. 2. Distinguish between kinetic and potential energy. Kinetic energy is the energy of object in motion. Potential energy is the energy a object has due to its position or traits. 3. Distinguish between
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Alpha Amylase with Starch at Specific pH ’s and Temperatures Page 1 Abstract Enzyme ’s are used as catalysts in certain reactions. They help lower the activation energy needed for the reaction to go to completion. At optimum temperature and pH the amount of collisions of substrate and enzyme is at its highest‚ any deviation from the optimum temperature and pH will result in the denaturization of the enzyme. The purpose of this experiment is to find the optimum temperature and pH for the reaction
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point for the enzyme (catalase) to substrate (H2O2(aq)) concentration ratio. Thus‚ to truly understand this‚ the trial time period should be extended insofar that a declination in the rate of the reaction can be observed with multiple trials. If the trends of the independent trials coincide with one another‚ then it is plausible that a saturation point may have been a factor of the linear-like trend. This case will be further discussed in one of the five major factors that influence enzyme activity:
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peroxide affects the rate of reaction of the enzyme catalase. Background Information: Enzymes such as catalase are globular protein molecules with catalytic properties. A catalyst is a substrate which can alter the rate of reaction without itself undergoing any permanent change. As they are not changed my reactions which they catalyse‚ enzymes can be used over and over again. They are therefore quite effective in small amounts. All enzymes are specific as each one performs a particular
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Enzyme Study Questions 1. Definitions/terminology: o enzyme: a protein molecule that catalyzes chemical reactions without itself being destroyed or altered o catalyst: a substance that increases the rate of a chemical reaction but is not consumed or changed by it. o substrate: a substance upon which the enzyme acts. o denaturation: the partial or total alteration of the structure of a protein without change in covalent structure by the action of certain
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enzymatic hydrolysis is characterized by high reaction rate‚ high stability of the enzyme towards the denaturizing action of solvents‚ detergents‚ proteolytic enzymes‚ and a decrease in the viscosity of the reaction medium at higher temperatures‚ etc. Most often‚ enzymatic hydrolysis is carried out with the enzyme α-amylase from different sources and less often β-amylase is employed. The bacterial α-amylase enzymes attack the polysaccharide molecules in the inner part of the chain. They act on the
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ethanol since it is non-functional. The liver contains cells called hepatocytes; the breakdown of ethanol requires multiple enzymatic processes in these cells‚ which requires the organism to be alive to activate these enzymes.6 Since the chicken liver is not a live sample‚ these enzymes are not able to perform its functions‚ therefore it is
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carbohydrates begin in the mouth‚ where an enzyme‚ salivary amylase (α-amylase;ptyalin) starts to breaking the polysaccharides (starch) into short polysaccharides (dextrin). Dextrin is a partial degradation of starch‚ shorter chains of maltose units. Salivary amylase is inactivated by stomach acid in the stomach and to a small extent‚ it continues breaking down starch (but there’s no enzymatic activities on carbohydrates in the stomach). An intestinal enzyme‚ pancreatic amylase‚ continues the activity
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Amylase 1. List the substrate and the subunit product of amylase. _starch & maltose respectively__ 2. What effect did boiling and freezing have on enzyme activity? Why? How well did the results compare with your prediction?__Boiling caused amylase to be denatured‚ thus inactivating the enzyme. Freezing has no effect. The function of an enzyme is directly related to its environment‚ like temperature.__ 3. At what pH was the amylase most active? Describe the significance of this result. __ pH
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