Bioprocess Engineering : Kinetics, Sustainability, and Reactor Design.

Format:

Book

Author/Creator:

Liu, Shijie.

Language:

English

Subjects (All):

Biochemical engineering.

Physical Description:

1 online resource

Edition:

3rd ed.

Place of Publication:

Chantilly : Elsevier, 2020.

Summary:

Bioprocess Engineering: Kinetics, Sustainability, and Reactor Design, Third Edition, is a systematic and comprehensive textbook on bioprocess kinetics, molecular transformation, bioprocess systems, sustainability and reaction engineering.

Contents:

Cover

Title

Copyright

Contents

Chapter 1 - What is bioprocess engineering?

1.1 - Biological cycle

1.2 - Bioprocess engineering applications

1.3 - Scales: living organism and manufacturing

1.4 - Green chemistry

1.5 - Sustainability

1.6 - Biorefinery

1.7 - Biotechnology and bioprocess engineering

1.8 - Mathematics, biology, and engineering

1.9 - The story of penicillin: the dawn of bioprocess engineering

1.10 - Bioprocesses: regulatory constraints

1.11 - The pillars of bioprocess kinetics and systems engineering

1.12 - Summary

Problems

References

D. History of Penicillin

Further readings

A. Green Chemistry

B. Sustainability

C. Biorefinery

E. Regulatory Issues

Chapter 2 - An overview of biological basics

Chapter outline

2.1 - Cells and organisms

2.1.1 - Microbial diversity

2.1.2 - How cells are named

2.1.3 - Prokaryotes

2.1.3.1 - Eubacteria

2.1.3.2 - Archaebacteria

2.1.4 - Eukaryotes

2.2 - Viruses

2.3 - Prions

2.4 - Stem cell

2.5 - Cell chemistry

2.5.1 - Amino acids and proteins

2.5.2 - Monosaccharides

2.5.2.1 - Aldoses

2.5.2.1.1 - D-hexoses

2.5.2.1.2 - Pentoses

2.5.2.1.3 - D-tetroses

2.5.2.1.4 - D-trioses

2.5.2.2 - Ketoses

2.5.2.2.1 - Ketohexoses

2.5.2.2.2 - Ketopentoses

2.5.2.2.3 - Ketotetroses

2.5.2.2.4 - Ketotriose

2.5.2.3 - Deoxysugars

2.5.3 - Disaccharides

2.5.4 - Polysaccharides

2.5.4.1 - Starch

2.5.4.2 - Glycogen

Fructan

2.5.4.4 - Cellulose

2.5.4.5 - Hemicelluloses

2.5.5 - Phytic acid and inositol

2.5.6 - Chitin and chitosan

2.5.7 - Lignin

2.5.8 - Lipids, fats, and steroids

2.5.9 - Nucleic acids, RNA, and DNA

2.6 - Cell feed

2.6.1 - Macronutrients

2.6.2 - Micronutrients

2.6.3 - Growth media.

2.7 - Non earthly/unnatural biological agents

2.8 - Summary

Chapter 3 - An overview of chemical reaction analysis

3.1 - Chemical species

3.2 - Chemical reactions

3.3 - Reaction rates

3.3.1 - Definition of the rate of reaction, rA

3.3.2 - Rate of a single irreversible reaction

3.3.3 - Rate of an elementary reaction

3.3.4 - Rate of a reversible reaction

3.3.5 - Rates of multiple reactions

3.3.6 - Rate coefficients

3.4 - Approximate reactions

3.5 - Stoichiometry

3.6 - Yield and yield factor

3.7 - Reaction rates near equilibrium

3.8 - Energy regularity

3.9 - Classification of multiple reactions and selectivity

3.10 - Coupled reactions

3.11 - Reactor mass balances

3.12 - Reaction energy balances

3.13 - Reactor momentum balance

3.14 - Ideal reactors

3.15 - Bioprocess systems optimization

3.16 - Summary

Chapter 4 - Batch reactor

4.1 - Isothermal batch reactors

4.2 - Batch reactor sizing

4.3 - Nonisothermal batch reactors

4.4 - Numerical solutions of batch reactor problems

4.5 - The reactor pinch graph

4.6 - Summary

Chapter 5 - Ideal flow reactors

5.1 - Commonly useful parameters

5.2 - Plug flow reactor (PFR)

5.3 - Continuous stirred tank reactor (CSTR) and chemostat

5.4 - Multiple reactors

5.5 - Recycle reactors

5.6 - PFR with distributed feeding and withdrawing

5.6.1 - Distributed feed

5.6.2 - Membrane reactor

5.7 - Reactive distillation

5.8 - PFR or CSTR?

5.9 - Steady nonisothermal flow reactors

5.10 - Reactive extraction

5.11 - Graphic solutions using batch concentration data

5.11.1 - Solution of A PFR using batch concentration data

5.11.2 - Solution of A CSTR using batch concentration data.

5.12 - Summary

Chapter 6 - Kinetic theory and reaction kinetics

6.1 - Elementary kinetic theory

6.1.1 - Distribution laws

6.1.2 - Collision rate

6.2 - Collision theory of reaction rates

6.3 - Reaction rate analysis/approximation

6.3.1 - Fast equilibrium step (FES) approximation

6.3.2 - Pseudosteady state hypothesis (PSSH)

6.4 - Unimolecular reactions

6.5 - Free radicals

6.6 - Kinetics of acid hydrolysis

6.7 - Parametric estimation

6.8 - Summary

Chapter 7 - Enzymes

7.1 - How enzymes work?

7.2 - Simple enzyme kinetics

7.2.1 - The fast equilibrium step (FES) assumption

7.2.2 - The pseudosteady-state hypothesis (PSSH)

7.2.3 - Specific activity

7.3 - Competitive and allosteric enzyme kinetics

7.3.1 - Reversible reactions

7.3.2 - Competitive reactions

7.3.3 - Reactions with nbound substrates

7.3.4 - Enzyme-substituted reactions-the ping-pong mechanism

7.3.5 - Bimolecular reactions on allosteric enzymes

7.4 - Enzyme inhibition

7.4.1 - Allosteric inhibition

7.4.1.1 - Noncompetitive inhibition: β = 0 and αS = 1

7.4.1.2 - Uncompetitive inhibition: β = 0 and KI → ∞ while αS/KI is finite

7.4.2 - Competitive inhibition

7.5 - Higher order substrate kinetics

7.6 - pH effects

7.7 - Temperature effects

7.8 - Insoluble substrates and/or high-enzyme loading

7.9 - Immobilized enzyme systems

7.9.1 - Methods of immobilization

7.9.1.1 - Entrapment

7.9.1.2 - Surface immobilization

7.9.2 - Electrostatic and steric effects in immobilized enzyme systems

7.10 - Analysis of bioprocess with enzymatic reactions

7.11 - Large-scale production of enzymes

7.12 - Medical and industrial utilization of enzymes.

7.13 - Kinetic approximation: why Michaelis-Menten equation works

7.13.1 - Pseudosteady state hypothesis (PSSH)

7.13.2 - Fast equilibrium step (FES) approximation

7.13.3 - Modified-fast equilibrium approximation

7.14 - Summary

Chapter 8 - Chemical reactions on solid surfaces

8.1 - Catalysis

8.2 - How does reaction with solid occur?

8.3 - Langmuir: theoretical basis of adsorption kinetics

8.4 - Idealization of nonideal surfaces

8.4.1 - UniLan adsorption isotherm

8.4.2 - Common empirical approximate isotherms

8.5 - Cooperative adsorption

8.5.1 - Cooperative adsorption of single species

8.5.2 - Competitive cooperative adsorption

8.5.3 - Pore size and surface characterization

8.6 - LHHW: surface reactions with rate-controlling steps

8.7 - Why rate approximation such as LHHW works?

8.8 - Chemical reactions on nonideal surfaces based on the distribution of interaction energy

8.9 - Cooperative catalysis

8.9.1 - Unimolecular reactions

8.9.2 - Bimolecular reactions

8.10 - Kinetics of reactions on surfaces where the solid is either a product or reactant

8.11 - Decline of surface activity: catalyst deactivation

8.12 - Summary

Chapter 9 - Protein-ligand interactions

9.1 - Multifunctionalization of proteins

9.2 - Covalently bound oligomers

9.3 - Noncovalent assembly of protein

9.4 - Protein assembly via domain swapping

9.5 - Coexistence of protein oligomer mixtures

9.6 - Three simplistic models of enzyme interactions

9.6.1 - The MWC model

9.6.2 - The KNF model

9.6.3 - The morpheein model

9.7 - Protein-ligand interactions

9.8 - Single ligand species versus enzymes with two identical sites

9.9 - Single-ligand species on a homosteric enzyme.

9.10 - Sequential single ligand species on allosteric enzymes

9.11 - Single-ligand species on random-access allosteric enzymes

9.12 - Multiple different ligand-specific active centers

9.12.1 - Simple allosteric enzyme

9.12.2 - Dimers with parallel allosteric sites

9.12.3 - Parallel interaction

9.12.4 - Uniallosteric interaction

9.13 - Competitive multiligand interactions on homosteric enzymes

9.13.1 - Two-site homosteric enzyme

9.13.2 - n-site homosteric enzyme

9.14 - Summary

Chapter 10 - Molecular regulation

10.1 - Single substrate reactions

10.1.1 - Catalysis of a homosteric enzyme

10.1.2 - Catalysis of an allosteric enzyme

10.2 - "Unimolecular" reactions

10.2.1 - Homosteric dimeric enzyme

10.2.2 - Homosteric enzymes

10.3 - Bimolecular reactions

10.3.1 - Multisited enzymes

10.3.2 - Enzyme substitution

10.4 - The simplest polymorph: a bimorph of two monomeric forms of the same enzyme

10.4.1 - An indifferent bimorph or morpheein

10.4.2 - A ligand-stabilized bimorph

10.4.3 - A lignd-induced bimorph

10.4.4 - A simplistic kinetic polymorph

10.5 - Kinetics of polymorphic catalysis

10.5.1 - Substrate-induced polymorph

10.5.1.1 - A bimorph of two n-oligo enzymes

10.5.2 - Substrate-stabilized polymorph

10.5.2.1 - Substrate-stabilized interconvertible polymorph with noninteractive sites

10.5.3 - Substrate-indifferent polymorph

10.5.3.1 - Substrate-indifferent interconvertible biprotomer polymorph with noninteractive sites

10.5.3.2 - An example of polymorph

10.6 - Multimolecular reactions on enzymes with ligand-specific active centers

10.6.1 - Simplistic allosteric enzyme

10.6.2 - Dimers with parallel allosteric sites

10.6.3 - Catalysis on allosteric enzyme with n-pairs of parallel sites.

10.7 - Parallel allosteric competitive interactions.

Notes:

Description based on publisher supplied metadata and other sources.

ISBN:

0-12-821012-5

OCLC:

1149141596