ChE 661 is a course on Biochemical Engineering covering topics such as industrial microbiology, enzyme kinetics, and bioreactor design. It emphasizes the role of biochemical engineers in optimizing biological processes and the applications of biotechnology in various industries. The document also details the composition and functions of proteins and nucleic acids, highlighting their significance in biological systems.
ChE 661 is a course on Biochemical Engineering covering topics such as industrial microbiology, enzyme kinetics, and bioreactor design. It emphasizes the role of biochemical engineers in optimizing biological processes and the applications of biotechnology in various industries. The document also details the composition and functions of proteins and nucleic acids, highlighting their significance in biological systems.
ChE 661 is a course on Biochemical Engineering covering topics such as industrial microbiology, enzyme kinetics, and bioreactor design. It emphasizes the role of biochemical engineers in optimizing biological processes and the applications of biotechnology in various industries. The document also details the composition and functions of proteins and nucleic acids, highlighting their significance in biological systems.
ChE 661 is a course on Biochemical Engineering covering topics such as industrial microbiology, enzyme kinetics, and bioreactor design. It emphasizes the role of biochemical engineers in optimizing biological processes and the applications of biotechnology in various industries. The document also details the composition and functions of proteins and nucleic acids, highlighting their significance in biological systems.
E. G. Ankudey January, 2024 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 References 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. 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. Applications of Biotechnology Role of Biochemical Engineer 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 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. 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 Disadvantages Complex product mixtures Dilute aqueous environments Contamination Variability Sources of Enzymes Plants Animals Microorganisms Microbial cells 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+, SO42- )
vitamins. Typical cell composition 50% carbon, 20% oxygen, 14% nitrogen, 8% hydrogen, 3% phosphorus, 1% sulfur, small amounts of K+, Na+, Ca2+, Mg2+, Cl-, vitamins. 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). Cell composition
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. 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. 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. Amino acid structure
Only L-amino acids are found in proteins.
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 Amino acids Amino acids 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. 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 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. The peptide bond 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.
Peptide bond Many proteins contain organic and/or inorganic components other than amino acids. These components are called prosthetic groups Proteins containing prosthetic groups are called conjugated proteins Hemoglobin is an example of conjugated protein
Haemoglobin has four heme groups, which are iron-
containing organometallic complexes. 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 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 Primary Structure 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. Secondary structure 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. 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 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 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 Nucleotides
pentose (ribose, deoxyribose
Nucleotide base (purine, pyrimidine
Phosphoric acid Nucleotides Nucleotides Bases in nucleotides Purines Bases in nucleotides
Pyrimidines 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 Phosphodiester bond 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 DNA Structure
Amino Acids are linked by peptide bonds to form formed by linking the α-carboxyl group of one amino acid to the α-amino group of another amino acid with a peptide bond (also called an amide bond)
Amino Acids are linked by peptide bonds to form formed by linking the α-carboxyl group of one amino acid to the α-amino group of another amino acid with a peptide bond (also called an amide bond)
