ChE 661 Unit One.pptx, Biochemical Engineering
- 1. ChE 661 Biochemical Engineering E. G. Ankudey January, 2021
- 2. Course Content Industrial Microbiology Cell growth Metabolism Thermodynamics and Energetics Membrane Transport Mixing and Oxygen Uptake Enzyme kinetics and immobilized enzyme technology Principles of microbial reaction engineering Design and modelling of biological reactors Mass, heat and momentum transfer in bioreactors Application of bioreactors in food processing, waste water treatment, medicine and pharmaceutical industries
- 3. Introduction Biochemical engineering conducting biological processes on an industrial scale. Link between biological sciences and chemical engineering. Biotechnology Commercial techniques that use living organisms, or substances from those organisms, to make or modify a product Also includes techniques used for the improvement of the characteristics of economically important plants and animals and for the development of microorganisms to act on the environment One of the oldest chemical technologies - Use of micro-organisms to ferment beverage and food. - crossbreeding of plants and animals for better yields.
- 4. Modern biotechnology Recombinant DNA allows the direct manipulation of genetic material of individual cells, which may be used to develop microorganisms that produce new products as well as useful organisms. (Genetic Engineering) Cell fusion process to form a single hybrid cell with nuclei and cytoplasm from two different types of cells in order to combine the desirable characteristics of the two.
- 6. Role of Biochemical Engineer
- 7. Role of Biochemical Engineer to obtain the best biological catalyst for a desired process to create the best possible environment for the catalyst to perform by designing the bioreactor and operating it in the most efficient way to separate the desired products from the reaction mixture in the most economical way
- 8. Advantages Mild reaction conditions The typical condition is at room temperature, atmospheric pressure, and fairly neutral medium pH. As a result, the operation is less hazardous, and the manufacturing facilities are less complex compared to typical chemical processes. Specificity An enzyme is highly specific and catalyzes only one or a small number of chemical reactions. A great variety of enzymes exist that can catalyze a very wide range of reactions.
- 9. Advantages Effectiveness The rate of an enzyme-catalyzed reaction is usually much faster than that of the same reaction when directed by non- biological catalysts. A small amount of enzyme is required to produce the desired effect. Renewable resources The major raw material is biomass Recombinant DNA technology The development of the recombinant DNA technology promises enormous possibilities to improve biological processes
- 10. Disadvantages Complex product mixtures Dilute aqueous environments Contamination Variability
- 12. Microbial cells
- 13. Prokaryotic cell Found in two microbial groups: bacteria and blue-green algae. The cell is small and simple, not compartmentalized by unit membrane systems. The cell has only two structurally distinguishable internal regions: cytoplasm and nuclear region The cytoplasm has grainy dark spots as a result of its content of ribosomes, which are composed of protein and ribonucleic acid (RNA). The ribosome is the site of important biochemical reactions for protein synthesis. The nuclear region is of irregular shape, sharply segregated even though it is not bounded by membrane.
- 15. The nuclear region contains deoxyribonucleic acid (DNA), which contains genetic information The prokaryotic cell is surrounded with a cell wall and a cell membrane. The cell wall, considerably thicker than the cell membrane, protects the cell from external influences. The cell membrane (or cytoplasmic membrane) is a selective barrier between the interior of the cell and the external environment. Prokaryotic cell
- 16. Prokaryotic cell The largest molecules known to cross this membrane are DNA fragments and low-molecular-weight proteins. The cell membrane can be folded and extended into the cytoplasm or internal membranes. The cell membrane serves as the surface onto which other cell substances attach and upon which many important cell functions take place.
- 17. Eukaryotic cell The unit structure in plants, animals, protozoa, fungi, and algae. The eukaryotic cell has internal unit membrane systems that segregate many of the functional components of the cell They are more complex and 1,000 to 10,000 times larger than prokaryotic cells. The nucleus is surrounded by a double membrane with pores 40 to 70 μm wide, containing cytologically distinguishable chromosomes. The nucleus controls hereditary properties and all vital activities of the cell.
- 18. Eukaryotic cell
- 19. The chromosomes are long and threadlike bodies and are found in the nuclei of cells, which contain the genes arranged in linear sequence. The cytoplasm contains large numbers of granules called ribosome, which are involved in continuous reactions to synthesize cell materials. Eukaryotic cell
- 20. The ribosome is especially concentrated along the rough surface of the endoplasmic reticulum The mitochondria contain the electron transport enzymes that utilize oxygen in the process of energy generation. Vacuole and lysosome are organelles that serve to isolate various chemical reactions in a cell. Eukaryotic cell
- 21. Cell Composition cells are composed of high-molecular-weight polymeric compounds proteins, nucleic acids, polysaccharides, lipids, other storage materials (fats, polyhydroxybutyrate, glycogen). inorganic salts (e.g., NH+4 , PO3 -4 , K+ , Ca2+ , Na+ , SO4 2- ), metabolic intermediates (e.g., pyruvate, acetate), vitamins.
- 22. Typical cell composition 50% carbon, 20% oxygen, 14% nitrogen, 8% hydrogen, 3% phosphorus, 1% sulfur, small amounts of K+ , Na+ , Ca2+ , Mg2+ , Cl- , vitamins.
- 23. Cell composition The cellular macromolecules are functional only when in the proper three-dimensional configuration. Each macromolecule is part of an intracellular organelle and functions in its unique microenvironment. Information transfer from one organelle to another (e.g., from nucleus to ribosomes) is mediated by special molecules (e.g., messenger RNA). Most of the enzymes and metabolic intermediates are present in cytoplasm. However, other organelles, such as mitochondria, contain enzymes and other metabolites. A living cell can be visualized as a very complex reactor in which more than 2000 reactions take place. These reactions (metabolic pathways) are interrelated and are controlled in a complicated fashion.
- 24. Proteins most abundant organic molecules in living cells, 40% to 70% of their dry weight. Proteins are polymers built from amino acid monomers. Typical molecular weights of 6000 to several hundred thousand. The amino acids contain at least one carboxyl group and one a-amino group, They differ from each other in the structure of their R groups or side chains.
- 25. Amino acids The building blocks of proteins are α-amino acids, and there are 20 common amino acids. Amino acids are named on the basis of the side (R) group attached to the a-carbon. Amino acids are optically active and occur in two isomeric forms.
- 26. Amino acid structure Only L-amino acids are found in proteins.
- 27. Amino acids Proteins found in nature made from a repertoire of 20 amino acids Basic, aromatic, acidic At low pH, the acidic group is neutral (-COOH) At high pH, it is negatively charged (-COO- ) At intermediate pH, an amino acid has positively and negatively charged groups. Molecule is referred to as zwitterion
- 28. Amino acids
- 29. Amino acids
- 30. Amino acids The pH value at which amino acids have no net charge is called the isoelectric point, It varies depending on the R group of amino acids. At its isoelectric point, an amino acid does not migrate under the influence of an electric field. Knowledge of the isoelectric point can be used in developing processes for protein purification.
- 31. Functions of proteins Structural proteins: glycoproteins, collagen, keratin Catalytic proteins: enzymes Transport proteins: hemoglobin, serum albumin Regulatory proteins: hormones (insulin, growth hormone) Protective proteins: antibodies, thrombin
- 32. Proteins as enzymes The enzymes represent the largest class of proteins. Over 2000 different kinds of enzymes are known. Enzymes are highly specific in their function and have extraordinary catalytic power. Each enzyme’s molecule contains an active site to which its specific substrate is bound during catalysis. Some enzymes are regulated and are called regulatory enzymes. Most enzymes are globular proteins.
- 33. The peptide bond
- 34. Peptide bond The peptide bond is planar. Peptides contain two or more amino acids linked by peptide bonds. Polypeptides usually contain fewer than 50 amino acids. Larger amino acid chains are called proteins. Many proteins contain organic and/or inorganic components other than amino acids. These components are called prosthetic groups, and the proteins containing prosthetic groups are called conjugated proteins Hemoglobin is a conjugated protein and has four heme groups, which are iron-containing organometallic complexes.
- 35. Structure and function Enzyme activity or otherwise modulated by 3 dimensional structure of the protein The sequence of amino acids dictates the structure of the protein
- 36. Levels of structure Primary structure The linear sequence of amino acids in the protein. The unique arrangement of the amino acids determines the three-dimensional structure and hence the function of the protein Only 1st and last residue have amino or carboxylic acid groups N-terminus and C-terminus A protein sequence is written in the N-C direction
- 38. Levels of structure Secondary structure The extension of the chain as a result of hydrogen bonding between residue not too far apart. Two common structures that result are the α-helices and β-sheets. In an α-helical structure, hydrogen bonding occurs between the α-carboxyl group of one residue and the — NH group of its neighbor four units down the chain. β-sheets are formed by hydrogen bonds between sections of the same chain parallel or anti-parallel.
- 40. Levels of structure Tertiary structure This is a result of interactions between R groups widely separated along the chain. It is a collection of helices and sheets The interaction can be by covalent, di-sulphide or hydrogen bonds There may also be hydrophobic and hydrophilic interactions Tertiary structure is responsible for the proper folding and activity of the protein as an enzyme.
- 41. Levels of structure Quaternary structure Some proteins are made up of 2 different polypeptide chains called subunits. These subunits fold separately and interact with each other to form a quaternary structure Hemoglobin has four subunits
- 42. Antibodies Special proteins that bind to particular molecules with a high degree of specificity They appear in the cell system in response to a foreign macromolecule called antigen They are used industrially in diagnostic kits and protein separation schemes
- 43. Nucleic Acids: RNA, DNA Central role in reproduction Deoxyribonucleic acid (DNA) stores and preserves the genetic information Ribonucleic acid (RNA) plays a central role in protein synthesis DNA, RNA are polymers of nucleotides
- 45. Nucleotides
- 46. Nucleotides
- 49. DNA, RNA Polymers of nucleotides (condensation rxn) Link is between the 3’ and 5’ carbons on successive sugar rings by phosphodiester bonds One end has a free 3’ position and the other end has a free 5’ position DNA, RNA has direction Usually written in the 5’ - 3’ direction
- 51. DNA, RNA DNA is made up of 2 helical polynucleotide chains coiled around a common axis The two chains (known as strands) run in opposite directions, 5’-3’ and 3’-5’ The two chains are held together by hydrogen bonds between pairs of bases A-T (2 hydrogen bonds) and G-C (3 hydrogen bonds) The two strands must be complementary Sequence of bases is not restricted The precise sequence carries the genetic code
- 52. DNA Structure