chapter 3 enzyme-药事情

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enzyme3(酶的抑制)

E2
A
active
12 A
Inactቤተ መጻሕፍቲ ባይዱve
adenylylation
3.4.4 Proteolytic activation
• Some enzymes are synthesized as larger inactive precursors called proenzymes or zymogens. • These are activated by the irreversible hydrolysis of one or more peptide bonds.
• A noncompetitive inhibitor binds reversibly at a site other than the active site and causes a change in the overall three-dimensional shape of the enzyme that leads to a decrease in catalytic activity. • The enzyme may bind the inhibitor,the substrate or both the inhibitor and substrate together.
Concerted model
T state
S
R state
S
S
S S
S
S S S
S
S S S S
carbamoyl phosphate
aspartate carbamoylaspart ate
3.4.3 Reversible covalent modification
• The activity of many enzymes is altered by the reversible making and breaking of a covalent bond between the enzyme and a small nonprotein group.

生物化学英文课件Biochemistry-chapter 3

Requirement：1. Less cleave sites; 2. High specificity； 3. More production.
（1）Proteases cleavage：
1．Trypsin：C-terminal of Arg, Lys. High specificity
2．Chymotrypsin： C-terminal of Phe, Trp, Tyr.
1. Separation of amino acids by ion exchange chromatography
Amino Acid Separation
Unfortunately, amino acids are not colored as described in this overhead. Therefore, what methods would you use to first check if an amino acid is indeed present?
A-E-F-S-G-I-T-P-K
L-V-G-K
• Chymotrypsin Cleavage:
L-V-G-K-A-E-F S-G-I-T-P-K
• Edman degradation: L
• Correct sequence:
L-V-G-K-A-E-F-S-G-I-T-P-K
<2> Enzymatic hydrolysis：
7. Clostripain（Arg protease ）： c-terminal of Arg.
（2）Chemical cleavage：
1．CNBr： c-terminal of Met.
CNBr is useful because proteins usually have only few Met residues.

细胞治疗药典参考目录(Gene and Cell Therapy Products)

1 Chapter Guide: Gene and Cell Therapy ProductsTo return to the Chapter Charts main list, click her e.Universal TestsIdentification•á11ñ USP Reference Standards•á1030ñ Biological Assay Chapters—Overview and Glossary•á1032ñ Design and Development of Biological Assays•á1033ñ Biological Assay Validation•á1034ñ Analysis of Biological Assays•á1044ñ Cryopreservation of Cells•á1102ñ Immunological Test Methods—General Considerations•á1103ñ Immunological Test Methods—Enzyme-Linked Immunosorbent Assay (ELISA)•á1104ñ Immunological Test Methods—Immunoblot Analysis•á1285ñ Preparation of Biological Specimens for Histologic and Immunohistochemical Analysis•á1285.1ñ Hematoxylin and Eosin Staining of Sectioned Tissue for Microscopic ExaminationAssay•á621ñ Chromatography•á1030ñ Biological Assay Chapters—Overview and Glossary•á1032ñ Design and Development of Biological Assays•á1033ñ Biological Assay Validation•á1034ñ Analysis of Biological Assays•á1044ñ Cryopreservation of Cells•á1102ñ Immunological Test Methods—General Considerations•á1103ñ Immunological Test Methods—Enzyme-Linked Immunosorbent Assay (ELISA)•á1430.1ñ Analytical Methodologies Based on Scattering Phenomena—Static Light Scattering Specific Tests1, 2Biocompatibility•á87ñ Biological Reactivity Tests, In Vitro•á88ñ Biological Reactivity Tests, In Vivo•á1031ñ The Biocompatibility of Materials Used in Drug Containers, Medical Devices, and Implants•á1184ñ Sensitization TestingMicrobial/Sterility Issues•á61ñ Microbiological Examination of Nonsterile Products: Microbial Enumeration Tests•á62ñ Microbiological Examination of Nonsterile Products: Tests for Specified Microorganisms•á63ñ Mycoplasma Tests•á71ñ Sterility Tests•á85ñ Bacterial Endotoxins Test•á151ñ Pyrogen Test•á161ñ Medical Devices—Bacterial Endotoxin and Pyrogen Tests•á1050ñ Viral Safety Evaluation of Biotechnology Products Derived from Cell Lines of Human or Animal Origin•á1071ñ Rapid Microbial Tests for Release of Sterile Short-Life Products: A Risk-Based Approach•á1085ñ Guidelines on Endotoxins Test•á1113ñ Microbial Characterization, Identification, and Strain Typing•á1116ñ Microbiological Control and Monitoring of Aseptic Processing Environments•á1208ñ Sterility Testing—Validation of Isolator Systems•á1211ñ Sterility Assurance•á1227ñ Validation of Microbial Recovery from Pharmacopeial Articles•á1228ñ Depyrogenation•á1228.1ñ Dry Heat Depyrogenation•á1228.3ñ Depyrogenation by Filtration•á1228.4ñ Depyrogenation by Rinsing•á1228.5ñ Endotoxin Indicators for Depyrogenation•á1229ñ Sterilization of Compendial Articles•á1229.3ñ Monitoring of Bioburden•á1229.4ñ Sterilizing Filtration of Liquids2•á1229.14ñ Sterilization Cycle Development•á1229.15ñ Sterilizing Filtration of Gases•á1229.17ñ Mycoplasma Sterilization•á1229.18ñ Viral Clearance MethodsProduction Issues•á1ñ Injections and Implanted Drug Products (Parenterals)—Product Quality Tests•á90ñ Fetal Bovine Serum—Quality Attributes and Functionality Tests•á92ñ Growth Factors and Cytokines Used in Cell Therapy Manufacturing•á797ñ Pharmaceutical Compounding—Sterile Preparations•á1024ñ Bovine Serum•á1041ñ Biologics•á1043ñ Ancillary Materials for Cell, Gene, and Tissue-Engineered Products•á1044ñ Cryopreservation of Cells•á1046ñ Cell-based Advanced Therapies and Tissue-Based Products•á1047ñ Gene Therapy Products•á1074ñ Excipient Biological Safety Evaluation Guidelines•á1126ñ Nucleic Acid-Based Techniques—Extraction, Detection, and Sequencing•á1127ñ Nucleic Acid-Based Techniques—Amplification•á1229.16ñ Prion Inactivation•á1229.17ñ Mycoplasma Sterilization•á1229.18ñ Viral Clearance Methods•á1237ñ Virology Test Methods•á1285ñ Preparation of Biological Specimens for Histologic and Immunohistochemical Analysis•á1285.1ñ Hematoxylin and Eosin Staining of Sectioned Tissue for Microscopic Examination Product Issues•á381ñ Elastomeric Components in Injectable Pharmaceutical Product Packaging/Delivery Systems•á382ñ Elastomeric Component Functional Suitability in Parenteral Product Packaging/Delivery Systems•á1046ñ Cell-based Advanced Therapies and Tissue-Based Products•á1086ñ Impurities in Drug Substances and Drug Products•á1121ñ Nomenclature•á1151ñ Pharmaceutical Dosage Forms•á1229.17ñ Mycoplasma SterilizationEquipment•á31ñ Volumetric Apparatus•á41ñ Balances•á1051ñ Cleaning Glass Apparatus•á1228.4ñ Depyrogenation by Rinsing•á1229.13ñ Sterilization-in-Place•á1229.15ñ Sterilizing Filtration of Gases•á1229.16ñ Prion Inactivation•á1251ñ Weighing on an Analytical BalanceCharacterization•á111ñ Design and Analysis of Biological Assays•á507ñ Protein Determination Procedures•á621ñ Chromatography•á785ñ Osmolality and Osmolarity•á787ñ Subvisible Particulate Matter in Therapeutic Protein Injections•á788ñ Particulate Matter in Injections•á791ñ pH•á905ñ Uniformity of Dosage Units•á911ñ Viscosity—Capillary Methods•á912ñ Viscosity—Rotational Methods•á913ñ Viscosity—Rolling Ball Method•á1027ñ Flow Cytometry•á1030ñ Biological Assay Chapters—Overview and Glossary•á1032ñ Design and Development of Biological Assays•á1033ñ Biological Assay Validation•á1034ñ Analysis of Biological Assays•á1044ñ Cryopreservation of Cells•á1046ñ Cell-based Advanced Therapies and Tissue-Based Products3•á1048ñ Quality of Biotechnology Products: Analysis of the Expression Construct in Cells Used for Production of r-DNA Derived Protein Products•á1049ñ Quality of Biotechnological Products: Stability Testing of Biotechnological/Biological Products•á1052ñ Biotechnology Derived Articles—Amino Acid Analysis•á1053ñ Capillary Electrophoresis•á1054ñ Biotechnology Derived Articles—Isoelectric Focusing•á1055ñ Biotechnology Derived Articles—Peptide Mapping•á1056ñ Biotechnology Derived Articles—Polyacrylamide Gel Electrophoresis•á1057ñ Biotechnology Derived Articles—Total Protein Assay•á1084ñ Glycoprotein and Glycan Analysis—General Considerations•á1102ñ Immunological Test Methods—General Considerations•á1103ñ Immunological Test Methods—Enzyme-Linked Immunosorbent Assay (ELISA)•á1104ñ Immunological Test Methods—Immunoblot Analysis•á1126ñ Nucleic Acid-Based Techniques—Extraction, Detection, and Sequencing•á1127ñ Nucleic Acid-Based Techniques—Amplification•á1128ñ Nucleic Acid-Based Techniques—Microarray•á1129ñ Nucleic Acid-Based Techniques—Genotyping•á1130ñ Nucleic Acid-Based Techniques—Approaches for Detecting Trace Nucleic Acids (Residual DNA Testing)•á1237ñ Virology Test Methods•á1285ñ Preparation of Biological Specimens for Histologic and Immunohistochemical Analysis•á1285.1ñ Hematoxylin and Eosin Staining of Sectioned Tissue for Microscopic Examination•á1430.1ñ Analytical Methodologies Based on Scattering Phenomena—Static Light Scattering•á1776ñ Image Analysis of Pharmaceutical Systems•á1787ñ Measurement of Subvisible Particulate Matter in Therapeutic Protein Injections•á1788ñ Methods for the Determination of Subvisible Particulate Matter•á1788.1ñ Light Obscuration Method for the Determination of Subvisible Particulate Matter•á1788.2ñ Membrane Microscope Method for the Determination of Subvisible Particulate Matter•á1788.3ñ Flow Imaging Method for the Determination of Subvisible Particulate Matter。

生物化学英文课件Biochemistry-chapter 3

(2) Storage and transport of biochemical molecules (Hb, Mb)
(3) Physical cell support and shape (tubulin, actin, collagen)
(4) Mechanical movement (flagella, mitosis, muscles)
➢ (2) According to polymerization of protein molecules;
➢ Monomeric proteins ➢ Oligomeric proteins (multimeric proteins)
➢ (3) According to conjugation of protein molecules;
106 Da or more。 ➢ Usually insulin (5700 Da) or RNase (126000 Da)
was as the boundary of proteins and polypeptides. ➢ Mr of proteins ≈ Mr of amino acid ×110.
➢Mirror image pairs of amino acids are designated L (levo) and D (dextro)
➢Proteins are assembled from L-amino acids (few D-amino acids occur in nature)
Chapter 3 Amino Acids and the Primary
Structures of Proteins
3.1 Outline of Proteins 3.2 Structures of Amino Acids 3.3 Other Amino Acids and Amino

Chapter-3活性包装

Often the rate of loss can be reduced adequately by inert-gas flushing and
barrier packaging.
Chemical forms of in-pack oxygen scavenging have been introduced to reduce…
These include amines formed rapidly in fish or rancid odors in oil-containing foods. Such
compounds can be present in trace amounts that are significant organoleptically but may not constitute a health hazard.
•Chemical deterioration : food components hydrolysis, industrial chemical oxidation Industrial chemical such as amines , and particularly some printing inks, are oxidized on storage， fried snacks’ oxidation and so on.
dioxide to the beverage.
The presence of an oxygen scavenger is required.(beer and White Wine)
Chemical deterioration:
The flavor of some foods changes on storage because of effects other than oxidation. Tainting is a recurrent problem.

生化--英文题

生化历来都不画重点的，但留学生老是过不了，于是就有了这个重点资料，和我们考的差不多，但是英语的，求高人翻译啊Brief Exercises of BiochemistryChapter 1 The structure and function of proteinExplain the following terms1. peptide bond2. Amino acid residues3. Primary structure of protein4. isoelectric point5. Secondary structure of protein6. Tertiary structure of protein7. Domain8. Protein denaturation9. Quaternary structure of proteinAnswer the following questions briefly1. What is physiological significance of hemoglobin oxygen dissociation curve as S-shaped?2. Please describe physiological functions of proteins.Discuss the following questions (Essay questions)1. Explain the relationship between the primary and spatial structure and the function of protein.Chapter 2 The structure and function of nucleic acidsExplain the following terms1. primary structure of nucleic acids2. DNA denaturation3. Tm4. DNA renaturation5. nucleic acid hybridizationAnswer the following questions briefly1. What is the structural characteristics of an eukaryocyte mature mRNA?2. What is the biological significance of Tm?Discuss the following questions (Essay questions)1. Please compare the two types of nucleic acids (DNA and RNA) in the chemical composition, molecular structure, cell distribution and biological functions.2. Please describe the structural characteristics of the B-DNA.3. Describe the molecular composition, structural features and functions of tRNA.Chapter 3 EnzymeExplain the following terms1. enzyme2. enzyme active center3. enzyme competitive inhibition4. Km5. isoenzyme6. zymogen activationAnswer the following questions briefly1. Explains with examples the competitive inhibition characteristic and the practical significance.2. What is the relationship between the enzyme cofactor and vitamine?3. What is the physiological significance of zymogen?4. What is isoenzyme? What is clinical significance of isoenzyme?5. How many kinds of essential group of enzyme are there? What is the role of each?Chapter 4 Metabolism of carbohydrateExplain the following terms1. glycolysis2. glycolytic pathway3. tricarboxylic acid cycle4. gluconeogenesis5. blood sugarAnswer the following questions briefly1. Describe briefly source and fate of blood sugar2. Describe briefly the physiological significance of gluconeogenesis3. Describe briefly the physiological significance of glycolysis4. Describe briefly the outline of TCA cycle5. Describe briefly the physiological significance of TCA cycle6. Describe briefly the physiological significance of pentose phosphate pathway7. Outline the reasons for the formation of lactic acid cycle and the physiological significance.8. Overview the important role of B vitamins in glucose metabolism.9. Why 6-phosphate glucose dehydrogenase activity will increase after uptake high-carbohydrate diet?Discuss the following questions (Essay questions)1. Explain how is lactate converted into glucose? (Write down the main reactions and key enzymes)2. Explain how is lactate converted into CO2, H2O and releases ATP? (Write down the main reactions and key enzymes)3. Overview the regulation molecular mechanism of adrenaline on the blood sugar level.4. Please explain why a slimmer has to reduce the intake of carbohydrates from the point of view of nutrients metabolism. (Write down the related pathways, cellular localization, main reactions and key enzyme)Chapter 5 Metabolism of lipidsExplain the following terms1. fat mobilization2. ketone body3. plasma lipoprotein4. apolipoprotein5. essential fatty acid6. blood lipidsAnswer the following questions briefly1. What is the function of bile acid at lipids digestion?2. What is the physiological significance of ketone body generation?3. What are materials of fatty acid synthesis?4. What is the physiological significance of cholesterol?5. What are the functions of apolipoprotein?Discuss the following questions (Essay questions)1. Describe the sources, chemical composition characteristics and main physiological functions of plasma lipoprotein.2. Explain how is the stearic acid converted into CO2, H2O and releases ATP?3. Please describe the oxidation catabolism process of glycerol generated from fat mobilization4. Explain how is the glycerol converted into glycogen?5. Describe the source and fate of acetyl-CoA?Chapter 6 Biological oxidationExplain the following terms1. biological oxidation2. respiratory chain3. oxidative phosphorylation4. substrate level phosphorylationDiscuss the following questions (Essay questions)1. Write down the sequence of two respiratory chainChapter 7 Metabolism of amino-acidExplain the following terms1. essential amino acid2. deamination of amino acid3. transamination of amino acid4. one carbon unit5. hyperammonemiaAnswer the following questions briefly1. What is the physiological significance of one carbon units?2. What is meaning of PAPS, GABA, SAM and FH4 each?3. Write down the deamination of amino acids in vivo.4. Outline the source and fate of blood ammonia.Discuss the following questions (Essay questions)1. How does a glutamate be oxidized to supply energy? What is the final product?2. What are functions of vitamins B in the metabolism of amino acids?3. Use the alanine as an example, try to explain the gluconeogenesis process of glucogenic amino acids.Chapter 8 Metabolism of nucleotideExplain the following terms1. de novo synthesis pathway of purine nucleotide2. nucleotide antimetaboliteAnswer the following questions briefly1. Outline the biological function of nucleotide.2. Outline the physiological significance of salvage synthesis of purine nucleotide.Discuss the following questions (Essay questions)1. Use the 6-mercaptopurine as an example, please explain the mechanism of antimetabolite.Chapter 10 Biosynthesis of DNAExplain the following terms1. semi-conservative replication2. reverse transcription3. replication4. excision repairing5. frame-shift mutationAnswer the following questions briefly1. Outline the classification and function of prokaryote DNA polymerase.2. Outline the classification and function of eukaryote DNA polymerase.3. Outline the factors causing DNA damage.4. Outline the repairing of DNA damage.5. Outline the central dogma.Discuss the following questions (Essay questions)1. Describe the materials involved in prokaryote DNA replication and their functions in that process.2. Describe the biological significance of mutation.Chapter 11 Biosynthesis of RNAExplain the following terms1. transcription2. posttranscriptional process3. hnRNA4. promoter5. ribozyme6. structure geneAnswer the following questions briefly1. Outline the eukaryote posttranscriptional process.2. Outline the products of three kinds of eukaryote RNA polymerases.Discuss the following questions (Essay questions)1. Describe the similarity and dissimilarity of replication and transcription.Chapter 12 Biosynthesis of proteinExplain the following terms1. translate2. polyribosomes3. genetic code4. degeneracy of codonAnswer the following questions briefly1. Describe briefly the RNAs involved in the protein synthesis and their functions in that process.2. Outline the main features of the genetic code.3. Describe briefly the dissimilarity of translation initiation complex formation of prokaryotes and eukaryotes.Discuss the following questions (Essay questions)1. Describe the materials involved in protein biosynthesis and their functions in that process.3. Please comparing the process of translation of prokaryotes and eukaryotes.Chapter 13 The regulation of gene expressionExplain the following terms1. gene expression2. cis-acting element3. trans-acting factor4. operon5. general transcription factor6. enhancerAnswer the following questions briefly1. What is biological significance of regulation of gene expression?2. Outline the function of each component of operon.3. What characteristics does eukaryotic genome structure have?Discuss the following questions (Essay questions)1. Explain the regulation mechanism of lactose operon.Chapter 14 Gene recombination and gene engineeringExplain the following terms1. restriction endonuclease2. genomic DNA3. vector4. cDNA. library5. genetic engineering6. DNA cloning7. homologous recombinationAnswer the following questions briefly1. What are the main selection criteria of gene vector?2. What is the significance of restriction endonuclease of bacteria themselves?3. At present, How many ways to get target genes?4. Outline the basic process of DNA cloning.Discuss the following questions (Essay questions)1. Why plasmid can be used as the vector of genetic engineering?2. Explain how to connect the foreign gene and the vector.3. What is α-complementary? Explain how to screening recombinant by it using an example.Chapter 15 Cellular signal transductionExplain the following terms1. signal transduction2. receptor3. ligand4. signal transduction pathway5. protein kinase6. second messenger7. G proteinAnswer the following questions briefly1. Describe briefly which protein kinases are regulated by intracellular second messenger.2. Outline the classification of receptor and its chemical signals.3. Describe briefly the basic mode of G protein-coupled receptor (seven transmembrane receptor)-mediated signal transduction.4. Describe briefly the signal transduction pathway of intracellular receptor of steroid hormone.Discuss the following questions (Essay questions)1. How does intracellular receptor play its function?2. Explain the process of the glycogen metabolism regulated by glucagon.3. Use fat mobilization as an example, explain the process of cAMP-protein kinase pathway. Chapter 16 Blood biochemistryExplain the following terms1. 2, 3-BPG shuntAnswer the following questions briefly1. Outline the function of plasma protein.Chapter 17 Liver biochemistrExplain the following terms1 biotransformation 2. primary bile acid 3. secondary bile acid4. bile pigment5. jaundiceAnswer the following questions briefly1. Describe briefly the physiological significance of biotransformation.2. Outline the main physiological functions of bile acids.3. Describe briefly production and blood transportation of bilirubin.Discuss the following questions (Essay questions)1. Describe the influence factor of biotransformation.2. Explain the dissimilarity of unconjugated and conjugated bilirubin.Chapter 18VitaminsExplain the following terms1. vitamin2. lipid-soluble vitamin3. water-soluble vitaminAnswer the following questions briefly1. Outline the biochemical function of vitamin E.2. Describe briefly the biochemical function of vitamin D and its deficiency disease.Discuss the following questions (Essay questions)1. Explain the relationship between the water-soluble vitamin and the coenzyme. Chapter 20 Oncogenes, tumor suppressor genes and growth factorExplain the following terms1. oncogene2. proto-oncogene3. tumor suppressor geneAnswer the following questions briefly1. Describe characteristics of proto-oncogene.2. Describe briefly wild-type p53 tumor suppressor gene mechanism.Chapter 21 The Principle and Application of Common Used Techniques in Molecular Biology Explain the following terms1. probe2. PCR3. Gene diagnosis4. gene therapyDiscuss the following questions (Essay questions)1. Describe the definition, type and application of the blotting technique.2. Describe the PCR reaction principle and the basic steps.。

chapter 3 enzymes

Induced-fit Theory
substrate
Complex of substrate-enzyme enzyme
Mechanisms Proximity effect and orientation arrange: For a biochemical reaction to occur, the substrate must come into close proximity to catalytic functional groups (side chain groups involved in a catalytic mechanism ) within the active site. In addition, the substrate must be precisely, spatially oriented to the catalytic groups. Once the substrate is correctly positioned, a change in the enzyme’s conformation may result in a strained enzymesubstrate complex. This strain helps to bring the enzyme-substrate complex into the transition state.
3
Enzyme kinetics
The rate or velocity of a biochemical reaction is defined as the change in the concentration of a reactant or product per unit time. Plotting initial velocity v versus substrate concentration [S].The rate of the reaction is directly proportional (first order reaction) to substrate concentration only when [S] is low. When [S] becomes sufficiently high that the enzyme is saturated, the rate of the reaction is zero-order with respect to substrate.

生化英文名词解释

名词解释Glossary第一章蛋白质的结构与功能Chapter 1 Structure and Function of Proteinpeptide bond（肽键）：a covalent bond linking the α- amino group of one amino acid and theα-carboxyl group of another in a protein molecule.peptide（肽）：a molecule containing two or more amino acids linked by peptide bond. primary structure of protein（蛋白质的一级结构）：the amino acid sequence of a polypeptide.secondary structure of protein（蛋白质的二级结构）：the spatial arrangement of local portions of a polypeptide chain.tertiary structure of protein（蛋白质的三级结构）：the spatial arrangement of all the atoms of a protein or a subunit.quaternary structure of protein（蛋白质的四级结构）：the spatial arrangement of a protein that consists of more than one folded polypeptide chain or subunit.subunit（亚基）：an individual polypeptide chain that associates with one or more separate chains to form a complete protein.motif（模序）：a substructure formed with two or more secondary-structure peptide segments that are drawn close to each other.domain（结构域）：a region within a protein, particularly within a large polypeptide, that functions in a semi-independent manner.positive cooperativity（正协同效应）：an effect that the binding of one ligand to a protein facilitates the subsequent ligand binding.allosteric effect（变构效应）：an effect that a small molecule, called an effector, noncovalently binds to a protein and alters its activity.isoelectric point（pI）of protein （蛋白质的等电点）：the pH at which a protein has an equal number of positive and negative charges and hence bears no net charge. denaturation of protein（蛋白质变性）： the disruption of the natively folded structure of a protein caused by exposure to heat, radiation, or chemicals, or change in pH, that leads to an alteration of chemical, physical and biological properties of the第二章核酸的结构与功能Chapter 2 Structure and Function of Nucleic Aciddenaturation of DNA（DNA的变性）：the disruption of the native conformation of DNA by separation of the DNA double helix into its two component strands, due to heat, chemicals, or change in pH, etc.hyperchromic effect（增色效应）：the increase in ultraviolet absorbance of a DNA while the DNA is denatured.melting temperature（Tm, 融解温度）：the temperature corresponding to half the maximal increase in ultraviolet absorbance of a thermally denatured DNA.annealing（退火）：the process of returning a thermally denatured DNA to its original native structure when it is cooled gradually.第三章酶Chapter 3 Enzymessimple enzyme（单纯酶）：an enzyme that consists of only polypeptide chain(s). conjugated enzyme（结合酶）：an enzyme with its polypeptide portion(apoenzyme) linked to one or more substance other than amino acids, such as metals or small organic molecules.holoenzyme（全酶）：a complete enzyme consisting of the apoenzyme portion plus the cofactor component.essential group（必需基团）： a chemical group on the side chain of amino acid residue of an enzyme that is closely related to the activity of the enzyme.active center / active site（活性中心）：the region of an enzyme molecule that contains the substrate binding site and the catalytic site for converting the substrate(s) into product(s).activation energy（活化能）：the threshold energy that must be overcome to produce a chemical reaction.absolute specificity（绝对特异性）：the extreme selectivity of an enzyme that allows it to catalyze only the reaction with a single substrate in the case of a monomolecular reaction, or the reaction with a single pair of substrates in the case of a bimolecularrelative specificity（相对特异性）：the relative selectivity of an enzyme that allows it to catalyze the reaction with one type of reactants or one type of chemical bond. stereospecificity（立体异构特异性）：the selectivity of an enzyme for a particular stereoisomer.zymogen（酶原）：the inactive precursor of an enzyme.zymogen activation（酶原激活）：the process in which a zymogen is converted to an active enzyme by limited proteolysis and subsequently the active center of the enzyme is formed or exposed.isoenzyme（同工酶）：multiple forms of an enzyme that catalyze the same reaction but differ from one another in one or more of the properties, such as structural, physical, chemical and even immunological properties.第四章糖代谢Chapter 4 Carbohydrate Metabolismglycolysis（糖酵解）： the anaerobic degradation of carbohydrate whereby a molecule of glucose is converted to two molecules of lactic acid.substrate-level phosphorylation（底物水平磷酸化）：the synthesis of ATP from ADP by the phosphorylation of ADP coupled with exergonic breakdown of a high-energy organic substrate molecules.Pastuer effect（巴斯德效应）：the phenomenon that the glycolytic pathway is inhibited under aerobic conditions.glycogen（糖原）： a highly branched polymer of glucose residues primarily in 1,4 linkage but with 1,6 linkage at branchpoints.gluconeogenesis（糖异生）： the synthesis of glucose or glycogen from noncarbohydrate molecules, i.e., lactic acid, glycerol, glucogenic amino acids, etc.第五章脂类代谢Chapter 5 Lipid Metabolismessential fatty acids（必需脂肪酸）： the fatty acids, including linoleic acid, linolenic acid, and arachidonic acid, which can not be synthesized in the mammalian body and must be obtained from diet.mobilization of fat（脂肪动员）： a process of lipolysis in which the fat stored in adipose tissues is converted to free fatty acids and glycerol, which are consequently released into blood so that they can be used in other tissues.β-oxidation of fatty acid（脂肪酸的β-氧化）： a process in which a fatty acid is degraded through a sequential removal of two-carbon fragments from the carboxyl end and therefore acetyl CoA is formed as the bond between the α- and β-carbon atoms is broken.ketone bodies（酮体）： a group of molecules, i.e., acetone, acetoacetate, and β–hydroxybutyrate, that are synthesized in the liver from acetyl CoA.第六章生物氧化Chapter 6 Biological Oxidationrespiratory chain （呼吸链）/ electron transfer chain（电子传递链）： a series of electron carriers responsible for the transport of reducing equivalent from metabolite to molecular oxygen, with the net results of capturing energy for use in ATP synthesis, and of the reduction of oxygen to water.P/O ratio（P/O比值）： the number of molecules of Pi consumed in ATP formation for each oxygen atom reduced to H2O.oxidative phosphorylation（氧化磷酸化）： the process in which the phosphorylation of ADP to yield ATP is coupled to the electron transport through respiratory chain. uncoupler（解偶联剂）： a molecule, such as dinitrophenol, that uncouples ATP synthesis from electron transport.第七章氨基酸代谢Chapter 7 Amino Acid Metabolismessential amino acids（必需氨基酸）： the amino acids，including valine, leucine, isoleucine, threonine, phenylalanine, tryptophan methionine and lysine, that cannot be synthesized by animal body and must therefore be supplied by diet. transdeamination（联合脱氨基作用）： the coupled action of an aminotransferase and a glutamate dehydrogenase involved in deamination of the majority of amino acids. transamination（转氨基作用）： a reaction catalyzed by an aminotransferase, in which an amino group is transferred from an amino acid to a keto acid.ketogenic amino acids（生酮氨基酸）： the amino acids that can be converted to ketone bodies, i.e., leucine and lysine.glucogenic and ketogenic amino acids（生糖兼生酮氨基酸）： the amino acids, i.e., isoleucine, phenylalanine, tyrosine, threonine and tryptophan, that can be converted to either ketone bodies or carbohydrates.one carbon units（一碳单位）/ one carbon groups（一碳基团）： organic groups, including methyl(—CH3), methylene(—CH2—), methenyl(—CH＝), formyl(—CHO) and formimino(—CH＝NH) groups, each containing only one carbon atom generated through catabolisms of some amino acids.第八章核苷酸代谢Chapter 8 Nucleotide Metabolismthe de novo pathway of nucleotide synthesis（核苷酸的从头合成途径）： a pathway through which nucleotides are synthesized by using simple molecules, such as ribose 5-phosphate, amino acids, one carbon units and carbon dioxide.the salvage pathway of nucleotide synthesis（核苷酸的补救合成途径）： a pathway through which nucleotides are synthesized by using the existing nitrogenous bases or nucleosides.第九章物质代谢的联系与调节Chapter 9 Integration and Regulation of Metabolismkey enzyme（关键酶）/ pacemaker enzyme（限速酶）/ regulatory enzyme（调节酶）：an enzyme that sets the rate for the entire biochemical pathway, usually catalyzes the slowest and irreversible step, and can be regulated by a number of metabolites and effectors in addition to its substrates.allosteric regulation（变构调节）： a regulatory mechanism through which a specific low-molecular-weight molecule, called an effector or a modulator, noncovalently binds to a regulatory site outside the active center of a regulatory enzyme and alters the conformation and activity of the enzyme.chemical modification（化学修饰调节）： a regulatory mechanism through which enzyme activities are regulated by means of reversible interconversion between the active and inactive forms of the enzyme resulted from enzyme-catalyzed covalent modificationto a specific amino acid residue.第十章 DNA的生物合成（复制）Chapter 10 Biosynthesis of DNA (Replication)replication（复制）：a process in which an exact copy of parental DNA is synthesized by using each polynucleotide strand of the parental DNA as templates. semiconservative replication（半保留复制）： duplication of DNA after which the daughter duplex carries one parental strand and one newly synthesized strand.DNA polymerase（DNA聚合酶）：any of various enzymes, with the full name of DNA dependent DNA polymerase, that catalyzes the formation of polynucleotides of DNA using an existing strand of DNA as a template.point mutation（点突变）：a mutation that causes the replacement of a single base pair with another, including nonsense mutation, missense mutation and silent mutation. frameshift mutation（框移突变）：a mutation of insertion or deletion of a genetic material that leads to a shift in the translation of the reading frame, resulting in a completely different translation.reverse transcriptase（逆转录酶）：any of various enzymes, with the full name of RNA dependent DNA polymerase, that catalyzes the formation of polynucleotides of DNA using an existing strand of RNA as a template.telomeres（端粒）： structures that occur at the ends of eukaryotic chromosomes that prevent the unraveling of DNA.第十一章 RNA的生物合成（转录）Chapter 11 Biosynthesis of RNA (Transcription)RNA polymerase（RNA聚合酶）：any of various enzymes, with the full name of DNA dependent RNA polymerase, that catalyzes the formation of polynucleotides of RNA using an existing strand of DNA as a template.promoter（启动子）： a DNA sequence immediately before a gene that is recognized by RNA polymerase and signals the start point of transcription.intron（内含子）： a noncoding intervening sequence in a split or interrupted gene that is missing in the final RNA product.exon（外显子）： the region in a split or interrupted gene that codes for RNA which endup in the final product (e.g., mRNA).ribozyme（核酶）：ribonucleic acid with catalytic ability whose substrate is ribonucleic acid.第十二章蛋白质的生物合成（翻译）Chapter 12 Biosynthesis of Proteins (Translation)reading frame（阅读框）： a group of three nonoverlapping nucleotides that is read asa codon during protein synthesis. The reading frame begins with the initiator codonAUG.molecular chaperon (分子伴侣)：a sort of intracellular conservative protein, which can recognize the unnatural conformation of peptide and assist in the accurate folding of domains or the whole protein.signal peptide（信号肽）： a sequence of amino acid residues located at the N-terminal portion of a nascent secretory protein, which marks the protein for translocation across the rough endoplasmic reticulum.第十三章细胞信息转导Chapter 13 Cell Signalingprimary messenger（第一信使）： an extracellular signaling molecule that is released from the signaling cell and can regulate the physiological activity of the target cell.secondary messenger（第二信使）： a small intracellular molecule, such as Ca2+,cAMP, cGMP, diacylglycerol (DAG), inositol triphosphate (IP3), ceramide, or arachidonic acid (AA), etc., that is formed at the inner surface of the plasma membrane in response to a primary messenger.receptor （受体）： a molecular structure on the surface or interior of the target cell that specifically binds signaling molecule and initiates a response in the cell. ligand（配体）： a biologically active molecule that can bind to its specific receptor.G protein （G蛋白）/ guanylate binding proteins （鸟苷酸结合蛋白）：a trimeric guanylatebinding protein in the cytoplasmic side of plasma membrane that acts as a switch to turn activities on and off by interconversion between its monomeric GTPase andtrimeric GDP binding form.hormone response element （激素反应元件，HRE）：a specific DNA sequence that binds hormone-receptor complex; The binding of a hormone-receptor complex either enhances or diminishes the transcription of a specific gene.第十四章血液的生物化学Chapter 14 Biochemical Aspects of Bloodnon-protein nitrogen（非蛋白氮）：nitrogen contained in urea, creatine, creatinine, uric acid, bilirubin, and ammonia.acute phase protein（急性时相蛋白质）：a protein whose plasma concentration can be altered when acute inflammation or a certain type of tissue damage occurs.2,3-bisphosphoglyerate shunt（2,3-二磷酸甘油支路）：the pathway in erythrocyte glycolysis in which glycerate 1,3-bisphosphate(1,3-BPG) is isomerized to 2,3-bisphosphoglyerate(2,3-BPG) and the latter is consequently hydrolyzed to form 3-phosphoglycerate. The importance of 2,3-BPG in the erythrocyte lies in its ability to alter the extent to which hemoglobin binds with oxygen.第十五章肝的生物化学Chapter 15 Biochemical Aspects of the Liverbiotransformation（生物转化）： a series of enzyme-catalyzed processes through which non-nutritional molecules, which are usually hydrophobic, are converted into more soluble metabolites.jaundice（黄疸）： a clinical manifestation of hepatic disease, featuring yellow discolration of the plasma, skin, and mucous membranes, caused by bilirubin accumulation and staining.。

药理学医学英语词汇.

协同作用治疗效应治疗指数阈浓度毒性反应
Chapter 3 Pharmacokinetics
英文 absorption active transport apparent volume of distribution(vd) bioavailability biotransformation blood-brain-barrier clearance, cl distribution drug transport rate elimination enzyme inducer enzyme inhibitor first order kinetics first-pass effect half life( t1/2) hepatoenteral circulation maintenance dose metabolism one-compartment model passive diffusion peak concentration (cmax ) placental barrier redistribution of drugs steady state concentration(css ) Plateau concentration time-concentration curve two-compartment model zero order kinetics
中文卡巴胆碱胆碱酯酶抑制剂胆碱受体激动剂调节麻痹调节痉挛加兰他敏新斯的明毒扁豆碱毛果芸香碱有机磷酸酯类胆碱酯酶复活剂
Chapter 7 Cholinoceptor blocking drugs
英文
anisodamine
atropine
homatropine
pirenzepine

生物化学第三章酶化学

通式：AH2+B→BH2+A
系统命名可分为19亚类，习惯上可分为4个亚类： (1)脱氢酶：受体为NAD或NADP，不需氧。
(2)氧化酶：以分子氧为受体，产物可为水或H2O2，常需黄素辅基。
(3)过氧化物酶：以H2O2为受体，常以黄素、血红素为辅基。 (4)氧合酶（加氧酶）：催化氧原子掺入有机分子，又称羟化酶。按
His 活性中心重要基团: His57 , Asp102 , Ser195
Asp
3 活性中心的研究方法 1.酶分子侧链基团修饰法 (1)非共价特异修饰法： (2)特异性共价修饰法 (3)亲和标记法
2.动力学参数测定方法 3.X－射线晶体结构分析法 4.定点诱变法
二酶原及酶原的激活没有催化活性的酶的前体称为酶原（zymogen）。
V max 初速度 v c b 1/2 V max
a
0
Km
[S]
图5-14 底物浓度对酶促反应速度的影响
酶促反应速度V与底物浓度[S]的关系
（二）Michaelis-Menten方程和米氏常数
米氏方程式推导来源于中间产物学说解释酶促反应中底物浓度和反应速率关系的最合理的
学说是中间产物学说。该学说认为酶促反应形成酶－

通式： AB→A+B

包括醛缩酶、水化酶、脱羧酶等。共7个亚类。
5、异构酶类催化同分异构体之间的相互转化。

通式：A→B
其中：A、B为同分异构

包括消旋酶、异构酶、变位酶等。共6个亚类。
6、合成酶类催化由两种物质合成一种物质，必须与ATP 分解相偶联。也叫连接酶，如DNA连接酶。
通式：A+B+ATP→AB+ADP+Pi 或 A+B→AB+AMP+PPi

药事管理ppt课件

抽样；受理药品、医疗器械、餐饮服务环节食品和保健食品、
化妆品违法案件的举报，并依法查处制售假冒伪劣药品、医疗
器械、餐饮服务环节食品和保健食品、化妆品违法案件；协助
对食品重大事故进行查处。
二、国家和省级药品监督管理部门职能
国家食品药品监督管理局
办公室
局
药品注册司
内
安全监管司
设司
市场监督司
室
食品安全监管司
药事管理体制一般可分解为药品质量监督管理体
制，药品生产经营管理体制，药学教育和科技管理体制。
第二节药品监督管理组织
一、药品监督管理组织体系
国务院
省级人民政府
国家食品药品监督管理局
省级食品药品监督
省
管理局
级
以
下垂直
市级食品药品监局管理局
管
理
县级食品药品监督
管理分局
领导关系 -------- 指导关系
直属单位内设机构(一)办公室（财务股）
（二）食品化妆品监督管理股
（三）药品医疗器械监督管理股
（四）医药经济发展股
直属单
霍山县食品药品监位督管理所
主要职责：
受县食品药品监督管理局委托，依法对餐饮服务环节是食
品安全、药品、医疗器械生产、经营企业和医疗机构的药品、
医疗器械质量进行稽查、抽样；依法对保健食品、化妆品稽查、
8. 拟定和完善执业药师资格准入制度，监督和指导执业药师注册工作。
9. 组织培训药品监督管理干部。 10. 组织药品质量管理和麻醉药品、精神药品方面的国际交流，承办有关国际合作事项。 11. 承办国务院交办的其他事项。
（二）省级药品监督管理部门的职能

3 Enzymes and Enzyme Kinetics - Comprehensive …：3酶和酶动力学综合…

(S)-lactate
(R)-lactate
6: ligases
• involve the synthesis of various bonds with
the concomitant breakdown of energycontaining compounds like ATP.
pyruvate
acetaldehyde + CO2
5: isomerases
• involve the isomerization of a molecule
Example:
Common name: lactate racemase
Formal name: lactate racemase EC 5.1.2.1
acetyl CoA + phosphate
CoA + acetylphosphate
3: hydrolases
• involve hydrolytic reactions, using water to
break bonds
Example:
Common name: oxaloacetase
Formal name: oxaloacetate acetylhydrolase EC 3.7.1.1
A.B.C.D
/iubmb/enzyme
1: oxidoreductases
• involve transfer of hydrogen, oxygen or
electrons between substrates
• require a hydrogen (or electron) donor and a
• Formal names have been assigned by

Enzyme酶

研究作出更大的贡献
第一节酶的分子结构与功能一、酶的分子组成
酶分子可根据其化学组成的不同，分为两类：单纯酶
酶→
酶蛋白
结合酶（全酶）→
辅酶
辅助因子→ 辅基
金属离子
由酶蛋白与辅助因子组成的酶称为全酶。
与酶蛋白疏松结合并与酶的催化活性有关的耐热低分子有机化合物称为辅酶。
与酶蛋白牢固结合并与酶的催化活性有关的耐热低分子有机化合物称为辅基。
催化反应历程
一般化学反应历程： S →P
酶促反应历程： S+E →
ES → E + P
（二）具有高度的底物特异性 l 一种酶只作用于一种或一类化合物，以促进一定的化学变化，生成一定的产物，这种现象称为酶作用的特异性。
一种酶只作用于一类化合物或一定的化学键，以促进一定的化学变化，并生成一定的产物，这种现象称为酶的特异性或专一性(specificity)。受酶催化的化合物称为该酶的底物或作用物(substrate)。
三、酶促反应的机制
（一）中间复合物学说
酶催化时，酶活性中心首先与底物结合生成一种酶-底物复合物（ES），此复合物再分解释放出酶，并生成产物。
S + E → SE → E + P
（二）诱导契合学说
当底物与酶接近时，底物分子可以诱导酶活性中心的构象发生改变，使之成为能与底物分子密切结合的构象。
丙二酸对琥珀酸脱氢酶的竞争性抑制
H2N-
-COOH对氨基苯甲酸
H2N-
-SO2NH对氨R 基苯磺酰胺
磺胺类药物对二氢叶酸合成酶的竞争性抑制
某些抑制剂的化学结构与底物相似，因而能与底物竟争与酶活性中心结合。当抑制剂与活性中心结合后，底物被排斥在反应中心之外，其结果是酶促反应被抑制了。

Lehninger Principles of Biochemistry 习题答案chapter 3

12
11.30 9.60 (IV)
P O
C
NH2
(V)
10
8 5.97
pH
6
(III)
4 2.34 2 (I) 0.5 1.0 1.5 2.0 OH (equivalents) (II)
0
Note: before considering statements (a) through (o), refer to Figure 3–10. The three species involved in the titration of glycine can be considered in terms of a useful physical analogy. Each ionic species can be viewed as a different floor of a building, each with a different net charge:
S-26
2608T_ch03sm_S26-S43
2/1/08
11:45AM
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Chapter 3 Amino Acids, Peptides, and Proteins
S-27
H3NOCH2OCOOH H3NOCH2OCOO H2NOCH2OCOO
CH3 H3N C H C O O H2N CH3 C H C OH O
Zwitterionic
Uncharged
(a) Why is alanine predominantly zwitterionic rather than completely uncharged at its pI? (b) What fraction of alanine is in the completely uncharged form at its pI? Justify your assumptions. Answer (a) The pI of alanine is well above the pKa of the a-carboxyl group and well below the pKa of the a-amino group. Hence, at pH pI, both groups are present predominantly in their charged (ionized) forms. (b) From Table 3–1, the pI of alanine is 6.01, midway between the two pKa values 2.34 and 9.69. From the Henderson-Hasselbalch equation, pH pKa log ([A ]/[HA]). For the carboxyl group: log [A ] [HA] [HA] [A ] 6.01 10

分子生物学英文版Chapter3

CHAPTER 3 Transcription3.1 Outline of Transcription3.2 Transcription in Prokaryotes 3.3 Transcription in Eukaryotes 3.4 RNA Splicing and ProcessingCentral Dogma3.1 Outline of TranscriptionKey Terms•Transcription: a DNA segment that constitutes a gene is read and transcribed into a single stranded sequence of RNA.•The sense strand(coding strand)of DNA has the same sequence as the mRNA and is related by the genetic code to the protein sequence that it represents.•The antisense strand(Template strand)of DNA is complementary to the sense strand, and is the one that acts as the template for synthesis of mRNA.•A promoteris a region of DNA where RNA polymerase binds to initiate transcription.•Startpoint (startsite) refers to the position on DNAcorresponding to the first base incorporated into RNA. •A terminator is a sequence of DNA that causes RNA polymerase to terminate transcription.Key TermsTranscription unitEnzymatic synthesis of RNADNA templaterN′TP+n rNTP rN′TP-(rNMP)n +nPPiRNA-P, Mg2+RNA合成:前体为4种5′-核苷三磷酸(rNTP) —ATP,GTP,CTP和UTP;模板为DNA双链分子中的一条链;催化合成的酶为RNA polymerase;不需要引物,直接开始新生RNA链的延伸;碱基配对原则:A-U(T), C-G;聚合反应中生成磷酸二酯键,释放出PPi;新生RNA链的延伸方向: 5′→3′3.2 Transcription in Prokaryotes3.2.1 RNA polymerases3.2.2 Promoter recognition3.2.3 Initiation and elongation of transcription 3.2.4 Two types of terminators in E.coli3.2.1 RNA polymeraseRNA聚合酶核心酶：α2ββ′RNA聚合酶全酶：α2ββ′σRNA聚合酶各亚基的功能（见左图）Sigma factor changes the DNA-binding properties of RNApolymerase so that its affinity for general DNA is reduced and its affinity for promoters is increased. E.coli has several sigma factors, each of which causes RNApolymerase to initiate at a set of promoters defined by specific –35 and –10 sequences.The sigma subunit is required only fortranscription initiation3.2.2 Promoter recognitionThe promoter has three components1）-10区, 又称Pribnow Box保守序列为T80A95T45A60A50T96。

Assignments-III

Problems for Chapter 88.1 Enzyme kineticsLactase, also known as β-galactosidase, catalyses the hydrolysis of lactose to produce glucose and galactose from milk and whey. Experiments are carried out to determine the kinetic parameters for the enzyme. Initial rate data are listed below.Lactose concentration mol l-1⨯ 103Initial reaction velocity mol l-1 min-1⨯ 1032.50 2.27 1.84 1.35 1.25 0.73 0.46 0.20 1.94 1.91 1.85 1.80 1.78 1.46 1.17 0.78Evaluate νmax and K m.8.2 Effect of temperature on hydrolysis of starchα-Amylase from malt is used to hydrolyze starch. The dependence of initial reaction rate on temperature is determined experimentally. Results measured at fixed starch and enzyme concentrations are listed below.Temperature︒C Rate of glucose production mmol m-3 s-120 30 40 50 0.310.661.20 6.33(a)Determine the activation energy for this reaction.(b) α-Amylase is used to break down starch in baby food. It is proposed to carry out the reaction at a relatively high temperature so that the viscosity is reduced. What is the reaction rate at 55 ︒C compared with 25 ︒C? (c) Thermal deactivation of this enzyme is described by the equation: k d = 2.25 ⨯ 1027RT e /41630-where k d is the deactivation rate constant in h -1, R is the ideal gas constant in cal gmol -1K -1, and T is temperature in K. What is the half-life of the enzyme at 55 ︒C compared with 25 ︒C? Which of these two operating temperatures is more practical for processing baby food?8.3 Growth parameters for hairy rootsHairy roots are produced by genetic transformation of plants using Agrobacterium rhizogenes . The following biomass and sugar concentration were obtained during batch culture of Atropa belladonna hairy roots in a bubble-column fermenter. Time(d)Biomass (g l -1 dry weight)Sugar (g l -1)Time (d) Biomass (g l -1 dry weight) Sugar (g l -1) 0510152025 0.64 1.95 4.21 5.54 6.98 9.50 30.0 27.4 23.6 21.0 18.4 14.8 30 35 40 45 50 55 10.3 12.0 12.7 13.1 13.5 13.7 13.3 9.7 8.0 6.8 5.7 5.1 (a) Plot μ as a function of culture time. When is the growth rate maximum? (b) Plot the specific rate of sugar uptake as a function of time.(c) What is the observed biomass yield from substrate? Is Y X/S ’ constant?8.4 Ethanol fermentation by yeast and bacteriaEthanol is produced by anaerobic fermentation of glucose by Saccharomyces cerevisiae . For the particular strain of S. cerevisiae employed, the maintenance coefficient is 0.18 kg kg -1h -1, Y X/S is 0.11 kg kg -1, Y P/X is 3.9 kg kg -1 and μmax is 0.4 h -1. It is decided to investigate the possibility of using Zymomonas mobilis bacteria instead of yeast for making ethanol. Z. mobilisis known to produce ethanol under anaerobic conditions through a different metabolic pathway to that employed by yeast. Typical values of Y X/S are lower than for yeast at about 0.06 kg kg-1; on the other hand, the maintenance coefficient is higher at 2.2 kg kg-1. Y P/X for Z. mobilis is 7.7 kg kg-1; μmax is 0.3 h-1.(a)From stoichiometry, what is the maximum theoretical yield of ethanolfrom glucose?(b)Y p/x’ is maximum and equal to the theoretical yield when there is zerogrowth and all substrate entering the cell is used for maintenance activities. If ethanol is the sole extracellular product of energy-yielding metabolism, calculate m for each organism.(c)S. cerevisiae and Z. mobilis are cultured in batch fermenters. Predict theobserved product yield from substrate for the two cultures.(d)What is the efficiency of ethanol production by the two organisms?Efficiency is defined as the observed product yield from substrate divided by the maximum or theoretical product yield.(e)How does the specific rate of ethanol production by Z. mobilis comparewith that by S. cerevisiae?(f)Using Eq.(8.80), compare the proportions of growth-associated andnon-growth-associated ethanol production by Z. mobilis and S. cerevisiae.For which organism is non-growth-associated production more substantial?(g)In order to achieve the same volumetric ethanol productivity from thetwo cultures, what yeast concentration is required compared with the concentration of bacteria?(h)At zero growth, the efficiency of ethanol production is the same in bothcultures. Under these conditions, if the same concentration of yeast and bacteria are employed, what size fermenter is required for the yeast compared with the bacteria in order to achieve the same total productivity?(i)Predict the observed biomass yield from substrate for the two organisms.For which organism is biomass disposal less of a problem?(j)Make a recommendation about which organism is better suited for industrial ethanol production, and give your reasons.8.5 Plasmid loss during culture maintenanceA stock culture of plasmid-containing Streptococcus cremoris cells is maintained with regular sub-culturing for a period of 28 d. After this time, the fraction of plasmid-carrying cells is measured and found to be 0.66. The specific growth rate of plasmid-free cells at the storage temperature is 0.033 h-1; the specific growth rate of plasmid-containing cells is 0.025 h-1. If all the cells initially contained plasmid, estimate the probability per generation of plasmid loss.8.6 Medium sterilizationA steam steriliser is used to sterilize medium for fermentation. The initial concentration of contaminating organisms is 108 per liter. For design purpose, the final acceptable level of contamination is usually taken to be 10-3 cells; this corresponds to a risk that one batch in a thousand will remain contaminated even after the sterilization process is complete. For how long should 1 m3 medium be treated if the temperature is:(a)80 ︒C?(b)121 ︒C?(c)140 ︒C?Problems for Chapter 99.1 Diffusion and reaction in a waste treatment lagoon Industrial wastewater is often treated in large shallow lagoon. Consider such a lagoon covering land of area A. Microorganisms form a sludge layer ofsludge layer, thereby establishing a concentration gradient across the thickness L.(a) Set up a shell mass balance on substrate by considering a thin slice of sludge of thickness ∆z perpendicular to the direction of diffusion. The rate of microbial reaction per unit volume sludge is:r s = k1swhere s is the concentration of substrate in the sludge layer (gmol cm-3) and k1 is the first order rate constant (s-1). The effective diffusivity of substrate in sludge is D Se. Obtain a differential equation relating s and z.(b) External mass-transfer effects at the liquid-sludge interface are negligible. What are the boundary conditions for this problem?(c) The differential equation obtained in (a) is solved by making the substitution:s = Ne Pzwhere N and P are constants.1) Substitute this expression for s into the differential equation derived in (a) to obtain an equation for P . (Remember thatP P ±=2)2) Because there two possible values of P , let:s = Ne pz + Me -PzApply the boundary condition at z = 0 to this expression and obtain a relationship between N and M .3) Use the boundary condition at z = L to find N and M explicitly. Obtain an expression for s as a function of z .4) Use the definition of cosh x : 2coxh xx e e x -+= to prove that:)/( cosh )/( cosh 11Se Se b D k L D k z s s = (d) At steady state, rate of substrate consumption must be equal to the rate at which substrate enters the sludge. As substrate enters the sludge by diffusion, the overall rate of reaction can be evaluated using Fick’s lawL z Se obs A dz dsA D r ==,Use the equation for s from (c) to derive an equation for r A,obs .(e) Show from the result of (d) that the internal effectiveness factor is given by the expression:111i tanh φφ=η whereSeD k L 11=φ andxx x cosh sinh tanh = (f) Plot the concentration profiles through a sludge layer of thickness 2 cm for the following sets of conditions:k 1 (s -1)D Ae (cm 2 s -1) (1) 4.7 ⨯ 10-8 7.5 ⨯ 10-7 (2) 2.0 ⨯ 10-7 2.0 ⨯ 10-7 (3) 1.5 ⨯ 10-4 6.0 ⨯ 10-6 Take s b to be 10-5 gmol cm -3. Label the profiles with corresponding values of φ1 and ηi1. Comment on the general relationship between φ1, the shape of the concentration profile, and the value of ηi1.9.2 Oxygen profile in immobilized enzyme catalystL-Lactate 2-monooxygenase from Mycobacterium smegmatis is immobilized in spherical agarose beads. The enzyme catalyzes the reaction:C 3H 6O 3 + O 2 → C 2H 4O 2 + CO 2 + H 2O Beads 4 mm in diameter are immersed in a well-mixed solution containing 0.5 mM oxygen. A high lacftic acid concentration is provided so that oxygen is the only rate-limiting substrate. The effective diffusivity of oxygen in agarose is 2.1 ⨯ 10-9 m 2 s -1. K m for the immobilized enzyme is 0.015 mM; νmax is 0.12 mol s -1 per kg enzyme. The beads contain 0.012 kg enzyme m -3 gel. External mass-transfer effects are negligible.(a) Plot the ixygen concentration profile inside th ebeads.(b) What fraction of the catalyst volume is active?(c) Determine the largest bead size that allows the maximum conversion rate.9.3 Effect of oxygen transfer on recombinant cellsRecombinant E. coli cells contain a plasmid derived from Pbr322 incorporating genes for the enzyme β-lactamase and catechol 2,3-dioxygenase from Pseudomonas putida . To produce th edesired enzymes th eorganism requires aerobic conditions. The cells are immobilized in spherical beads of carrageenan gel. The effective diffusivity of oxygen is 1.4 ⨯ 10-9 m 2 s -1. Uptake of oxygen is zero order with intrinsic rate constant 10-3mol m-3 (particle) s-1. The concentration of oxygen at the surface of the catalyst is 8 ⨯ 10-3 kg m-3. Cell growth is negligible.(a)What is the maximum particle diameter for aerobic conditionsthroughout the catalyst?(b)For particles half the diameter calculated in (a), what is the minimumoxygen concentration in the beads?(c)The density of cells in the gel is reduced by a factor of five. If specificactivity is independent of cell loading, what is the maximum particle size for aerobic conditions?9.4 Ammonia oxidation by immobilized cellsThiosphaera pantotropha is being investigated for aerobic oxidation of ammonia to nitrite in wastewater treatment. The organism is immobilized in spherical agarose particles of diameter 3 mm. The effective diffusivity of oxygen in the particles is 1.9 ⨯ 10-9 m2 s-1. The immobilized cells are placed in a flow chamber for measurement of oxygen uptake rate. Using published correlations, the liquid-solid mass-transfer coefficient for oxygen is calculated as 6 ⨯ 10-5 m s-1. When the bulk oxygen concentration is 6 ⨯ 10-3 kg m-3, the observed rate of oxygen consumption is 2.2 ⨯ 10-5 kg m-3 (catalyst) s-1.(a)What effect does external mass-transfer have on respiration rate?(b)What is the effectiveness factor?(c)For optimal activity of cells, oxygen level must be kept above the criticallevel, 1.2 ⨯ 10-3 kg m-3. Is this condition satisfied?9.5 Microcarrier culture and external mass transfer Mammalian cells form a monolayer on the surface of microcarrier beads of diameter 120 μm and density 1200 kg m-3. The culture is maintained in spinner flasks in serum-free medium of viscosity 10-3 N s m-2 and density 1000 kg m-3. The diffusivity of oxygen in the medium is 2.3 ⨯ 10-9 m2 s-1. The observed rate of oxygen uptake is 0.015 mol s-1 m-3 at a bulk oxygen concentration of 0.2 mol m-3. What is the effect of external mass transfer on bioreaction rate?9.6 Immobilized-enzyme reaction kineticsInvertase catalyzes the reaction:C12H22O11 + H2O → C6H12O6 + C6H12O6sucrose glucose fructoseInvertase from Aspergillus oryzae is immobilized in porous resin particles of diameter 1.6 mm at a density of 0.1 μmol enzyme g-1. The effective diffusivity of sucrose in the resin is 1.3 ⨯ 10-11 m2 s-1. The resin is placed in a spinning-basket reactor operated so that external mass-transfer effects are eliminated. At a sucrose concentration of 0.85 kg m-3, the observed rate of conversion is 1.25 ⨯ 10-3 kg m-3 (resin) s-1. K m for the immobilized enzyme is 3.5 kg m-3.(a)Calculate the effectiveness factor.(b)Determine the true first order reaction constant for immobilized enzyme.(c)Assume that specific enzyme activity is not affected by steric hindranceor conformational changes as enzyme loading increases. This means that k1 should be directly proportional to enzyme concentration in the resin.Plot changes in effectiveness factor and reaction rate as a function of enzyme loading from 0.01 μmol g-1 to 2.0 μmol g-1. Comment on the relative benefit of increasing the concentration of enzyme within the resin.9.7 Mass-transfer effects in plant cell cultureSuspended Catharanthus roses cells form spherical clumps approximately 1.5 mm in diameter. Oxygen uptake is measured using the apparatus of Figure 9.13. Medium is recirculated with a superficial liquid velocity of 0.83 cm s-1. At a bulk concentration of 8 mg l-1, oxygen is consumed at a rate of 0.28 mg g-1 (wet weight cells) h-1. Assume that density and viscosity of the medium are similar to water, the specific gravity of wet cells is 1, and oxygen uptake is zero order. The effective diffusivity of oxygen in the clumps is 9 ⨯ 10-6 cm2 s-1, or half that in the medium.(a)Does external mass transfer affect the oxygen uptake rate?(b)To what extent does internal mass transfer affect oxygen uptake?(c)Roughly, what would you expect the profile of oxygen concentration tobe within the aggragates?9.8 Respiration in mycelial pelletsAspergillus niger cells are observed to form aggregates of average diameter 5 mm. The effective diffusivity of oxygen in the aggregates is 1.75 ⨯ 10-9 m2 s-1. In a fixed-bed bioreactor, the oxygen consumption rate at a bulk oxygen concentration of 8 ⨯ 10-3 kg m-3 is 8.7 ⨯ 10-5 kg m-3 (biomass) s-1. The liquid-solid mass-transfer coefficient is 3.8 ⨯ 10-5 m s-1.(a)Is oxygen uptake affected by external mass transfer?(b)What is the external effectiveness factor?(c)What reaction rate would be observed if both internal and externalmass-transfer resistances were eliminated?(d)If only external mass-transfer effects were removed, what would be thereaction rate?。