Biotechnology-Textbook-v-3-2016-2017

CHAPTER 1: INTRODUCTION TO BIOTECHNOLOGY

  • 1.1 What is Biotechnology?

    • Biotechnology is the use of a living organism for one’s own benefit; its roots date back to early civilization through agriculture (cultivation of crops, domestication of animals).

    • In modern biotechnology, gene splicing and recombinant organisms take center stage, enabling genetic engineering.

    • The biotechnology industry has grown to affect daily life via healthcare products, vaccines, and industrial processes.

  • 1.2 Biotechnology: Healing, Fueling & Feeding the World

    • Biotech is technology based on biology, harnessing cellular and biomolecular processes to develop technologies and products.

    • Historically, microorganisms have been used for >6,000 years to make food (bread, cheese) and preserve dairy products.

    • Modern biotech aims to combat diseases, reduce environmental footprint, improve food security, generate cleaner energy, and make manufacturing processes safer and cleaner.

    • Current impact indicators:

    • >250 biotechnology healthcare products and vaccines available to patients (for previously untreatable diseases).

    • >13.3 million farmers worldwide using agricultural biotechnology to increase yields and reduce crop damage.

    • >50 bio-refineries across North America to convert renewable biomass into biofuels and chemicals.

    • Healing (examples): reducing infectious disease rates, saving millions of lives, tailoring treatments to individuals, improving disease detection, etc.

    • Fueling (examples): fermentation-based production, enzymes and biocatalysts as microscopic manufacturing plants, improving process efficiencies and reducing petrochemical reliance.

    • Feeding (examples): biotech crops with insect resistance, herbicide tolerance, enhanced nutrition, reduced pesticide use, and improved oil content for cardiovascular health.

  • 1.3 What is Biotechnology Used for?

    • Four main subfields: green (plants), blue (aquatic), white (industrial/bioprocessing), red (medical).

    • Green biotech is the oldest and most widely used; blue biotech is relatively rare.

    • White biotech focuses on using biological organisms to produce or process chemicals for industry; can include bioremediation (e.g., bacteria degrading environmental pollutants).

    • Red biotech involves medical applications: drug production via modified organisms, gene therapy, and genome manipulation.

    • Debate: GMOs and environmental/health concerns versus potential for environmental friendliness and food security.

  • 1.4 Safety in a Biotechnology Lab

    • Lab safety is a shared responsibility; following rules protects individuals and the lab community.

    • Lab security is emphasized due to hazardous materials and potential misuse; post-9/11 regulations increased security measures.

  • 1.5 Proper Handling & Storage of Chemicals & Reagents

    • MSDS (Material Safety Data Sheets): each chemical labeled with chemical identity, hazard ingredients, physical/chemical properties, fire/explosion data, reactivity, health hazards, handling precautions, and control measures.

    • NFPA ratings: color-coded blue (health), red (flammability), yellow (reactivity); numbers indicate hazard level.

    • 8 sections of MSDS standard; details include TLV (threshold limit value) exposure levels and emergency contacts.

  • 1.6 General Safety Precautions in Handling Hazardous Chemicals in the Lab

    • Routes of exposure: inhalation, skin/eye contact, ingestion, injection; use PPE and fume hoods.

    • Safety rules by chemical type (flammables, corrosives, reactives, toxic chemicals) with practical handling guidance.

    • Common hazardous chemicals and hazards (carcinogens, mutagens, neurotoxins, teratogens, nephrotoxins, hepatotoxins, corrosives).

  • 1.7 Biological Safety: Containment

    • Live organisms and recombinant DNA are handled as biosafety hazards; treat all living materials and recombinant DNA as potential hazards.

    • Routes of exposure mirror chemical hazards; maximize containment and training.

    • Practices include restricting access, PPE, hand washing, no mouth pipetting, disinfection, autoclaving regulated waste, insect/rodent control, and using a laminar flow cabinet where available.

  • 1.8 Disposal of Hazardous Chemicals & Biological Materials

    • Hazardous chemical disposal subject to state/federal regulations; autoclave bags for biohazard waste; autoclave to kill organisms.

    • Clean benches with bleach after messy sessions; turn off equipment when leaving.

  • 1.9 Micropipettors & Tip Boxes

    • Each station has a dedicated micropipettor set; tips labeled to workstation for tracking.

  • 1.10 Glassware

    • Proper washing/storage areas; do not leave glassware in sinks; labeling conventions; use label tape for labeling; broken glass disposed in designated box; clean-up rules.

  • 1.11 Biotechnology Student Checkout Duties

    • Lab etiquette and workspace cleanliness; label solutions and prep forms; return equipment; wipe benches with bleach; wash glassware; assist others; ensure hazardous materials stored properly; turn off balances, hot plates, spectrophotometers, and other equipment.

CHAPTER 2: MATH SKILLS & BASIC TOOLS IN A BIOTECH LAB

  • 2.1 Mass & Volume with SI Units

    • Mass measured directly, by difference, or by subtraction; units: mass in grams (g); volume in milliliters (mL); 1 mL = 1 cm^3.

    • Volume measurements typically with graduated cylinders; micropipettes for small volumes.

    • Volume concepts: cuboid volume V = L × W × H.

    • Volume by displacement for irregular solids: Solid Volume = Total Volume − Liquid Volume.

    • Density d = m/V; density is an intensive property, enabling interconversion between mass and volume.

  • 2.2 Metric Units

    • Metric prefixes and conversions (based on powers of ten); importance of scientific notation for small measurements.

    • Example conversion process using the staircase concept to shift decimal places.

  • 2.3 Difference Between Accuracy & Precision

    • Accuracy: closeness to a known/accepted value.

    • Precision: reproducibility or consistency of measurements.

    • Analogy: hitting bullseye vs. clustering around a point.

  • 2.4 Common Biotechnology Lab Equipment

    • Volume measurement tools:

    • Erlenmeyer flasks (not calibrated for accurate volumes).

    • Beakers (not reliable for precise volume).

    • Graduated cylinders (calibrated for reasonable accuracy).

    • Volumetric flasks (high accuracy for standard solutions).

    • Pipets including Pasteur, Beral, serological, Mohr, volumetric, automatic micropipettes, and multichannel pipettes.

    • Mass measurement: balances (mechanical vs electronic); analytical electronic balances with high sensitivity.

    • pH measurement: pH meters (calibration with buffers); pH readouts to 0.1 pH unit.

    • Light measurement: spectrophotometers (VIS, UV/VIS, scanning, NanoDrop, microplate readers).

    • Solution preparation devices: magnetic stirrers, vortex mixers.

    • Microbiology tools: autoclaves, biosafety hoods, fermentors.

    • Microscopy: brightfield/light, stereoscope, SEM, TEM; magnifications and usage tips.

  • 2.5 Using the Spectrophotometer

    • Spectrophotometer measures transmittance or absorbance of light; relationship: absorbance increases with sample density.

    • Blank cuvette used to subtract cuvette/solvent contributions; auto-zero procedure.

    • Wavelength selection guided by absorption spectrum of the analyte; peak absorption gives best measurement precision.

  • 2.6 Microscopes

    • Types: Light microscope (40x, 100x, 400x), Stereoscope, Scanning Electron Microscope (SEMs) and Transmission Electron Microscope (TEM).

    • Magnification calculations: Total magnification = magnification of ocular × objective.

    • Focusing sequence: start with scanning, switch to medium, then high; adjust diaphragms and lighting; use fine adjustment for high power; avoid damage.

    • Drawing and sample prep practices for microscopy (wet mounts, staining, oil immersion).

CHAPTER 3: MICROBIOLOGY AND BACTERIA

  • 3.1 Origin of Life

    • Life originated ~4 billion years ago; earliest cells were prokaryotic (no nucleus or true organelles).

    • Oldest prokaryotic fossils ~3.5 billion years old; lithotrophic and fermentative metabolisms among early prokaryotes.

    • Eukaryotes with nuclei appeared ~1.5–2 billion years ago.

  • 3.2 Prokaryotic Life

    • Domains: Bacteria, Archaea; prokaryotic cells lack a defined nucleus.

    • Archaea (formerly archaebacteria) are a separate domain; endosymbiotic theory links mitochondria and chloroplasts to bacteria.

  • 3.3 Size, Distribution & Ecology

    • Typical bacterial cells ~1 μm in diameter; overwhelmingly abundant in soil and oceans; 10^9–10^9 cells per gram of soil; bacteria surpass eukaryotes in number and biomass in many habitats.

    • Endosymbiosis and mutualistic relationships between bacteria and eukaryotes; nitrogen fixation and methanogenesis as prokaryotic-specific metabolisms.

  • 3.4 Structure & Function of Prokaryotic Cells

    • Three architectural regions: appendages (flagella, pili), cell envelope (capsule, cell wall, plasma membrane), cytoplasmic region (DNA, ribosomes, inclusions).

    • Flagella: motility; patterns include polar and peritrichous; chemotaxis response to stimuli.

  • 3.5 Coverings of the Prokaryotic Cell

    • Cell wall composition differs by Gram staining:

    • Gram-positive: thick peptidoglycan layer with teichoic acids; retains crystal violet.

    • Gram-negative: thin peptidoglycan; outer membrane contains LPS (endotoxin); counterstain reveals pink.

    • Capsule, slime layer, glycocalyx: adherence, protection from phagocytosis, desiccation prevention; biofilms (e.g., dental plaque by Streptococcus mutans).

    • Fimbriae and pili: attachment and conjugation (sex pilus).

  • 3.6 Cytoplasmic Constituents

    • Prokaryotic chromosome typically one circular DNA molecule; plasmids may be present.

    • Ribosomes (70S) responsible for protein synthesis; inclusions act as nutrient reserves.

  • 3.7 Identification of Bacteria

    • Microscopy: cell shape (bacillus, coccus, spirilla), motility, Gram staining.

    • Use Bergey’s Manual as a field guide; follow with biochemical tests for definitive ID.

  • 3.8 Applications of Bacteria in Industry & Biotechnology

    • Fermentation, antibiotics production, vaccines, enzymes; industrial biotech uses bacteria for biosynthesis and gene engineering foundations.

  • 3.9 Growing Bacteria in Culture

    • Culture media types: broth (liquid), solid media with agar; defined vs undefined; selective vs differential media.

    • Aseptic technique and streaking for isolation to obtain pure cultures from mixed populations.

    • Inoculation tools: loop and stab inoculators; sterile technique; streaking pattern to isolate colonies.

  • 3.10 Bacterial Colony Characteristics

    • Observing colony size, shape, margin, surface, pigmentation, translucence, elevation.

  • Lab Backgrounds

    • Yogurt Lab: starter cultures Lactobacillus bulgaricus and Streptococcus thermophilus ferment lactose; yogurt standards: at least 8.25% solids not fat; fat content categories; stabilizers; demand for probiotic cultures.

    • Dental Caries & Microbial Flora: plaque bacterial communities; S. mutans as major caries contributor; plaque pH and fermentation of sugars; fluoride role; salivary restoration dynamics.

    • Gram Staining Lab: differentiates Gram-positive vs Gram-negative based on cell wall properties and dye retention; procedure steps and interpretation.

    • Aseptic Technique & Streaking Lab: steps to obtain well-isolated colonies; use of sterile loops, flame sterilization, plate handling, etc.

CHAPTER 4: BIOCHEMISTRY & PREPARING SOLUTIONS

  • 4.1 Atoms

    • Atoms are composed of protons, neutrons (nucleus) and electrons (electron cloud). Protons determine identity (Z, atomic number).

    • Nucleus held together by the strong force; electrons occupy orbitals; electron configuration predicts chemical behavior.

  • 4.2 The Periodic Table of Elements

    • Elements organized by increasing atomic number; cells contain symbol, atomic number, mass, and name; groups/families share similar valence electron counts; trends: atomic radius, ionization energy, electronegativity, electron affinity.

    • Protons = atomic number; Neutrons = atomic mass − atomic number; Electrons = atomic number.

  • 4.3 What is a Mole & Why are Moles Used?

    • Mole is a unit defined by Avogadro’s number: NA=6.022imes1023N_A = 6.022 imes 10^{23} particles per mole.

    • One mole of carbon = 12.0 g; mass of solute = molarity × volume × molar mass:

    • m<em>extsolute=MimesVimesM</em>extsolutem<em>{ ext{solute}} = M imes V imes M</em>{ ext{solute}}

    • Relationship: moles ↔ mass; molarity (M) = moles per liter (mol/L).

    • Example: Chromium oxide CrO₂:

    • M<em>extCrO</em>2=M<em>extCr+2imesM</em>extO=52.00+2(16.00)=84.00extg/molM<em>{ ext{CrO}</em>2} = M<em>{ ext{Cr}} + 2 imes M</em>{ ext{O}} = 52.00 + 2(16.00) = 84.00 ext{ g/mol}

  • 4.4 Mixing Solutions

    • Concentration concepts: grams per liter (g/L), molarity (M), parts per million (ppm), percent composition.

    • Percent solution:

    • Measure solute mass, measure total solution mass, extpercent=racm<em>extsolutem</em>extsolutionimes100ext{percent} = rac{m<em>{ ext{solute}}}{m</em>{ ext{solution}}} imes 100

    • Serial dilutions: used for achieving very small final concentrations; concept of fixed dilution factor.

CHAPTER 5: BASIC DNA STRUCTURE

  • 5.1 Basic Information

    • DNA stands for Deoxyribonucleic Acid; largest cellular molecule; genetic code contained in nucleotide sequence; inheritance through reproduction.

  • 5.2 History of Research

    • Griffith (1928): transformation with dead virulent bacteria transforming live non-virulent bacteria; Avery–McCarty–MacLeod (1944): DNA as the transforming material; Chargaff (late 1940s): A=T and C=G rule; Rosalind Franklin (1951): X-ray crystallography revealed DNA structure; Hershey–Chase (1952): DNA as genetic material; Watson & Crick (1953): DNA double-helix model with antiparallel strands; Nobel prizes awarded in 1962 (crick/wilkins) and 1968–1980s to various contributors.

  • 5.3 DNA Structure

    • Nucleotides consist of sugar (deoxyribose), phosphate, and a nitrogenous base (A, T, G, C).

    • Backbone: sugar–phosphate; bases pair via hydrogen bonds (A–T with 2, G–C with 3).

    • Strands are antiparallel (5' to 3' vs 3' to 5'); 3' end lacks phosphate, 5' end has phosphate; sequence written 5'→3' along each strand.

    • Base pairing maintains equal amounts of A/T and G/C across the two strands.

  • 5.4 DNA Extraction

    • Steps overview: lyse cells to release DNA; degrade proteins; precipitate DNA with salt; wash with cold alcohol; re-suspend; confirm via electrophoresis.

    • Applications include FISH, T-RFLP, sequencing; DNA extraction can target cheek cells, bacteria, viruses, etc.

CHAPTER 6: DNA PROFILING & GEL ELECTROPHORESIS

  • 6.1 A Brief Historical Introduction

    • Electrophoresis evolved from paper to gel-based methods; gels provide sieving through a porous matrix; DNA movement is length-dependent.

  • 6.2 Agarose Gel Electrophoresis of Nucleic Acids

    • Nucleic acids migrate toward the positive electrode; shorter fragments move faster; effective size range for dsDNA in agarose ~100 bp to 25,000 bp; very long fragments exhibit limiting mobility.

    • Concept of a linear DNA ladder and “nested sets” in sequencing contexts.

  • 6.3 DNA Fingerprinting (Beginner's Guide)

    • Six steps: extract DNA, cut with restriction enzymes, separate fragments on gel, transfer to paper (Southern blot), probe with radioactive or labeled DNA, visualize via film.

    • Probes exploit tandem repeats (STRs or VNTRs) to generate a distinctive pattern.

    • Forensics uses STRs (short tandem repeats) and VNTRs (variable number tandem repeats) for identity testing.

  • 6.4 RFLPs (Restriction Fragment Length Polymorphisms)

    • Exploits variations in DNA sequences; digestion with restriction enzymes yields different fragment patterns; historically foundational to DNA profiling; now largely supplanted by PCR-based methods due to sensitivity requirements.

  • 6.5 VNTRs

    • Regions with tandem repeats; length variations across individuals; used in identification and forensic analysis.

  • 6.6 DNA Fingerprinting Technology / DNA Profiling

    • Practical uses: crime scene analysis, paternity testing, missing persons, historical investigations; privacy concerns.

  • Candy Electrophoresis Lab Background; Paternity Testing Lab Background; Restriction Digestion Analysis of Lambda DNA Lab Background; (Crime Scene) DNA Fingerprinting Using Restriction Enzymes Lab Background – Applied labs accompanying the topics above.

CHAPTER 7: DNA REPLICATION

  • 7.1 Introduction to Replication

    • DNA replication produces two identical copies from one molecule; semi-conservative replication; origins of replication; replication forks expand bidirectionally.

  • 7.2 Short Review of DNA Structure

    • Double helix; nucleotides with sugar, phosphate, and base; base pairing; antiparallel strands; 3' and 5' ends; directionality of synthesis.

  • 7.3 DNA Polymerase

    • Polymerases extend existing 3' end; require a primer; DNA Polymerase III builds new strands; energy from hydrolysis of phosphate bonds in dNTPs.

  • 7.4 Replication Process

    • Three phases: initiation (origins opened by initiator proteins; AT-rich regions easier to unwind), elongation (leading strand synthesized continuously, lagging strand via Okazaki fragments; RNA primers removed and replaced with DNA; ligation fixes nicks), termination (for prokaryotes, forks meet; for eukaryotes telomeres). Telomeres shorten in somatic cells; telomerase maintains telomeres in germ cells.

  • 7.5 DNA Replication Proteins

    • Key players: Helicase, DNA Polymerase III, clamp, SSBs, Topoisomerase, DNA Gyrase, DNA Ligase, RNA Primase, Telomerase.

CHAPTER 8: PCR

  • 8.1 Introduction to PCR

    • PCR amplifies a targeted DNA region using DNA polymerase and primers; generates billions of copies from small starting material.

  • 8.2 History of PCR

    • Early work (Kleppe et al., 1971) described in vitro DNA amplification; Mullis (1983) conceived PCR; Nobel Prize (1993) for Mullis; PCR transformed genetic testing, mapping, sequencing, etc.

  • 8.3 PCR Step-by-Step

    • Cycle steps: denaturation at ~94°C (separates strands), annealing ~54–60°C (primers bind), extension ~72°C (DNA polymerase extends).

    • Each cycle doubles the amount of target DNA; after ~30–40 cycles, substantial amplification occurs; analysis via gel electrophoresis.

    • A typical cycle yields exponential growth: after n cycles, copies ≈ 2^n (assuming 100% efficiency).

  • 8.4 PCR Cycles Review

    • Mapping of cycle steps: Denaturing (C), Annealing (A), Extension (B) as shown in practice.

  • 8.5 PCR-Type DNA Testing

    • Two main methods: PCR-based amplification for analysis; non-amplified (RFLP) methods when sufficient DNA is available; PCR is more sensitive but more prone to contamination.

  • 8.6 Taq Polymerase

    • Thermostable DNA polymerase from Thermus aquaticus enables high-temperature cycling; eliminates need to replenish enzyme after denaturation steps.

  • 8.7 What is PCR Used For?

    • Applications include DNA fingerprinting, pathogen detection, genetic disease diagnosis, sequencing support, and forensic testing.

  • 8.8 Limitations of PCR

    • Plateau effect due to inhibitors and depletion of reagents; end-point quantification challenges; contamination risk.

  • 8.9 Using PCR to Sequence DNA – The Sanger Method

    • Manual sequencing via Sanger method uses ddNTP terminators; four reactions with each ddNTP; polyacrylamide gel separation; visualization via autoradiography or fluorescence.

  • 8.10 Fully Automated Sequencing – Computer Mediated Sequencing

    • Modern automated sequencing uses fluorescent labels and laser detection; high-throughput sequencing in a single lane possible; require careful data interpretation for signal quality.

  • PV92 Gene Lab Background; DNA Sequencing Lab Background – practical labs accompanying the PCR & sequencing chapters.

CHAPTER 9: RECOMBINANT DNA TECHNOLOGY

  • 9.1 Ribonucleic Acid (RNA)

    • RNA overview: roles in transcription, translation, and regulation; mRNA, tRNA, rRNA; RNA can also have catalytic roles (ribozymes); RNA-based regulation relates to various diseases.

  • 9.2 RNA Structure

    • RNA bases: A, G, C, U; single-stranded; ribose sugar; differences from DNA (no T); structural implications.

  • 9.3 Protein Synthesis

    • Central dogma: DNA → RNA → protein; transcription adds RNA copy; translation uses ribosomes to synthesize polypeptides; codons (triplets) specify amino acids; tRNA anticodons pair with mRNA codons; ribosome sites A, P, E; methionine as start codon; N- and C- termini orientation; post-translational modifications.

  • 9.4 Manipulating DNA

    • DNA manipulation and gene transfer enable production of recombinant proteins (e.g., insulin, growth hormone). Bacterial transformation serves as a foundation for biotech production.

  • 9.5 Central Dogma of DNA

    • Re-statement of DNA → RNA → Protein; gene as DNA sequence; mRNA as template; translation yields phenotype.

CHAPTER 10: GENETIC ENGINEERING

  • 10.1 What is Genetic Engineering?

    • Recombinant DNA technology: altering genes to create GMOs; major phases: synthesis of recombinant DNA and gene cloning.

  • 10.2 Techniques of Genetic Engineering

    • Gene isolation, vector selection, cloning of desired gene, gene transfer, selection of transformants, replication of recombinant DNA in host, and propagation of clones; in practice, two routes: DNA cloning in a vector or using PCR for amplification.

  • 10.3 Restriction Enzymes

    • Restriction enzymes cut DNA at specific sites; recognition sequences are palindromic; most cuts generate sticky ends; Type II restriction enzymes cut within recognition sequences.

    • Enzymes named after organism of origin (e.g., EcoRI). Methylases protect host DNA from restriction.

    • Gel electrophoresis separates fragments by size to analyze digestion patterns.

  • 10.4 DNA Ligase

    • DNA ligase seals nicks to complete DNA backbone after restriction fragment joining; works with compatible ends.

  • 10.5 Vectors

    • Vectors carry foreign DNA into host cells; must have origin of replication, selective marker, cloning sites, suitable size, and transcription control elements; circular plasmids are common

  • 10.6 Plasmids

    • Common vectors (e.g., pBR322); features include ori, multiple restriction sites, antibiotic resistance markers; used to clone and propagate recombinant DNA; transformation efficiency and selection strategies.

  • 10.7 Gene Transfer

    • Methods: heat shock, electroporation, viral delivery, plant transformation via Agrobacterium Ti plasmid, gene gun, microinjection, liposomes; markers used to identify transformed cells (e.g., antibiotic resistance).

    • Transformation efficiency statistics and selection strategies; on/off inducible promoters for regulated gene expression (e.g., IPTG induction of lac operon in plasmids; T7 RNA polymerase system).

  • 10.8 Genetic Technology in Perspective

    • Historical overview from Descartes to Boyer & Cohen; contributions of Berg, Cohen, and others; definition from European Federation of Biotechnology: integrating natural science and organisms for products and services.

  • 10.9 Principles of Genetic Engineering

    • Two core techniques: genetic engineering and sterile bioprocessing; safe design to avoid unwanted gene transfer; risk management and containment.