Name: Mohammad Ali Muzzammil
Group: D
Instructor: Dr. Tayabba Noor
Course: Organic Chemistry
Date: 10th November 2014
Biocatalysis
Abstract
Biocatalysis is basically two words joined together; Bio and Catalysis. “Bio” prefix denotes biological and “catalysis” means the acceleration of a chemical reaction due to a catalyst. So in general biocatalysis is the use of biological (natural) catalysts, such as enzymes. These biological catalysts are used to transform organic compounds chemically. An enzyme is a protein catalyst that is responsible for the reactions in your body. Enzymes help with digestion of food, production of essential nutrients, movement of muscles, etcetera. Enzymes not only exist in our body but are used for quite a lot of other
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They have been used since hundreds of years for the production of alcohol and the fermentation of cheese through the enzymatic breakdown of the proteins in milk. Science has excelled over the past few years. This has led to a better understanding of the “protein structure-function relationship” which has augmented the range of biocatalytic applications. Rational design, in chemical biology and biomolecular engineering, is the strategy of creating new molecules with a specific functionality, based upon the ability to forecast how the molecule's structure will affect its behavior through physical models. Rational designs are related to biocatalysts because it directs evolution which results in very specific protein variants for the enzyme. The enzyme can therefore be engineered to have the desired properties. These properties include stability, activity, selectivity and the substrate specificity. In the present era, Biocatalysis is being implemented in chemical, agricultural, pharmaceutical and food industries. Despite being used on such a scale, the true potential of Biocatalysis is yet to be …show more content…
Oxidases, peroxidase, oxygenases, dehydrogenases
Transferases Required for the catalysis of group transfer reactions. Glycosyltransferases, tansaminases, transketolases, acyltransferases
Hydrolases Provides catalysis for hydrolytic reactions. Lipases, protease, esterases, glycosidases, phosphatases
Lyases Catalyze nonhydrolytic removal of groups. Decarboxylases, ketolasesm dehydrateses, aldolases, hydratases
Isomerases Catalysis of isomerization reactions. Racemases, isomerases, epimerases,
Ligases Catalyze the synthesis of various kinds of bonds with the help of energy containing molecules. Carboxylases, synthetases
Table 3: Enzyme classification
Oxidoreductases
They catalyze the oxidation and reduction reactions that take place within the cell. They are very desirable in the industry because of their ability to catalyze specific types of reactions. They, however, need expensive cofactors.
Transferases
These enzymes catalyze the transfer of functional groups such as methyl, glycosyl, hydroxymethy and etcetera. They are not extensively used in industrial processes but ehy are used in some
Example of enzymes involved in biological processes are classified into; oxidoreductases, transferases, hydrolases, lyases, isomerase and ligases. Catalase an oxidoreductase and among the vital enzymes in the body, it catalyses the breakdown of hydrogen peroxide
Cofactor- Molecules that aren’t proteins nor organic, but help make the reaction go faster when they connect to the active site. 9. competitive inhibitor- prohibits the reaction from taking place by going into the enzyme’s active site so the substrate can’t. 10.
Introduction: Enzymes are needed for survival in any living system and they control cellular reactions. Enzymes speed up chemical reactions by lowering the energy needed for molecules to begin reacting with each other. They do this by forming an enzyme-substrate complex that reduces energy that is required for a specific reaction to occur. Enzymes determine their functions by their shape and structure. Enzymes are made of amino acids, it 's made of anywhere from a hundred to a million amino acids, each they are bonded to other chemical bonds.
The products are released from the enzyme surface to regenerate the enzyme for another reaction cycle. The active site has a unique geometric shape that is complementary to the shape of a substrate molecule, similar to the fit of puzzle pieces.
The competitive inhibitor that was added was lactose. We predicted this because competitive inhibitors block and bind to the active site so it will slow down the binding of the desired substrate. An alternative hypothesis that came up was that the reaction of substrate would stay consistent as if no inhibitor was added. The enzyme could reject the inhibitor if it does not fit in the active site, causing the substrate to bind as it normally would. Our results showed that with the addition of lactose, the reaction did slow down a considerably
The third reaction, enzymatic hydrolysis, can be used in neutral environments. It is a non-caustic manner of hydrolyzing, making it ideal for a neutral environment like the human body. With this reaction, lipases hydrolyze triglycerols to free fatty acids, allowing them to move more freely in aqueous environments. The reaction rate of lipase-catalyzed hydrolysis can be enhanced by the inclusion of other substrates such as crown ethers2. Triglycerides are composed of glycerol and three fatty acids and are hydrolyzed by
In every cell there are three main parts: the nucleus, the cytoplasm, and the cell membrane. The nucleus is a spherical body usually located near the center of the cell that contains the genetic code of the cell and its purpose is to serve as the control center. Cytoplasm is the fluid medium for the many molecules and organelles the cell has. The cell membrane is the outer layer that separates the cell from its environment and controls what enters and leaves the cell.
By completing this experiment, knowledge collected about optimal pH in enzymes will help
Catalyse Enzyme Experiment. Enzymes are biological catalysts. They speed up chemical reactions which go on inside living things. Without them reactions would be so slow that life would grind to halt.
Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.
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).
Bio Chem lab Report 04 Enzyme Biochemistry Group Member: Chan Man Jeun Duncan (16002621) Law Sze Man (16000478) Introduction Enzyme is a protein base structure substance in our body. It works at a biocatalyst that will catalyzing the chemical reaction, which helps to speed up the chemical reaction. Enzyme could only function in specific shape, and the shape of enzyme is depending on the environment, therefore it is hard for an enzyme to function well in an extreme environment. The aim of this experiment is to see can the enzyme functions normally in different environment(pH, temperature and salt concentration) via using starch solution, amylase from saliva, 0.5M HCl solution, 0.5M NaOH solution and NaCl solution, and using iodine solution
Introduction 1.1 Aim: To determine the kinetic parameters, Vmax and Km, of the alkaline phosphatase enzyme through the determination of the optimum pH and temperature. 1.2 Theory and Principles (General Background): Enzymes are highly specific protein catalysts that are utilised in chemical reactions in biological systems.1 Enzymes, being catalysts, decrease the activation energy required to convert substrates to products. They do this by attaching to the substrate to form an intermediate; the substrate binds to the active site of the enzyme. Then, another or the same enzyme reacts with the intermediate to form the final product.2 The rate of enzyme-catalysed reactions is influenced by different environmental conditions, such as: concentration
By observing figure 3, the more enzyme that is available, the faster the reaction rate is. The optimal enzyme concentration was chosen based on the R2 values from figure 2. The highest observable rate also had the best R2 number, which was closest to one. This enzyme concentration was used in part 2.
They can only quicken reactions that will eventually occur, but this enables the cell to have a productive metabolism, routing chemicals through metabolic pathways. Enzymes are very specific for the reactions they catalyze; they make sure the chemical processes go in the cell at any given time. Peroxidase was the enzyme being testing in this experiment. A peroxidase is an enzyme that acts as catalysts, which occurs in biological systems. Peroxidase is found in plants, which they play a role in helping to minimize damage caused by stress factors or insect pests.