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Core Concepts of Biochemical Engineering

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Core Concepts of Biochemical Engineering
Biochemistry
MicroBiology
Chemical Engineering

Published in: Engineering
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Core Concepts of Biochemical Engineering

  1. 1. Core Concepts of Biochemical Engineering Presented by: Raja Wajahat
  2. 2. Introduction Biotechnology  Biotechnology is the art and science of converting reactants into useful products by the action of microorganisms or enzymes. Examples:  production of a particular chemical, production of better plants/seeds, use of specially designed organisms to degrade wastes Bio-processing  Any process in which microorganisms play an essential role in getting transformation of feed into useful products is called as bio- processing. 2 Presented by Raja Wajahat
  3. 3. Biochemical Engineering  Biochemical Engineering is the extension of chemical engineering principles to systems using a biological catalyst to bring about desired chemical transformations.  It is usually divided into biochemical reaction engineering and bio separations.  Biochemical Engineering is an important area in modern biotechnology. 3 Presented by Raja Wajahat
  4. 4. Biochemical Engineering  Cells culture be scaled up, biological products be separated, purified and prepared on a large scale.  Biochemical engineering is expected to carry out the above tasks and to bring about huge economic benefits in realizing sustainable development. 4 Presented by Raja Wajahat
  5. 5. Biochemical Engineering  It is the key to biotechnology development to intensify the researches into biological reactorsand the separation, purification technologies for biological products.  And biochemical engineering has been playing an increasingly important role in the above research fields. 5 Presented by Raja Wajahat
  6. 6. Difference between bioprocess and biochemical engineering  In addition to chemical engineering, bioprocess engineering would include the work of mechanical, electricaland industrial engineers to apply the principles of their disciplines to processes based on using living cells.  Biologists and Engineers differ in their approach to research 6 Presented by Raja Wajahat
  7. 7. Difference between bioprocess and biochemical engineering  In life sciences, mathematicaltheories and quantitative methods (except statistics) have played a secondary role.  Results are qualitative and descriptive models are formulated and tested.  However, biologists are very strong with respect to laboratory tools and interpretation of laboratory data from complex systems. 7 Presented by Raja Wajahat
  8. 8. Difference between bioprocess and biochemical engineering  Engineers possess good background in the physical and mathematical sciences  Quantitative models and approaches even to complex systems are strengths  The skills of engineer and life scientist are complimentary 8 Presented by Raja Wajahat
  9. 9. Traditional and Modern Applications of Biotechnology/Bio-processing Traditional  Foods, bakery products, beverages, wine from fruit juices, fermentation of milk to make curd Modern  Commercial production of antibiotics, vaccines, fermented foods, organic acids etc. 9 Presented by Raja Wajahat
  10. 10. Biochemistry Presented by Raja Wajahat 10
  11. 11. What is Biochemistry?  Study of life cyclic processes in terms of chemicals  How life cycle proceeds with mutual cooperation of various activities of living beings  Energy is released by breaking of the high energy storing molecules usually phosphate containing molecules  Oxidation of NADH (nicotinamide adenine dinucleotide ) in the mitochondria is one of the main reactions 11 Presented by Raja Wajahat
  12. 12. Biochemistry  Some of the chemical/biochemicalreactionsin the living organisms are facilitated by another type of compounds called enzymes  Facilitation of a reaction is called as catalysis  Hence enzymes are called as biocatalysts or biological catalysts  Cells themselves contain some of the enzymes 12 Presented by Raja Wajahat
  13. 13. Biochemistry  Living organisms contain various bimolecules which are the building blocks of the cell and also help in storing and releasing energy for biotransformations  Living organisms contain a large number of bimolecules and they are essentially composed of carbon and nitrogen. The bimolecules have high molecular weights and are complex in structure  They include carbohydrates, lipids, proteins, nucleic acids, vitamins etc. 13 Presented by Raja Wajahat
  14. 14. Important Biomolecules  Carbohydrates  Lipids  Proteins  Nucleic acids Presented by Raja Wajahat 14
  15. 15. Carbohydrates  Carbohydrates are made from monomers called monosaccharides.  Some of these monosaccharides include glucose (C6H12O6), fructose (C6H12O6), and deoxyribose (C5H10O4).  When two monosaccharides undergo dehydration synthesis, water is produced, as two hydrogen atoms and one oxygen atom are lost from the two monosaccharides' hydroxyl group. Presented by Raja Wajahat 15
  16. 16. Carbohydrates Presented by Raja Wajahat 16
  17. 17. Carbohydrates Presented by Raja Wajahat 17
  18. 18. LIPIDS  Lipids are usually made from one molecule of glycerol combined with other molecules.  In triglycerides, the main group of bulk lipids, there is one molecule of glycerol and three fatty acids.  Fatty acids are considered the monomer in that case, and may be saturated (no double bonds in the carbon chain) or unsaturated (one or more double bonds in the carbon chain). 18 Presented by Raja Wajahat
  19. 19. LIPIDS  Lipids, especially phospholipids, are also used in various pharmaceuticalproducts,  either as co-solubilisers (e.g., in parenteralinfusions) or  else as drug carrier components (e.g., in a liposome or transfersome). 19 Presented by Raja Wajahat
  20. 20. LIPIDS Presented by Raja Wajahat 20
  21. 21. LIPIDS  Class of compoundswhich are fatty/oily in nature and present in cells and tissues  In addition to fats and oils, some other biological materials including waxes, cholesteroland some vitamins and hormones are also classified as lipids.  Generalstructure of fats and oils  Triglycerides are formed due to the reaction of alcohol glycerol and long chain fatty acids such as stearic acid 21 Presented by Raja Wajahat
  22. 22. Lipid Structure Presented by Raja Wajahat 22
  23. 23. Characteristics of Lipids  Insoluble in water  Soluble in non-polar solvents including hexane, chloroform etc  Release a lot of energy on breakdown and therefore considered as the energy storage media  Contain a large proportion of C-H bonds  Upon saponification, release fatty acids and glycerol  They are synthesized by the cells from sugars  Some lipid compounds such as vitamins and hormones have intense biological activity 23 Presented by Raja Wajahat
  24. 24. Characteristics of Lipids  As bimolecules, they are constituted of cells wall and form a protective coating to the cell and encourage some species.  They are also energy carriers and release energy as and when cell requires it 24 Presented by Raja Wajahat
  25. 25. Characteristics of Lipids  Lipids also include a heterogeneousgroup of structuralcomponent.  Some lipids are combined with other classes of compounds and they are known as:  Lipoproteins,  Proteolipids,  Lipoamino acids,  Phosphatidopeptides,  Lipopolysaccharides 25 Presented by Raja Wajahat
  26. 26. Proteins  Proteinsare very large molecules – macro-biopolymers – made from monomers called amino acids.  There are 20 standard amino acids, each containing a carboxylgroup, an amino group, and a side-chain (known as an "R" group).  The "R" group is what makes each amino acid different, and the properties of the side-chains greatly influence the overall three- dimensional conformation of a protein.  When amino acids combine, they form a special bond called a peptide bond through dehydration synthesis, and become a polypeptide, or protein. Presented by Raja Wajahat 26
  27. 27. Proteins Presented by Raja Wajahat 27
  28. 28. Proteins Presented by Raja Wajahat 28
  29. 29. Proteins  In order to determine whether two proteins are related, or in other words to decide whether they are homologous or not, scientists use sequence-comparison methods.  Methods like SequenceAlignments and StructuralAlignments are powerful tools that help scientists identify homologies between related molecules.  The relevance of finding homologies among proteins goes beyond forming an evolutionary pattern of protein families.  By finding how similar two protein sequences are, we acquire knowledge about their structure and therefore their function. Presented by Raja Wajahat 29
  30. 30. Nucleic acids  Nucleic acids are the molecules that make up DNA, an extremely important substance that all cellular organisms use to store their genetic information.  The most common nucleic acids are deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).  Their monomers are called nucleotides.  A nucleotide consists of a phosphate group, a ribose sugar, and a nitrogenous base. Presented by Raja Wajahat 30
  31. 31. Nucleic acids  The phosphate group and the sugar of each nucleotide bond with each other to form the backbone of the nucleic acid, while the sequence of nitrogenous bases stores the information.  The most common nitrogenous bases are adenine, cytosine, guanine, thymine, and uracil. Presented by Raja Wajahat 31
  32. 32. Nucleic acids  The nitrogenous bases of each strand of a nucleic acid will form hydrogen bonds with certain other nitrogenous bases in a complementary strand of nucleic acid (similar to a zipper).  Adenine binds with thymine and uracil; Thymine binds only with adenine; and cytosine and guanine can bind only with one another. Presented by Raja Wajahat 32
  33. 33. Nucleic acids Presented by Raja Wajahat 33
  34. 34. GENERALIZED VIEW OF BIOPROCESS RAW MATERIALS UPSTREAM PROCESSES Inoculum Preparation Equipment Sterilization BIOREACTOR - FERMENTER Reaction Kinetics and Bioactivity Transport Phenomena and Fluid Properties DOWNSTREAM PROCESSES Separation Recovery and Purification THE BOTTOM LINE REGULATIO N ECONOMIC S HEALTH AND SAFETY Waste Recovery, Reuse and Treatment Instrumenta tion and Control Media Formulation and Sterilization 34 Presented by Raja Wajahat
  35. 35. Microbiology Presented by Raja Wajahat 35
  36. 36. Microbiology  Microbiology is the study of microscopic organisms, those being unicellular (single cell), multicellular (cell colony), or acellular (lacking cells).  Microbiology encompasses numerous sub-disciplines including virology, mycology, parasitology, and bacteriology. 36 Presented by Raja Wajahat
  37. 37. Microbiology  Eukaryotic micro-organisms possess membrane-bound cell organelles and include fungi and protists, whereas prokaryotic organisms— which all are microorganisms—are conventionally classified as lacking membrane-bound organelles and include eubacteria and archaebacteria.  Microbiologists traditionally relied on culture, staining, and microscopy.  However, less than 1% of the microorganisms present in common environments can be cultured in isolation using current means Microbiologists often rely on extraction or detection of nucleic acid, either DNA or RNA sequences. 37 Presented by Raja Wajahat
  38. 38. Microbiology  Viruses have been variably classified as organisms, as they have been considered either as very simple microorganisms or very complex molecules.  Prions, never considered microorganisms, have been investigated by virologists, however, as the clinical effects traced to them were originally presumed due to chronic viral infections, and virologists took search—discovering "infectious proteins". 38 Presented by Raja Wajahat
  39. 39. Microbiology  As an application of microbiology, medical microbiology is often introduced with medical principles of immunology as microbiology and immunology.  Otherwise, microbiology, virology, and immunology as basic sciences have greatly exceeded the medical variants, applied sciences 39 Presented by Raja Wajahat
  40. 40. Microbiology  Study of microscopic organisms  Important branch of science As a basic biological science  Deals with nature of life processes and principles behind, genetics As an applied biological science  Study of useful as well as pathogenic microorganisms 40 Presented by Raja Wajahat
  41. 41. Why microbiology is important?  In biochemical engineering  To understand and analyze the process of biotechnology  Design and operate different units in rational a way  Therefore, a basic knowledge of cell growth and function is required  A living microorganism may be conceptualized as a chemical reactor (take nutrients from environment, grows, reproduces and releases products)  Products formed and released during cellular activities could be commercially important 41 Presented by Raja Wajahat
  42. 42. Why microbiology is important? Rates of nutrient utilization, growth and release of products depends upon:  Type of the cells involved  Temperature  Composition of media etc.  Quantitative understandingof biological systems (correlation of friction factor and Reynolds No.)  Understanding above interactionsrequires a foundation built on microbiology and biochemistry 42 Presented by Raja Wajahat
  43. 43. Industrial Microbiology  Study of the exploitation of the biochemical potentialof microbes for the production of various products  Antibiotics, vaccines, steroids, solvents, vitamins etc.  Developments of new products using genetic engineering 43 Presented by Raja Wajahat
  44. 44. What Are Microorganisms?  Microorganisms are actually a diverse group of organisms.  The fact that they’re micro isn’t even true of all microorganisms  some of them form multicellular structures that are easily seen with the naked eye Presented by Raja Wajahat 44
  45. 45. What Are Microorganisms? There are four main kinds of microorganisms, based on evolutionary lines:  Bacteria are a large group of unicellular organisms that scientists loosely group as Gram-negative and Gram-positive, but in reality there are many different kinds.  The bacteria and archaea are often talked about together under the heading of “prokaryotes”because they lack a nucleus. They do share a few characteristics and aren’t easily distinguished from one another at first, but they are distinct groups. Presented by Raja Wajahat 45
  46. 46. What Are Microorganisms?  Archaea are another group of unicellular organisms that evolved along with bacteria severalbillion yearsago.  Many are extremophiles, meaning that they thrive in very hot or very acidic conditions.  Archaea are more closely related to eukaryotes than to bacteria. Presented by Raja Wajahat 46
  47. 47. What Are Microorganisms?  Eukaryotic microorganisms are a structurally diverse group that includes protists, algae, and fungi.  They all have a nucleus and membrane-bound organelles, as well as other key differences from bacteria and archaea.  All the rest of the multicellular organisms on earth, including humans, have eukaryotic cells as well. Presented by Raja Wajahat 47
  48. 48. What Are Microorganisms? Presented by Raja Wajahat 48
  49. 49. What Are Microorganisms?  Viruses are smaller than bacteria and are not technically alive on their own — they must infect a host cell to survive.  Viruses are made up of some genetic material surrounded by a viral coat, but they lack all the machinery necessary to make proteins and catalyze reactions.  This group also includes subviral particles and prions, which are the simplest of life forms, made of naked ribonucleic acid (RNA) or simply protein. Presented by Raja Wajahat 49
  50. 50. Genetic Engineering 50 Presented by Raja Wajahat
  51. 51. Microscopy  Microorganisms are measured in smaller units such as microns, nanometers, mill microns andAngstrom  Various microscopes  Difference betweenordinary and electron microscope 51 Presented by Raja Wajahat
  52. 52. Range of microscopic measurements 52 Presented by Raja Wajahat
  53. 53. Building block of organisms  All living organisms are composed of cells  What is true for Escherichia coli is true for elephants  Cells are b/w 1 and 50 micrometer in diameter  Basic components of living cell  Cytoplasm  Cell membrane  Nucleus  Ribosome 53 Presented by Raja Wajahat
  54. 54. Cell Nucleus (DNA Structure) 54 Presented by Raja Wajahat
  55. 55. Cell components 55 Presented by Raja Wajahat
  56. 56. DNA DNA determines  Heredity  Cell reproduction  Protein synthesis When DNA is damaged by foreign substances, various toxic effects, including:  Mutations  Cancer  Birth effects  Defective immune system 56 Presented by Raja Wajahat
  57. 57. Cell Membrane  Acts as a barrier from externalenvironment  It closes the cell and regulates the passage of ions, nutrients, metabolic products and fat soluble substances into and out of it  It is composed of phospholipid bilayer about 8 nm thick  Highly selective membrane enabling the cell to concentrate specific metabolites and excrete waste  A number of complex transformation takes place across the membrane 57 Presented by Raja Wajahat
  58. 58. Cytoplasm 58 Presented by Raja Wajahat
  59. 59. Cytoplasm  Colloidal in nature  Thick semi-transparent and has higher water contents  It contains:  Hydrophilic components (protein particles, carbohydrates and salts)  Hydrophobic components (lipids or fats)  Main function of cytoplasm is absorption and excretion 59 Presented by Raja Wajahat
  60. 60. Prokaryotes and Eukaryotes Prokaryotic cell  Genetic material is not enclosed within the membrane  Cell walls contain complex polysaccharide peptidoglycan  Simple method of reproduction  Size is usually 0.5 to 3 micrometer in diameter Eukaryotic cell  Eukaryote means true nucleus  Genetic material enclosed in a specialized membrane  They are larger and more complex than prokaryotes  Size range from 2 to 200 micrometer 60 Presented by Raja Wajahat
  61. 61. Applications of Prokaryotes  Metabolically the most diverse of all living systems  Responsible for most degradation processes  Can be grown aerobically and anaerobically  Form a wide range of organic products (this property has both positive and negative impact on society) 61 Presented by Raja Wajahat
  62. 62. Applications of Prokaryotes Positive  represent a massive resource of biocatalysis for the biotransformation of organic materials and the degradation of herbicides, insecticides and other man-made chemicals Negative  Represent the principal agents causing the deterioration of biomaterial e.g food and wood and are major hazards to public health (food poisoning and other diseases) 62 Presented by Raja Wajahat
  63. 63. Classification of organisms  Classified according to their structure and function  Divided into three kingdoms  Plants  Animals  Protists (Neither plants nor animals) Most are unicellular but some have many cells Cells have a membrane around the nucleus (eukaryotes) 63 Presented by Raja Wajahat
  64. 64. Classification of organisms  Classifications show differences in several characteristics including:  Energy and nutritional requirements  Rates of growth and product release  Method of reproduction  Morphology 64 Presented by Raja Wajahat
  65. 65. Classification of organisms 65 Presented by Raja Wajahat
  66. 66. Naming the microorganisms  They are named in Latin using binary nomenclature  First name represents the group or genus  Second name represents the species  Escherichia coli C600  National collection of industrial and marine bacteria (NCIMB)  American type culture collection (ATCC)  Strain (A strain is a subset of a bacterialspecies differing from other bacteria of the same species by some minor but identifiable difference) 66 Presented by Raja Wajahat
  67. 67. Escherichia coli (E. coli)  Escherichia coli (E. coli) chosen as a test microorganism.  E. coli is currently the most specific indicator for faecal contamination of a water source and therefore it is considered as a model organism in laboratory research.  The cells are about 2 μm long and 0.5 μm in diameter, with a cell volume of 0.6 – 0.7 μm3 (Kubitschek, 1990). Presented by Raja Wajahat 67
  68. 68. Escherichia coli (E. coli) Presented by Raja Wajahat 68
  69. 69. Escherichia coli (E. coli)  Optimal growth of E. coli occurs at 37ºC. Under a microscope,  E. coli is a rod-shaped prokaryotic cell which has a long, rapidly rotating flagellum (tail) used for movement.  A strain of E. coli is a sub-group within the species that has unique characteristics that distinguish it from other E. coli strains. 69 Presented by Raja Wajahat
  70. 70. Escherichia coli (E. coli)  These differences are often detectable on the molecular level and may result in changes to the physiology or life cycle of the bacterium.  For example, a strain may gain pathogenic capacity or the ability to resist antimicrobial agents.  Different strains of E. coli are often host-specific, making it possible to determine the source of faecalcontamination in environmental samples. 70 Presented by Raja Wajahat
  71. 71. Different Bacteria Pseudomonas aeruginosa (P. aeruginosa)  is a gram-negative rod shaped free living bacteriumthat is ubiquitous in the environment Staphylococcus aureus (S. aureus)  is a gram positive bacteriumusually arranged in grape like irregular clusters.  Although it occurs widely in the environment it is found mainly on skin and the mucous membranes of animals. 71 Presented by Raja Wajahat
  72. 72. Different Bacteria  S. aureus can be released into environments including swimming pools, spa pools and other recreationalwatersby human contact. Legionella pneumophila (L. pneumophila)  is a gram negative rod shaped bacterium. 72 Presented by Raja Wajahat
  73. 73. Yeasts Rhodosporidium turoloides (R. turoloides)  Y4 is oil producing or oleaginous yeast (Wu et al. 2011).  Since these species contain intracellular valuable compounds such as lipids, therefore the disruption of this yeast would be interesting in order to release the lipids contained in vacoules within the yeast cell.  Once the lipids are released biodiesel could be produced via a conventionaltrans-esterification process. 73 Presented by Raja Wajahat
  74. 74. Enzymes Presented by Raja Wajahat 74
  75. 75. What are Enzymes?  Enzymes are biological catalysts and are one of the essential components of all living systems  Biochemical reactions occur rapidly through the mediation of natural catalysts called enzymes  Enzymes are bimolecules that catalyze (increase the rates of) chemical reactions  Enzymes have a key role in catalysing the chemical transformations that occur in all cell metabolism without themselves undergoing any overall change 75 Presented by Raja Wajahat
  76. 76. Enzymes  Some generic terms associated with enzymology:  Cofactor:the non-protein content of enzyme  Coenzyme: an enzyme with organic molecules as its cofactor  Haloenzyme: an active enzyme including cofactor  Apoenzyme: the inactive portion of protein  The nature and specificity of their catalytic activity is basically due to the three dimensional structure of folded protein (determined by the sequence of amino acids) 76 Presented by Raja Wajahat
  77. 77. Classification of Enzymes  Enzymes are usually named in terms of the reactionsthat are catalysed  Usual practice is to add ‘ase’to the major part of the name of the substrate e.g Urease, Urginase (urginine)  Enzymes are also classified by groups that catalyse similar reactions (see slide 17) 77 Presented by Raja Wajahat
  78. 78. Properties of enzymes  The catalytic activity of enzymes differs from that of other catalysts Efficiency  Turn over number= molecules reactedper catalytic site per unit time  Turn over number for enzymes at room temperatureare usually much higher than for industrial chemical catalysts 78 Presented by Raja Wajahat
  79. 79. Specificity of enzymes Specificity  A characteristic featureof enzymes is that they are specific in action, some showing complete specificity for only one type of molecule  If a substance exists in two stereochemicalforms, L and D isomers, enzymes may recognize only one of the two forms for example glucose oxidase will oxidise D(+) glucose only and no other hexose isomer. 79 Presented by Raja Wajahat
  80. 80. Specificity of enzymes  Active centre/Active site  A catalyst site on the molecule is called active site/active centre. Such sites constitute only a small proportion of the total volume of the enzyme and are located on or near the surface.  The active site is usually a very complex physico-chemical space, creating microenvironments in which the binding and catalytic areas can be found.  The forces operating at the active centre can involve Charge, hydrophobicity, hyfrogen bonding and redox processes 80 Presented by Raja Wajahat
  81. 81. How the biological catalysts work? A reaction proceedsaccordingto the two possible theories Collision theory Proposes that reactions take place by the collision of the reactantmolecules. More is the concentration of the reactants, more are the chances for the reactants to collide and hence more will be the rate of reaction. However, all collisions may not necessarily result in the reaction to proceed to produce products 81 Presented by Raja Wajahat
  82. 82. How the biological catalysts work? Transition state theory Propose that the collision of certain molecules which have crossed certain potentialenergy barrier alone will result in the reaction to take place. This potentialenergy barrier is known as activation energy 82 Presented by Raja Wajahat
  83. 83. Biological catalysts  Like all catalysts, enzymes work by lowering the activation energy for a reaction thus increasing the reaction rate  Not consumed by the reaction  Do not alter the equilibrium  Enzymes differ from most other catalysts by being much more specific  Enzymes are know to catalyze about 4000 biochemical reactions 83 Presented by Raja Wajahat
  84. 84. Types of specificity  Depending upon the reaction conditions and the specific nature of t5he enzymes, the enzymatic catalytic process exhibits different kinds of specificity including;  Group specificity  Stereochemicalspecificity  Product specificity  Substrate specificity 84 Presented by Raja Wajahat
  85. 85. Enzymatic process 85 Presented by Raja Wajahat
  86. 86. Enzyme specificity hypothesis  Several hypothesis have been proposed to explain the enzyme specificity in catalytic activity and its ability to interact with the substrates  Fischer lock and key hypothesis It was proposed by Fischer in 1890 who conceived the concept of ‘complementary structuralfeatures’between the enzyme and the substrate 86 Presented by Raja Wajahat
  87. 87. Fischer lock and key hypothesis The catalytic process is brought about because the substrate fits into the complementary site on the enzyme just as key fits into the lock Thus, the reacting group of the substrate gets struck with the catalytic site of the enzyme Similarly, the binding groups attach to the binding sites in the enzyme Hypothesis has been successful in explaining many features of the enzyme specificty 87 Presented by Raja Wajahat
  88. 88. Fischer lock and key hypothesis 88 Presented by Raja Wajahat
  89. 89. Fischer lock and key hypothesis Drawback  Could not explain some of the conformationalchanges taking place in the enzymes when they come in contact with the substrate  An enzyme may not be having exactly complementary feature that is compatible to the substrate, but still there are cases where reaction have taken place 89 Presented by Raja Wajahat
  90. 90. Fischer lock and key hypothesis Drawback  X-ray diffraction analysis and some spectroscopic analysis have shown differences in the structures of free enzymes and substrate bound enzymes.  This was explained by Koshland in 1958 with his Koshland induced-fit hypothesis 90 Presented by Raja Wajahat
  91. 91. Koshland induced-fit hypothesis 91 Presented by Raja Wajahat
  92. 92. Koshland induced-fit hypothesis  This hypothesis proposes that the structure of the substrate may not be complementary to the enzyme in its native format,  but it is complementary to the active site in the substrate-enzyme complex.  Both the enzyme and the substrate change their structure slightly to accommodate each other. 92 Presented by Raja Wajahat
  93. 93. Versatility Enzymes catalysis is shown by the type of reactions that can be catalysed. Six groups of enzymes are recognized according to their reactivity 1. Oxidoreductase……….oxidation-reduction reactions 2. Transferases…..transfer of atom b/w two molecules 3. Hydrolases……..hydrolysis reactions 4. Lyases…………….removal of a group from a substrate 5. Isomerases……..isomerisation reactions 6. Ligases……………catalyse the synthesis of various types of bonds where the reactions are coupled with breakdown of energy-containing materials such as ATP 93 Presented by Raja Wajahat
  94. 94. Difference b/w catalyst and enzyme Function:  Catalysts are substances that increase or decrease the rate of a chemical reaction but remain unchanged.  Enzymes are proteins that increase rate of chemical reactions converting substrate into product. Molecularweight:  Low molecular weight compounds.  High molecular weight globular proteins. 94 Presented by Raja Wajahat
  95. 95. Difference b/w catalyst and enzyme Types:  There are two types of catalysts – positive and negative catalysts.  There are two types of enzymes - activation enzymes and inhibitory enzymes. Alternate terms:  Inorganic catalyst. Organic catalyst or bio catalyst. Nature:  Catalysts are simple inorganic molecules  Enzymes are complex proteins 95 Presented by Raja Wajahat
  96. 96. Difference b/w catalyst and enzyme Reactionrates:  Typically slower Several times faster Specificity:  They are not specific and therefore end up producing residues with errors Enzymes are highly specific producing large amount of good residues Conditions:  High temp, pressure  Mild conditions, 96 Presented by Raja Wajahat
  97. 97. Difference b/w catalyst and enzyme  Enzymes are proteins, which act as catalysts.  Enzymes lower the energy required for a reaction to occur, without being used up in the reaction.  Many types of industries, to aid in the generation of their products, utilize enzymes.  Examples of these products are; cheese, alcohol and bread. 97 Presented by Raja Wajahat
  98. 98. Fermentation  Fermentation is a method of generating enzymes for industrial purposes.  Fermentation involves the use of micro organisms, like bacteria and yeast to produce the enzymes.  There are two methods of fermentation used to produce enzymes. 98 Presented by Raja Wajahat
  99. 99. Fermentation  These are submerged fermentation and solid-state fermentation.  Submerged fermentation involves the production of enzymes by microorganisms in a liquid nutrient media.  Solid-state fermentation is the cultivation of microorganisms, and hence enzymes on a solid substrate. 99 Presented by Raja Wajahat
  100. 100. Enzymes  Carbon containing compounds in or on the substrate are broken down by the micro organisms, which produce the enzymes either intracellular or extracellular.  The enzymes are recovered by methods such as centrifugation, for extracellular produced enzymes and lysing of cells for intracellular enzymes. 100 Presented by Raja Wajahat
  101. 101. Enzymes  Many industries are dependent on enzymes for the production of their goods.  Industries that use enzymes generated by fermentation are the brewing, wine making, baking and cheese making 101 Presented by Raja Wajahat
  102. 102. Immobilization of Enzymes Presented by Raja Wajahat 102
  103. 103. Immobilized Enzymes  The remarkable catalytic properties of enzymes make them very attractive for use in processes where mild chemical conditions and high specificity are required.  Cheese manufacture has traditionally used rennet, an enzyme preparation from calf stomach, as a specific protease which leads to the precipitation of protein from milk. 103 Presented by Raja Wajahat
  104. 104. Immobilized Enzymes  ‘Mashing’ in the malting of grain for the brewing of beer makes use of pamylase from germinating grain to hydrolyse starch to produce sugars for the fermentation  stage. In both of these examples the enzymes are not recovered from the reaction mixture and a fresh preparation is used for each batch. 104 Presented by Raja Wajahat
  105. 105. Immobilized Enzymes  Similarly, in more modern enzyme reaction applications, such as in biological washing detergents, the enzyme is discarded after single use but there are, however, situations where it may be desirable to recover the enzyme.  This may be because the product is required in a pure state or that the cost of the enzyme preparation is such that single use would be uneconomic. 105 Presented by Raja Wajahat
  106. 106. Immobilized Enzymes  To this end, immobilized biocatalysts have been developed where the original soluble enzyme has been modified to produce an insoluble material which can be easily recovered from the reaction mixture.  Many industrially important micro-organisms tend to agglomerate during their growth and form flocs suspended in the culture medium or films which adhere to the internal surfaces of the fermenter. 106 Presented by Raja Wajahat
  107. 107. Immobilized Enzymes  This tendency may or may not be advantageous to the process and is dependent on a variety of parameters such as the pH and ionic strength of the medium and the shear rate experienced in the growth vessel.  In some cases the formation of substantial flocs is essential to the proper operation of the process. 107 Presented by Raja Wajahat
  108. 108. Immobilized Enzymes  In the case of the activated sludge waste water treatment the settling properties of the flocculated micro-organisms are utilized in order to produce a concentratedstreamof biomass for the recycle.  The so-called ‘trickling filter’, also in widespread use in waste-water treatment, is reliant on the formation of a film of organisms on the surfaces of its packing material.  The operation is not that of a filter, in which material would be removed on the basis of its particle size, but that of a biological reactor in which the waste material forms the substrate for the growth of the microbes. 108 Presented by Raja Wajahat
  109. 109. Immobilized Enzymes  The presence of the film provides a means of retaining a higher microbial concentration in the reactor than would be retained in a comparable stirred-tank fermenter.  The formation of flom and films for the retention of high microbial densities or to facilitate separation of microbes from the growth medium may be desirable in other instances as well.  However, in some cases the microbe used may neither be amenable to the natural formation of large flocs nor adhere as surface films, and recourse may be made to the artificial immobilization of microbes. 109 Presented by Raja Wajahat
  110. 110. Immobilization techniques  There are various methods which have been developed for enzyme and microorganism immobilization and some of these have found commercial application.  The two largest scale industrial processes utilizing immobilized enzymes are the hydrolysis of benzyl penicillin by penicillin acylase and the isomerisation of glucose to a glucose-fructose mixture by immobilized glucose isomerase.  The immobilization techniques used in general may be broadly categorized as: 110 Presented by Raja Wajahat
  111. 111. Immobilization techniques (a) Physical adsorption on to an inert carrier.  The first of these methods has the advantage of requiring only mild chemical conditions so that enzyme deactivation during the immobilization stage is minimized.  The natural formation of microbial flocs and films may be considered to be in this category, although the subsequent adhesion of the microbes to the surface may not be a simple phenomenon.  Special materials may be used as supports which provide the microbes with environments which are particularly amenable to their adhesion; 111 Presented by Raja Wajahat
  112. 112. Immobilization techniques  such materials include foam plastics which provide conditions of low shear in their pores.  The process may also be relatively cheap but it does tend to have the drawback that desorption of the enzyme may also occur readily or that the microbial film may slough and be carried into the bulk of the growth medium.  The process is dependent on the nature of the specific enzyme or microbe used and its interaction with the carrier and, whilst it is common in the case of immobilized microbes, it has found only limited application in the case of immobilized enzymes. 112 Presented by Raja Wajahat
  113. 113. Immobilization techniques (b) Inclusion in the lattices of a polymer gel or in micro-capsules.  This method attempts to overcome the problem of leakage by enclosing the relatively large enzyme molecules or microbes in a tangle of polymer gel or to enclose them in a membrane which is porous to the substrate.  It is theoretically possible to immobilize any enzyme or micro- organism using these methods but they too have their problems. Some leakage of the entrapped species may still occur, although this tends to be minimal. 113 Presented by Raja Wajahat
  114. 114. Immobilization techniques  The main problem is due to mass transfer limitations to the introduction of the necessarily small substrate molecules into the immobilized structure, and to the slow outward diffusion of the product of the reaction.  If the substrate is itself a macro-molecule, such as a protein or a polysaccharide, then it will be effectively screened from the enzyme or microbes and little or no reaction will take place. 114 Presented by Raja Wajahat
  115. 115. Immobilization techniques (c) Covalent binding  Biological catalysts may be made insoluble and hence immobilized by effectively increasing their size.  This can be done either by chemically attaching them to otherwise inert carrier materials or by cross linking the individuals to form large agglomerations of enzyme molecules or micro-organisms.  The chemical reagents used for the linking process are usually bifunctional, such as the carbo-di-imides, and many have been developed from those used in the chemical synthesis of peptides and proteins. 115 Presented by Raja Wajahat
  116. 116. Immobilization techniques  The inert carriersused tend to be hydrophilic materials, such as cellulose and its derivatives,  but in some cases the debris of the original cells has been used, the cells having been broken and then crosslinked with the enzyme and each other to form large particles. 116 Presented by Raja Wajahat
  117. 117. Presented by Raja Wajahat 117
  118. 118. Immobilization techniques  The consumption or biotransformation of substrate by immobilized micro-organisms results in most cases in the growth of the micro- organisms.  The growth which gives rise to a significant increase of thickness in an established biofilm, occurs at a rate which is essentially slow in comparison with the rates of the diffusion processes. 118 Presented by Raja Wajahat
  119. 119. Immobilization techniques  Simultaneously, the attrition of biofilms or flocs arising from the effects of fluid flow tends to maintain their thickness or size, and, overall, the immobilized system can be considered to be in a steady state when short time intervals are involved.  The mathematical similarity of enzyme and microbial kinetics then means that a common set of equations can be used to describe the behavior of both immobilized enzymes and microbial cells. 119 Presented by Raja Wajahat
  120. 120. Thank You! Presented by: Raja Wajahat Presented by Raja Wajahat 120

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