...variety of enzymes which involved in different metabolic reaction. Peroximoses were named because of its enzyme contains that usually remove hydrogen atoms from particular organic substrates with molecular oxygen. This oxidative reaction will produce hydrogen peroxide. [pic] However, during “peroxidative” reaction (H2O2 + R′ H2 → R′ + 2H2O), catalase (an enzyme in peroxisomes) will capitalize on the H2O2 produced by other enzymes in the organelle, in order to oxidize other substrates such as phenols, formic acid, formaldehyde, and alcohol. These reaction were quite important in kidney and liver cells, because the peroxisomes responsible to detoxify different toxic molecules that enter the bloodstream. In addition, when excess H2O2 was generated in the cell, catalase will converts it to H2O through the reaction: [pic] Pulping the liver will increase the total surface area of the liver. This means the production rate of catalase has been raised because more particles have been exposed to the other reactant, which lead to a higher rate of collision between the particles of reactants. Thus, there’s a higher chance to gain the activation energy in order to carry out chemical reaction. Rate of reaction increased. Catalase was a biological catalyst (enzyme) which made of protein and will denature in high temperature due to the breakage of bond between molecule. In this case, boiling the liver will cause the enzyme inside the peroxisomes to be denature. When the enzyme was denature...
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...effect that increasing temperature has on the enzyme catalase and its reactivity to the substrate, hydrogen peroxide. Enzymes are biological catalysts, which allow chemical reactions to occur under cellular conditions (PennState University, 2017). Cells contain thousands of different enzymes, and their activities determine which chemical reactions actually take place within the cell. Cooper G.M. (2000) stated that without enzymatic catalysts, most chemical reactions are so slow that they would not occur, as enzymes accelerate the rates of such reactions by over a million-fold. Freeman, S. (2006) illustrated that chemical reactions require an input of energy to begin called the activation energy....
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...Hillsborough Community College - Ybor City Campus 1025C Laboratory Exercise 3: Characteristics of Enzymes Introduction What are Enzymes? Enzymes are very large and complex proteins that that function as catalysts. They are synthesized by the cell to perform very specific functions. Each type of enzyme has a very specific shape (conformation) which provides its specific function. The shape of an enzyme molecule is determined and maintained by many weak intermolecular interactions between many different parts of the molecule. A catalyst is a material that donates energy to reactants in order to reduce their activation energy. In other words, they allow reactions to occur with less energy input (i.e. more quickly or at lower temperatures). The very specific shape of enzymes allows them to “fit” into a reaction and reduce the energy necessary for the reaction to occur. If their shape is changed, their ability to function as a catalyst is reduced or eliminated. As biological catalysts, enzymes are important because they speed up the rate of the reaction they catalyze that would otherwise be too slow to support life. Factors Affecting Enzyme Activity The rate at which an enzyme works is influenced by several factors including temperature and pH. Enzymes are most effective as catalysts under optimum physical and chemical conditions; as conditions change away from optimum, enzyme activity decreases (Figure 1.). Changes in various environmental factors, such as temperature or pH, may affect...
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...March 12th 2010 2.1.18 Enzymes are Globular Proteins Catalyst Molecule/element that speeds up a chemical reaction but is not used up in the reaction and remains unchanged after the reaction Globular proteins have specific tertiary structures. The shape comes from the protein’s primary structure (Sequence of amino acids) and it’s secondary structure. In globular proteins the tertiary structure usually has hydrophobic R groups in the centre and hydrophilic R groups around the outside of the ball. Enzymes are: Globular proteins and soluble in water Able to break molecules down or build them up! Biological catalysts Specific- because they catalyse a reaction with only one type of substrate Their globular structure has a pocket called an active site Activity affected by temperature and pH (Rate of reaction) Enzymes are large molecules with hundreds of amino acids. A lot of these amino acids work to keep the specific tertiary structure of the enzyme. The function of the enzyme depends on the shape, and for the enzyme to work correctly the tertiary structure must be maintained specifically. All of the structures (primary, secondary, tertiary) of the enzyme is involved in the specific active site shape. (Where the catalytic activity of the enzyme happens) Enzymes are faster than catalysts and because they are specific to one reaction they do not produce unwanted by products. An individual cell could contain over one thousand enzymes to catalyse every process, like digestion, respiration...
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...Chapter 3 Enzymes Learning Outcomes Candidates should be able to: (a) explain that enzymes are globular proteins that catalyse metabolic reactions; (b) explain the mode of action of enzymes in terms of an active site, enzyme/substrate complex, lowering of activation energy and enzyme specificity; (c) [PA] follow the progress of an enzyme-catalysed reaction by measuring rates of formation of products (for example, using catalase) or rates of disappearance of substrate (for example, using amylase); (d) [PA] investigate and explain the effects of temperature, pH, enzyme concentration and substrate concentration on the rate of enzymecatalysed reactions; (e) explain the effects of competitive and non-competitive inhibitors on the rate of enzyme activity; (f) use the knowledge gained in this section in new situations or to solve related problems. Enzymes are globular protein which act as catalysts • Enzymes are protein molecules defined as biological catalysts which speed up a chemical reaction and remain unchanged at the end of reaction. • Enzyme names end in –ase E.g. amylase, ATPase • Enzyme are globular proteins. Enzymes are globular protein which act as catalysts • Enzyme molecules are coiled into a precise threedimensional shape, which hydrophilic R groups (side-chains) on the outside of the molecule ensuring that they are soluble. Enzymes are globular protein which act as catalysts • Enzyme molecules have active site. • The active site of an enzyme is a region...
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...of Reaction of Catalase Abstract Properties of Enzymes focused on the variations of reaction rates amongst enzymes subjected to various circumstances such as temperature, pH levels, different concentrations of substrate, salt concentrations, Metal Copper Sulfate and lastly, the presence of an Enzyme Inhibitor. The assigned section of this laboratory for our efforts was the effect of temperature variations on enzyme reactions. To perform the experiment, we used a spectrophotometer to monitor the baseline catalase activity when they are placed in these two temperatures. In this way, absorbance can be measured over time to monitor catalase activity of the main baseline reaction. Our results showed that temperatures at higher degrees led to being inactive, whereas those at lower degrees lowered the reaction time. This comes to show that each enzyme can have a different optimal temperature and this experiment helped us to understand how reaction rate can be affected by temperature change. Introduction Thousands of complex biological processes are constantly taking place within our bodies. We require material transport, energy synthesis, and the manufacturing of various proteins, hormones, and other molecules (Source 1). Almost all of these everyday processes rely on the function of enzymes to take place. Enzymes are specifically grouped according to their function, and this information can often provide us with clues regarding what type of reaction that enzyme will catalyze (Source...
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...Unit 5- Anatomy and physiology Unit 5.4 P4 M1 D1 P4- Explain the Physiology of Two Named Body Systems in Relation to Energy Metabolism in the Body M1-Discuss the Roles of Energy in the Body In this assignment I will be explaining the physiology of the cardiovascular system and the respiratory system. Whilst explaining the two body systems I will be explaining energy production, process of cellular respiration, the role of enzymes within these body systems, the way that these systems absorb food and the products of digestion. The Cardiovascular System The heart pumps the blood around the body through the blood vessels which is made of mostly veins and capillaries. The blood carries the dissolved oxygen around the bodily cells, whilst carrying the dissolved oxygen the blood removes the waste and the other products from respiration. The body’s blood pressure has to be maintained. The blood distributes heat around the body along with hormones, nutrients, salts, enzymes and urea. The cardiovascular system transports simple molecules and materials to the liver and the body cells via the blood stream. This happens through the hearts pumping actions. The Respiratory System The respiratory system always refreshes oxygen within the lungs, it gets rid of the waste products like carbon dioxide and water, and this is done throughout actions like breathing. The dissolved oxygen passes through the alveolar walls into the bloodstream; this is then transported into the...
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...Factors Affecting Enzyme Activity Analysis of Enzyme Activity: Catalase and Tyrosinase Introduction to Neurotransmitters: Acetylcholinesterase Abstract: A series of three labs were combined to observe the effects of some common biological enzymes: Catalase, Tyrosinase, and Acetylcholinesterase (AChE). Enzymes are catalytic proteins, that when present in a chemical reaction, are able to lower the action potential needed to create the reaction without being destroyed or altered themselves in the process. In Part A, my hypothesis stated that when Catalase is combined with H2O2 the rate of conversion to water and oxygen gas should double when 5-10 drops of enzyme is added and quadruple when 10-20 drops are added. In Part B, my hypothesis stated that increases in enzyme concentration or buffer pH the substrate of the final product will yield increased substrate, also, if the substrate concentration is increased then the enzyme will be less diluted, the buffer pH will increase, or there will be a temperature increase. In Part C, my hypothesis stated that tacrine will have an inhibitory effect on AChE, and that those effects will increase as the level of concentration increases. In all three labs I postulated that increases in temperature and concentration levels and would increase the rates and decrease time to form chemical reactions. We setup each lab with a series of increased concentrations and a control trial using DiH2O. We observed the results using the...
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...Enzymes • The secret ingredient in living organism is Catalysis, a process performed by protein enzymes. • Their three-dimensional architecture gives them exquisite specificity to select the substrate molecules to which they will bind and on which they will operate. • The scene of operation called “active site” is usually a groove ,cleft or cavity on the surface of the protein. • Enzyme function frequently occurs many times, and in some cases many thousands of times per second. • The miracle of life: a myriad chemical reactions in the cell occur simultaneously with great accuracy and at astonishing speed. • Without the proper enzymes to process the food you eat, it might take you 50 years to digest your breakfast. • Catalysis is probably the most important function of proteins. • Catalysts that serve this function in organism are called enzymes. • With the exception of some recently discovered RNAs that have catalytic activity, all enzymes are proteins. • Enzymes are the most efficient specific catalysts known (increase rate reaction up to 10²º). • Nonenzymatic catalysts (up to 10²-104). • Enzymes are highly specific,even to the point of distinguishing stereoisomers of a given compound. 1)Enzymes are Effective Biological Catalysts 2)Difference between Kinetic and Thermodynamic Aspects of Reactions • The rate of the reaction and its thermodynamic favorability are two different topics although so related. • The standard free energy change (ΔG°) is the difference...
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...ABSTRACT Food and feed is possibly the area where processing anchored in biological agents has the deepest roots. Despite this, process improvement or design and implementation of novel approaches has been consistently performed, and more so in recent years, where significant advances in enzyme engineering has fastened the place of such developments. Targeted improvements aim at enzymes with enhanced thermal and operational stability, improved specific activity, modification of pH-activity profiles, and increased product specificity, among others. This has been mostly achieved through protein engineering and enzyme immobilization, along with improvements in screening. The latter has been considerably improved due to the implementation of high-throughput techniques, and due to developments in protein expression and microbial cell culture. Expanding screening to relatively unexplored environments (marine, temperature extreme environments) has also contributed to the identification and development of more efficient biocatalysts. Technological aspects are considered, but economic aspects are also briefly addressed. INTRODUCTION: Food processing through the use of biological agents is historically a well-established approach. The earliest applications go back to 6,000 BC or earlier, with the brewing of beer, bread baking, and cheese and wine making, whereas the first purposeful microbial oxidation dates from 2,000 BC, with vinegar production. Coming to modern days, in the late XIX...
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...BIOL 3380 Name:_____________________________________ Circle Session: T-PM W-AM W-PM R-AM R-PM F-AM F-PM Experiment 9 – Pre-lab Homework Enzyme Kinetics of LDH This pre-lab homework assignment is due at the beginning of your lab session. You are provided with the following portion of a protocol: • Determine concentration of enzyme stock solution, if unknown, by taking an A280 nm reading of a 1:100 dilution (in water). Use a total volume of 1 ml in the cuvette. • Dilute some of the enzyme stock with buffer A to make a 4 mg/ml solution. • Serially dilute the 4 mg/ml solution with buffer A to make working solutions of 400 µg/ml and 40 µg/ml. • Prepare 30 µl of each working solution for every sample The PI of the lab gives you a tube of enzyme and tells you the following before disappearing into the office to write more grant proposals: ➢ There is 50 µl of enzyme stock solution. The enzyme is expensive to purify, so follow the protocol exactly, using as little of the stock solution as possible. ➢ The concentration of the stock solution is currently not known, but a 1 mg/ml concentration of the pure enzyme has an A280 nm of 2.0. ➢ You’ll be performing the assay on 12 samples. ➢ Make enough of each working solution so that you have at least 400 ul to work with when you do the assay (to cover any waste and/or inefficiencies in pippetting). Using the spectrophotometer to read the absorbance at 280 nm, you get...
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...engrained in other minerals such as taconite (Royal Society of Chemistry). Iron is produced commercially by heating the iron ores with carbon and limestone. The initial process results in an intermediate known as pig iron. Pig iron contains approximately 3% of carbon and other contaminants. It is utilized in the production of steel. The annual production of crude steel approximately about 1.3 billion tons (Royal Society of Chemistry). Pure iron crystals have a very soft texture. In order to enhance its strength, iron is either mixed with impurities such as carbon, or it is complexed with other metals as is done in the manufacture of steel. Iron is an element that is essential to all living organisms. Several biological processes utilize iron. Iron-containing enzymes, such as catalase, catalyze some of the oxidation reactions in the body. Hemoglobin, the biomolecule that carries oxygen in the body contains iron as well (Cengage Learning). Scientific Background of Iron Iron is a transition metal. In the periodic table, it is in period 4 and group 8 element. The atomic number of iron is 26. It's documented melting point is 1538°C and has a boiling point of 2861°C. Iron has a relative atomic mass of 55.845. A non-bonded iron atom has an atomic radius of 2.04 and a covalent radius of 1.24. There are four iron isotopes; 54Fe, 56Fe, 57Fe, 58Fe. The atomic masses of the isotopes are 53.940, 55.935, 56.935, and 57.933 respectively (Royal Society of Chemistry). There are two oxidation...
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...Lab Manual Introductory Biology (Version 1.4) © 2013 eScience Labs, LLC All rights reserved www.esciencelabs.com • 888.375.5487 2 Table of Contents: Introduc on: Lab 1: Lab 2: Lab 3: Lab 4: The Scien fic Method Wri ng a Lab Report Data Measurement Introduc on to the Microscope Biological Processes: Lab 5: Lab 6: Lab 7: Lab 8: Lab 9: The Chemistry of Life Diffusion Osmosis Respira on Enzymes The Cell: Lab 10: Lab 11: Lab 12: Lab 13: Lab 14: Lab 15: Cell Structure & Func on Mitosis Meiosis DNA & RNA Mendelian Gene cs Popula on Gene cs 3 4 Lab Safety Always follow the instruc ons in your laboratory manual and these general rules: eScience Labs, LLC. designs every kit with safety as our top priority. Nonetheless, these are science kits and contain items which must be handled with care. Safety in the laboratory always comes first! Lab Prepara on • • Please thoroughly read the lab exercise before star ng! If you have any doubt as to what you are supposed to be doing and how to do it safely, please STOP and then: Double-check the manual instruc ons. Check www.esciencelabs.com for updates and ps. Contact us for technical support by phone at 1-888-ESL-Kits (1-888-375-5487) or by email at Help@esciencelabs.com. • Read and understand all labels on chemicals. If you have any ques ons or concerns, refer to the Material Safely Data Sheets (MSDS) available at www.esciencelabs.com. The MSDS lists the dangers, storage requirements, exposure treatment...
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...Biology Units 3 &4 Notes -Chapter 1- The Chemical Nature of Cells | |Protein |Carbohydrates |Fats |Nucleic acid | |Monomer |Amino acids |Monosaccharaide |Fatty acids, glycerol |Nucleotide | |Example |2o Amino acids |Glucose, Fructose, Ribose |Triglycerides |Adenine, Cytosine, Guanine | | | | |Steroids, Phospholipids |&Thymine/ Uracil | |Diagram | | | | | | | | | | | | | | | | | | | | | | | |Bonding (how units combine – |1st structure-strong covalent |Strong covalent glycoside |Rarely ever forms polymer |covalent bonds b/w sugar | |polymers ...
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...AS Biology Unit 1 page 1 AQA AS Biology Unit 1 Contents Specification Biological Molecules Chemical bonds Carbohydrates Lipids Proteins Biochemical Tests Enzymes Eukaryotic Cells Prokaryotic Cells Cell Fractionation Microscopy The Cell Membrane Movement across Cell Membranes Exchange The Gas Exchange System Lung Diseases The Heart Coronary Heart Disease The Digestive System Cholera Lifestyle and Disease Defence against Disease Immunisation Monoclonal Antibodies 1 – Mathematical Requirements 2– The Unit 1 Exam 2 4 6 8 10 16 17 24 28 30 31 35 37 44 46 50 54 58 60 67 68 72 80 81 83 86 Cells Human Physiology Disease Appendices These notes may be used freely by A level biology students and teachers, and they may be copied and edited. Please do not use these materials for commercial purposes. I would be interested to hear of any comments and corrections. Neil C Millar (nmillar@ntlworld.co.uk) Head of Biology, Heckmondwike Grammar School High Street, Heckmondwike, WF16 0AH July 2011 HGS Biology A-level notes NCM/7/11 AS Biology Unit 1 page 2 Biology Unit 1 Specification Biochemistry Biological Molecules Biological molecules such as carbohydrates and proteins are often polymers and are based on a small number of chemical elements. • Proteins have a variety of functions within all living organisms. The general structure of an amino acid. Condensation and the formation of peptide bonds linking together amino acids to form polypeptides. The relationship...
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