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- Herausgeber: John Wiley & Sons
- Kategorie: Fachliteratur
- Serie: Enzyme Reaction Engineering
- Sprache: Englisch
Comprehensively introduces readers to modelling of rate of enzymatic reactions, including effects of physicochemical parameters Analysis of Enzyme Reaction Kinetics is the second set in a unique eleven-volume collection on Enzyme Reactor Engineering. It describes rate expressions pertaining to enzymatic reactions, including modulation by physicochemical factors, as well as tools for prediction and control of how fast substrates are transformed to products. Volume 1 details rate expressions mathematically derived from mechanistic postulates, and is complemented by appropriate statistical approaches to fit them to experimental data. Volume 2 discusses the effects of physical and chemical parameters upon the rates of both enzyme-catalyzed and enzyme-deactivation reactions. Starting with basic concepts and historical perspectives, the first volume introduces readers to the mathematics of rate expressions. It then goes on to cover kinetic features and the many forms of Michaelis & Menten's-type rate expressions (single and multiple enzymes, autocatalysis, single and multiple substrates, multiphasic systems, etc.), and concludes with the statistical analysis of rate expressions - including the assessment of data, fitting of models to data, and generation of data themselves. The second volume introduces readers to physicochemical modulation of reaction rate - starting with basic concepts, and looking specifically at temperature-, mechanical force-, pH- and compound-driven effects: both unimodal and bimodal deactivation are considered. Analysis of Enzyme Reaction Kinetics 2V Set is a comprehensive work for those studying or working with enzyme reactions, or practitioners involved in the control of reactors. SERIES INFORMATION Enzyme Reactor Engineering is organized into four major sets: Enzyme Reaction Kinetics and Reactor Performance; Analysis of Enzyme Reaction Kinetics; Analysis of Enzyme Reactor Performance; and Mathematics for Enzyme Reaction Kinetics and Reaction Performance.
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Seitenzahl: 1969
Veröffentlichungsjahr: 2023
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Table of Contents
Cover
Series Page
Title Page
Copyright Page
Dedication
About the Author
Series Preface
Preface
Volume 1
Part 1: Mathematical Approach to Rate Expressions
1 Introduction
1.1 Basic Concepts
1.2 Chemical Mechanism and Rate Expression
1.3 Historical Perspective
1.4 Further Refinements
1.5 Multisubstrate Approaches
1.6 Objective
1.7 Strategy
2 Rate Expression
2.1 Kinetic Features
2.2 Order of Reaction
3 Michaelis and Menten's Rate Expression with Single Enzyme
3.1 Michaelis and Menten's Rationale
3.2 Graphical Interpretation
3.3 Semilogarithmic Plot
3.4 Eisenthal and Cornish‐Bowden's Plot
3.5 Dixon's Plot
3.6 Concentration of Enzyme Forms
3.7 Best Reparameterization
3.8 van Slyke and Cullen's Rationale
3.9 Briggs and Haldane's Rationale
3.10 Absolute Sensitivity to Lumped Parameters
3.11 Relative Error of Alternative Derivations
3.12 Relative Sensitivity to Intrinsic Parameters
3.13 Biochemical Rationale
3.14 Derivatives of Rate Expression
4 Michaelis and Menten's Rate Expression with Multiple Enzymes
4.1 Several Isozymes
4.2 Two Isozymes
4.3 Infinite Isozymes
5 Michaelis and Menten's Rate Expression with Autocatalysis
6 Michaelis and Menten's Rate Expression with Multiphasic Systems
7 Improved Rate Expression with Single Enzyme
7.1 Morrison's Rationale
7.2 Graphical Interpretation
7.3 Low Enzyme Concentration
7.4 Best Reparameterization
7.5 Kim's Rationale
7.6 Graphical Interpretation
7.7 Specific Kinetic Features
7.8 Absolute Sensitivity to Intrinsic Parameters
7.9 Improved Simulation of Initial Transient
7.10 Improved Simulation of Final Transient
8 Alternative Forms of Michaelis and Menten's Rate Expression
8.1 Integrated Form
8.2 Linearized Form
9 Rate Expressions for Multisubstrate Reactions
9.1 Shortcut Approaches to Pseudo Steady-State
9.2
Uni Uni
Mechanism
9.3 Ordered
Bi Uni
Mechanism
9.4 Other
Bi
Uni
and
Bi Bi
Mechanisms
9.5 Simplification of Multisubstrate Rate Expressions
Part 2: Statistical Approach to Rate Expressions
10 Introduction
10.1 Basic Concepts
10.2 Objective
10.3 Strategy
11 Assessment of Data and Models
11.1 Independence Checks
11.2 Normality Checks
11.3 Homoskedasticity Checks
11.4 Linearity Checks
11.5 Relationship Checks
11.6 Adequacy Checks
11.7 Sufficiency Checks
12 Fitting of Models to Data
12.1 Linear Regression Analysis
12.2 Improved Regression Analysis
12.3 Nonlinear Regression Analysis
13 Generation of Data
13.1 Empirical Designs
13.2 Mechanistic Designs
Further Reading
Series Page
Title Page
Copyright Page
Dedication Page
About the Author
Series Preface
Preface
Volume 2
Part 3: Physical Modulation of Reaction Rate
14 Introduction
14.1 Basic Concepts
14.2 Thermodynamic Approach
14.3 Kinetic Approach
14.4 Physical Deactivation of Enzymes
14.5 Objective
14.6 Strategy
15 Unimodal Deactivation
15.1 Simple Reversible Deactivation
15.2 Simple Irreversible Deactivation
15.3 General Deactivation
16 Bimodal Deactivation
16.1 Simple Reversible Deactivation
16.2 Simple Irreversible Deactivation
17 Effects upon Nonelementary Reactions
18 Temperature‐Driven Modulation
18.1 Thermodynamic Formulation of Temperature-Dependence of Elementary Steps
18.2 Kinetic Formulation of Temperature-Dependence of Elementary Steps
18.3 Improvement of Parameter Fitting
19 Mechanical Force‐Driven Modulation
19.1 Normal Elastic Forces
19.2 Tangential Elastic Forces
19.3 Tangential Plastic Forces
20 Response of Enzyme Deactivation
21 Response of Enzymatic Reaction
Part 4: Chemical Modulation of Reaction Rate
22 Introduction
22.1 Basic Concepts
22.2 Thermodynamic Approach
22.3 Kinetic Approach
22.4 Chemical Deactivation
22.5 Chemical Modulation
22.6 Objective
22.7 Strategy
23
pH
‐Driven Modulation
23.1 Protolysis of Enzyme Only
23.2 Protolysis of Enzyme and Substrate
24 Ionic Strength‐Driven Modulation
25
pH
‐Driven Deactivation
25.1 Reversible Decay
25.2 Irreversible Decay
26 Self‐Deactivation
27 Microbial Deactivation
28 Heterologous Bimodal Deactivation
28.1 Reversible Deactivation
28.2 Irreversible Deactivation
29 Heterologous Unimodal Deactivation
29.1 Reversible Deactivation
29.2 Irreversible Deactivation
30 Mechanism Discrimination
30.1 Sequential Random
Bi Bi
30.2 Sequential Ordered
Bi Bi
30.3 Ping Pong
Bi Bi
30.4 Graphical Comparison
31 Homologous Modulation
31.1 Independent Sites
31.2 Sequential Transition
31.3 Concerted Transition
31.4 Asymptotic Patterns
Further Reading
Index
End User License Agreement
List of Tables
Chapter 2
Table 2.1 Values of intrinsic kinetic constants,
k
1
,
k
−1
, and
k
2
, of M...
Table 2.2 Values of intrinsic kinetic constant,
k
2
, and lumped kinetic const...
Chapter 6
Table 6.1 Examples of common enzymes acting in soluble form upon substrates ...
Chapter 8
Table 8.1 Numerical values of
b
i,j
coefficients (
i =
2, 3
, …,
8;...
Chapter 9
Table 9.1 Description of
Bi Uni
and
Bi Bi
enzymatic reactions, in terms of s...
Chapter 10
Table 10.1 List of original or sample data,
y
i,j
(
i =
1, 2, …,
N
;
j
= ...
Table 10.2 List of original, or sample data, as predictor,
x
i
(
i =
1, ...
Chapter 11
Table 11.1 Critical (unilateral) values,
V
crt
, of
V
statistic, for samples o...
Table 11.2 Critical (unilateral) values,
D
crt
, of Kolmogorov and Smirnov's
D
Table 11.3 Critical (unilateral) values,
B
crt
, of Bartlett's
B
statistic, fo...
Table 11.4 Critical (bilateral) values,
R
P,crt
, of absolute Pearson's
R
P
sta...
Table 11.5 Critical (bilateral) values,
R
S,crt
, of Spearman's
R
S
statistic, ...
Table 11.6 Critical (unilateral) values,
L
crt
, of Fisher's
L
statistic, for
Table 11.7 Critical (unilateral) values,
S
crt
, of Fisher's
S
statistic, for ...
Chapter 12
Table 12.1 Results of linearization of rate expression,
r
, describing enzyma...
Table 12.2 Results of linearization of rate expression,
r
, describing enzyma...
Table 12.3 Results of linearization of rate expression,
r
, describing enzyma...
Table 12.4 Results of linearization of rate expression,
r
, describing enzyma...
Table 12.5 Results of linearization of rate expression,
r
S
, describing enzym...
Table 12.6 Results of linearization of rate expression,
r
E
, describing enzym...
Table 12.7 Combination of linear models encompassing rate of enzymatic react...
Table 12.8 Results of linearization of rate expression,
r
, describing enzym...
Table 12.9 Functional form of first
a
i,j
terms, required for numerical calcu...
Table 12.10 Functional form of first
b
i,j
terms, required for numerical cal...
Table 12.11 Functional form of first
c
i,j
terms, required for numerical calc...
Chapter 13
Table 13.1 Layout of clumping empirical designs – with indication of suggest...
Table 13.2 Values of (second row) and (first row) leading to maximum val...
Table 13.3 Values of (first row), (second row), and (third row) leadin...
Chapter 14
Table 14.1 Ratio of local variation of concentration of reference reactant n...
Table 14.2 Molar enthalpy change,
Δh
act,dnt
, entropy change,
Δs
act
...
Chapter 18
Table 18.1 Theoretical estimates for frequency of productive collisions,
ζ
...
Chapter 19
Table 19.1 Variation of negative of normalized molar Gibbs' energy, −
g
/
RT
, a...
Table 19.2 Classification of surfactant agents according to
HLB
, using Griff...
Table 19.3 Group contribution,
H
i
, for calculation of
HLB
, using Davies' sca...
Chapter 22
Table 22.1 Typical (aqueous) buffers used in enzymatic systems – with indica...
Table 22.2 Dependence of enthalpy change,
Δh
θ
cdnt
, and entropy cha...
Table 22.3 Typical Hofmeister's series of anions and cations, pertaining to ...
Table 22.4 Values of inhibition equilibrium constants,
K
i
, for selected enzy...
Table 22.5 Selected enzymes and corresponding natural substrates – with exam...
Table 22.6 Selected coenzymes required for enzyme action – with examples of ...
Table 22.7 Selected compounds acting as chemical inhibitors of enzymes – wit...
Table 22.8 Optimum
pH
values for activity,
pH
opt
, of selected enzymes – with...
Table 22.9 Values of
pK
a
associated with prototropic groups of amino acids, ...
Chapter 24
Table 24.1 Estimated Debye's radius,
R
j
, of selected ions in aqueous reactio...
Chapter 30
Table 30.1 Graphical descriptors of linearized plots describing enzymatic ra...
Chapter 31
Table 31.1 Possibilities of interconversion between enzyme forms
E
,
ES
,
ES
2
,...
Table 31.2 Possibilities of interconversion between enzyme forms
E
and
ES
,
E
...
Table 31.3 Generalized models for three-sited allosteric enzyme involving hy...
List of Illustrations
Chapter 2
Figure 2.1 Chemical equation describing a physicochemical event involving re...
Figure 2.2 Variation of (a) yield of adsorbed (or intermediate) substrate,
C
Figure 2.3 Evolution in time,
t
, of rate associated with conversion of
E
and...
Figure 2.4 Evolution in time,
t
, of ratio of rate of forward reaction,
r
1
, t...
Figure 2.5 Variation of (a) apparent order of reaction,
m
app
, and (b) averag...
Chapter 3
Figure 3.1 Chemical equation describing transformation of reactant
S
to prod...
Figure 3.2 Molecular mechanism – via Michaelis and Menten's approach, associ...
Figure 3.3 Reaction progress curve (evolving in the direction indicated by a...
Figure 3.4 Variation of (a) rate of reaction,
r
{
C
S
} (), and (b) its recipr...
Figure 3.5 Variation of (a) reciprocal rate of reaction, 1/
r
{
C
S
}, subtracted...
Figure 3.6 Variation of rate of reaction,
r
{
C
S
}, as a function of concentrat...
Figure 3.7 Variation of rate of reaction,
r
{
C
S
} (), as a function of concen...
Figure 3.8 Variation of rate of reaction,
r
{
C
S
} (), as a function of concen...
Figure 3.9 Variation of (a) normalized concentrations of free enzyme, , and...
Figure 3.10 Variation of normalized rate of reaction,
r
#
, as a function of d...
Figure 3.11 Molecular mechanism – via van Slyke and Cullen's approach, assoc...
Figure 3.12 Molecular mechanism – via Briggs and Haldane's approach, associa...
Figure 3.13 Reaction progress curves in terms of concentrations of enzyme,
C
Figure 3.14 Variation of ratio of rate of reaction obtained with
K
m
calculat...
Figure 3.15 Variation of normalized rate,
r
**
, and normalized derivative the...
Figure 3.16 Variation of (a) partial objective function explicit on activity...
Chapter 4
Figure 4.1 Molecular mechanism – via Briggs and Haldane's approach, associat...
Figure 4.2 Variation of overall rate of reaction,
r
, as a function of concen...
Figure 4.3 Variation of ratio of overall rate of reaction,
r
, to substrate c...
Figure 4.4 Variation of ratio of (a) overall rate of reaction,
r
, or (b, d) ...
Figure 4.5 Variation of normalized rate of reaction,
r
#
, as a function o...
Figure 4.6 Postulated distribution of (a) enzyme population,
d
(
C
E
/
C
E,tot
)/
dk
Chapter 5
Figure 5.1 Description of autocatalytic transformation of reactant
S
, cataly...
Figure 5.2 Variation of (a) concentration of free enzyme,
C
E
, and (b) rate o...
Chapter 6
Figure 6.1 Chemical equation describing transformation of reactant
S
Im
contr...
Figure 6.2 Molecular mechanism – via Michaelis and Menten's approach, associ...
Figure 6.3 Molecular mechanism associated with physical adsorption of reacta...
Figure 6.4 Variation of lumped kinetic parameters (), (a)
v
max,I
and (b)
Km
...
Figure 6.5 Variation of bulk rate of reaction,
r
(), as a function of (a, d...
Chapter 7
Figure 7.1 Reaction progress curve (evolving in the direction indicated by a...
Figure 7.2 Variation of (a) rate of,
r
{
C
S,tot
} (), and (b) its reciprocal,...
Figure 7.3 Reaction progress curves, in terms of concentrations of enzyme,
C
Figure 7.4 Variation of (a) rate of reaction,
r
{
C
S,tot
}, as a function of...
Figure 7.5 Variation of (a) dimensionless concentration of free substrate,
Figure 7.6 Reaction progress curves in terms of (a, b) actual concentrations...
Figure 7.7 Reaction progress curves in terms of
C
E
C
S
/
C
ES
(), with...
Figure 7.8 Reaction progress curves in dimensionless variables, during the i...
Figure 7.9 Reaction progress curves, in terms of normalized concentration of...
Figure 7.10 (a) Reaction progress curve, in terms of concentration of substr...
Figure 7.11 Evolution of
ϕ
S
{
t
*
,} as a function of dimensionless ...
Figure 7.12 Diagram of stopped‐flow setup, including two syringes – one cont...
Figure 7.13 (a) Reaction progress curve in terms of concentration of substra...
Figure 7.14 Reaction progress curve in terms of concentration of substrate,
Figure 7.15 Diagram of one-way, stopped‐flow setup, including three syringes...
Figure 7.16 Evolution of as a function of dimensionless deviation time, ,...
Figure 7.17 Reaction progress curve () in terms of (a) concentration of rea...
Figure 7.18 Variation of 1 − (), where denotes normalized concentration...
Chapter 8
Figure 8.1 Reaction progress curves in terms of normalized concentration of ...
Figure 8.2 Reaction progress curves, in terms of (a) argument of Lambert's f...
Figure 8.3 Reaction progress curves, in terms of normalized concentration of...
Figure 8.4 Typical variation of (a)
r
as a function of
r
/
C
S
and (b)
r
/
C
S
as ...
Figure 8.5 Typical variation of (a)
C
S
as a function of
C
S
/
r
and (b)
C
S
/
r
as...
Figure 8.6 Typical variation of (a) 1/
C
S
as a function of 1/
r
and (b) 1/
r
as...
Figure 8.7 Typical variation of (a) (
C
S,
0
−
C
S
)/
t
as a function of (ln
C
S
,0
/
Figure 8.8 Typical variation of (a)
t
/(
C
S,
0
−
C
S
) as a function of (ln
CS,0/
...
Figure 8.9 Typical variation of (a)
t
/ln
C
S,
0
/
C
S
as a function of (
C
S,
0
−
C
S
Chapter 9
Figure 9.1 Description of a putative enzymatic reaction as a set of three co...
Figure 9.2 Molecular mechanism describing a putative enzymatic reaction, inv...
Figure 9.3 Listing of (a) all distinct patterns containing three sides (and ...
Figure 9.4 Listing of (a) all distinct closed loop‐free patterns containing ...
Figure 9.5 Condensation of sum of (a) distinct patterns corresponding to who...
Figure 9.6 Description of general (reversible) enzyme‐catalyzed reaction via...
Figure 9.7 Molecular mechanism describing a putative enzymatic reaction foll...
Figure 9.8 Molecular mechanism describing a putative enzymatic reaction foll...
Figure 9.9 Cleland's representation of molecular mechanism describing a puta...
Figure 9.10 Description of an enzymatic reaction following the
Uni
Uni
molec...
Figure 9.11 Description of an enzymatic reaction following the
Uni Uni
molec...
Figure 9.12 Listing of (a) patterns containing one side from a total of one ...
Figure 9.13 Description of an enzymatic reaction following the
Uni Uni
molec...
Figure 9.14 Description of an enzymatic reaction following the
Uni Uni
molec...
Figure 9.15 Listing of (a) pattern containing one side from a total of one s...
Figure 9.16 Description of an enzymatic reaction following the
Bi Uni
molecu...
Figure 9.17 Description of an enzymatic reaction following the
Bi Uni
molecu...
Figure 9.18 Listing of (a) all distinct patterns containing two sides from a...
Figure 9.19 Description of an enzymatic reaction following the
Bi Uni
molecu...
Figure 9.20 Variation of (a) modified concentration of product
P
, , and (b)...
Chapter 10
Figure 10.1 Experimental data used for fitting of (differential) rate expres...
Figure 10.2 Experimental data used for fitting of (differential) rate expres...
Figure 10.3 Schematic representation of (a) replicated original data,
y
i,j
(...
Figure 10.4 General flowchart pertaining to statistical assessment of data: ...
Figure 10.5 General flowchart pertaining to statistical assessment of model:...
Chapter 11
Figure 11.1 Experimental data (○) plotted (a) on an ordinal basis as origina...
Figure 11.2 Experimental residuals (○), , of dependent variable plotted ver...
Figure 11.3 Averages of experimental dependent variable, , plotted versus (
Chapter 12
Figure 12.1 Schematic representation, for the
i
th experimental point (○), of...
Figure 12.2 Experimental data encompassing (a) replicates,
y
i
(○), and (b) m...
Figure 12.3 Schematic representation of predicted values of dependent variab...
Figure 12.4 Schematic representation of (a) elliptical confidence region and...
Figure 12.5 Schematic representation of (a) confidence interval () and (b) ...
Figure 12.6 Schematic representation of (a, b) normal probability density fu...
Figure 12.7 Experimental data pertaining to variation of rate,
r
, versus sub...
Figure 12.8 Transformed experimental data pertaining to substrate concentrat...
Figure 12.9 Schematic representation of (a) pseudo elliptical confidence reg...
Figure 12.10 Schematic representation of (a) confidence interval () and (b)...
Chapter 13
Figure 13.1 Schematic representation of kinetic data pertaining to reaction ...
Chapter 14
Figure 14.1 Typical variation, as a function of absolute temperature,
T
, of ...
Figure 14.2 Variation of ratio of derivative of equilibrium concentration of...
Figure 14.3 Typical variation of ln
K
eq
as a function (a) reciprocal tempera...
Figure 14.4 Typical variation of overall molar enthalpy change, , entropy c...
Figure 14.5 Chemical (and mechanistic) equations describing (a) irreversible...
Chapter 15
Figure 15.1 Michaelis and Menten's mechanism involving two isozymes,
E
1,1
an...
Figure 15.2 Typical variation of rate of reaction () catalyzed by two isozy...
Figure 15.3 Michaelis and Menten's mechanism involving two isozymes,
E
1,1
an...
Figure 15.4 General first-order enzyme deactivation mechanism involving
MN
i...
Figure 15.5 First‐order enzyme deactivation mechanism involving
N
isozymes,
Figure 15.6 Variation of (a, b) fractional concentration of each,
i
, of
N
is...
Figure 15.7 First‐order deactivation mechanism involving
M
isozymes,
E
1,1
,
E
Figure 15.8 Variation of (a, b) fractional concentration of each,
j
, of
M
is...
Figure 15.9 Variation of (a, b) fractional concentration of each,
j
, of
M
is...
Figure 15.10 Variation of (a, b) fractional concentration of each,
j
, of
M
i...
Figure 15.11 Variation of apparent order of decay,
m
app
, of
M
isozymes, for ...
Figure 15.12 First-order enzyme deactivation mechanism involving
N
isozymes,...
Figure 15.13 Variation of fractional concentration of each,
i
, of 2
N
isozyme...
Figure 15.14 Variation of correction factor,
Φ
rev,irr,
2,
N
, for rate of ...
Figure 15.15 First‐order enzyme deactivation mechanism involving
M
isozymes,...
Figure 15.16 Variation of fractional concentration of each,
j
, of 2
M
isozyme...
Figure 15.17 Variation of correction factor,
Φ
rev,irr,M,
2
, for rate of ...
Chapter 16
Figure 16.1 Michaelis and Menten's mechanism involving two isoenzymes,
E
1,1
...
Figure 16.2 Variation of fractional concentration of each of two isozymes, i...
Figure 16.3 Variation of correction factor,
Φ
rev,
1,2
, for rate of react...
Figure 16.4 Michaelis and Menten's mechanism involving two isozymes,
E
1,1
an...
Figure 16.5 Variation of fractional concentration of each of two isozymes, i...
Figure 16.6 Variation of correction factor,
Φ
irr,
2,1
, for rate of react...
Chapter 18
Figure 18.1 Variation of enthalpy between reactant,
S
, and product,
Q
, along...
Figure 18.2 Variation of logarithm of reaction rate,
r
, following Michaelis ...
Figure 18.3 Schematic representation of (a) cylindrical volume,
V
S,swp
, swep...
Figure 18.4 Schematic representation of single molecule (○) of mass
m
, (a) m...
Figure 18.5 Variation of (a, b) overall probability density function, 4
πv
...
Figure 18.6 Profile of Gibbs' potential energy along a hypothetical reaction...
Chapter 19
Figure 19.1 Variation of volume between reactant
S
and product
Q
, along an e...
Figure 19.2 Path followed by generic state variable between reactant
S
and p...
Figure 19.3 (a) Typical variation of surface tension,
σ
, of mixture con...
Figure 19.4 Variation of (a) fractional adsorption at interface, as ratio of...
Figure 19.5 Variation of concentration of active enzyme,
C
E,a
, at temperatur...
Figure 19.6 Variation of average value, , of product of shear rate,
γ
,...
Figure 19.7 Variation of concentration of active enzyme,
C
E,a
, at temperatur...
Chapter 20
Figure 20.1 Typical variation of normalized molar concentration of active en...
Chapter 22
Figure 22.1 Typical variation of (a) partial derivative with regard to (buff...
Figure 22.2 Variation of
pH
as a function of (a) concentration of buffer,
C
b
...
Figure 22.3 Variation of buffering capacity,
β
, as a function of
pH
(a)...
Figure 22.4 Mechanistic equation describing elementary reaction in forward d...
Figure 22.5 Mechanistic equation describing elementary reaction in reverse d...
Figure 22.6 Predicted structural changes of chymotrypsin inhibitor 2 by (i) ...
Figure 22.7 Variation of equilibrium fraction () of chemically denatured en...
Figure 22.8 Formation of gel by lysozyme in aqueous solution at 95
°
C, ...
Figure 22.9 Stoichiometric equation describing solubilization of pure protei...
Figure 22.10 Typical variation of solubility of protein in solution, , as a...
Figure 22.11 Variation, as a function of
pH
, of normalized stability of enzy...
Figure 22.12 Variation, as a function of absolute temperature,
T
, of median ...
Chapter 23
Figure 23.1 Michaelis and Menten's mechanism, involving three isozymes,
E
−
...
Figure 23.2 Variation, as a function of
p
H
, of
v
max,app
/
v
max
,1
() and
K
m,a
...
Figure 23.3 Dixon and Webb’s plot, as a function of
pH
, encompassing variati...
Figure 23.4 Variation, as a function of
pH
, of
v
max,app
() and ratio of con...
Figure 23.5 Michaelis and Menten’s mechanism, involving three isozymes,
E
−
...
Figure 23.6 Variation, as a function of
pH
, of
v
max,app
/
v
max
, for (a, d, g)
Figure 23.7 Dixon and Webb's plot encompassing variation of decimal logarith...
Chapter 24
Figure 24.1 Variation of activity coefficient,
γ
j
, of
j
th substrate bea...
Chapter 25
Figure 25.1 Second-order enzyme deactivation mechanism driven by
pH
, involvi...
Figure 25.2 Second-order enzyme deactivation mechanism driven by
pH
, involvi...
Figure 25.3 Variation, as a function of incubation
pH
, of (a) concentration ...
Figure 25.4 Second-order enzyme deactivation mechanism driven by
pH
, involvi...
Figure 25.5 Second-order enzyme deactivation mechanism driven by
pH
, involvi...
Figure 25.6 Variation, as a function of incubation
pH
, of (a) concentration ...
Chapter 26
Figure 26.1 Description of self-decaying reaction of enzyme, as (a) chemical...
Figure 26.2 Variation of (a) concentration of free enzyme,
C
E
, and (b) rate ...
Chapter 27
Figure 27.1 Description of apparent deactivation of enzyme via microbial rem...
Figure 27.2 Variation, as a function of processing time in stirred batch rea...
Chapter 28
Figure 28.1 Michaelis and Menten's mechanism involving enzyme
E
and substrat...
Figure 28.2 Variation of rate of enzymatic reaction,
r
(
‐‐‐‐‐‐‐‐‐
...
Figure 28.3 Variation of (a) ratio of apparent maximum rate of enzymatic rea...
Figure 28.4 Variation of (a) reciprocal of apparent maximum rate of enzymati...
Figure 28.5 Variation of reciprocal of rate of enzymatic reaction,
r
, as a f...
Figure 28.6 Variation of ratio of concentration of substrate,
C
S
, to rate of...
Figure 28.7 Variation of rate of enzymatic reaction,
r
, as a function of rat...
Figure 28.8 Variation of ratio of rate of enzymatic reaction,
r
, to concentr...
Figure 28.9 Variation of reciprocal of rate of enzymatic reaction,
r
, as a f...
Figure 28.10 Variation of ratio of concentration of substrate,
C
S
, to rate o...
Figure 28.11 Variation of function of rates of enzymatic reaction,
r
and
r
0
,...
Figure 28.12 Dixon's (a) original plot and (b) magnification of first portio...
Figure 28.13 Variation, as a function of substrate concentration,
C
S
, of ap...
Figure 28.14 (a) Michaelis and Menten's mechanism involving enzyme
E
and sub...
Figure 28.15 Variation of rate of enzymatic reaction,
r
(), characterized b...
Figure 28.16 Variation of (a) reciprocal of apparent maximum rate of enzymat...
Figure 28.17 Typical variation of (a) 1/
r
as a function of 1/
C
S
as per Linew...
Figure 28.18 Typical variation of (a) 1/
r
as a function of
C
I
as per Dixon’s...
Figure 28.19 (a) Michaelis and Menten's mechanism involving enzyme
E
and sub...
Figure 28.20 Variation of rate of enzymatic reaction,
r
(
‐‐‐‐‐‐‐‐‐
...
Figure 28.21 Variation of (a) reciprocal of apparent maximum rate of enzymat...
Figure 28.22 Typical variation of (a) 1/
r
as a function of 1/
C
S
as per Linew...
Figure 28.23 Typical variation of (a) 1/
r
as a function of
C
I
as per Dixon’s...
Figure 28.24 Michaelis and Menten's mechanism involving enzyme
E
and substra...
Figure 28.25 Reaction progress curve, as a function of dimensionless process...
Chapter 29
Figure 29.1 (a) Michaelis and Menten's mechanism involving enzyme
E
and subs...
Figure 29.2 Variation of rate of enzymatic reaction, reaction,
r
(), charac...
Figure 29.3 Variation of (a) reciprocal of apparent maximum rate of enzymati...
Figure 29.4 Typical variation of (a) 1/
r
as a function of 1/
C
S
as per Linewe...
Figure 29.5 Typical variation of (a) 1/
r
as a function of
C
I
as per Dixon’s ...
Figure 29.6 Michaelis and Menten's mechanism involving enzyme
E
and substrat...
Figure 29.7 Variation of normalized rate of enzymatic reaction,
r
*
, as a fun...
Figure 29.8 Variation, as a function of total concentration of active enzyme...
Chapter 30
Figure 30.1 Enzymatic
Bi Bi
mechanisms, viz. (a) sequential random, (b) sequ...
Figure 30.2 Typical variation of 1/
r
as a function of (a–c) 1/
C
S
or (d–f) 1/
Chapter 31
Figure 31.1 Variation of forward rate,
r
f,sr,ssBU
, of enzymatic reaction fol...
Figure 31.2 Michaelis and Menten's mechanism involving enzyme
E
(possessing ...
Figure 31.3 Michaelis and Menten's mechanism involving enzyme
E
(possessing ...
Figure 31.4 Variation of fractional concentration of enzyme in free form,
C
E
Figure 31.5 Variation of rate of reaction catalyzed by three‐sited enzyme as...
Figure 31.6 Variation of rate of reaction catalyzed by
N
-sited enzyme as pre...
Figure 31.7 Michaelis and Menten's mechanism involving enzyme
E
(possessing ...
Figure 31.8 Variation of fractional concentration of enzyme in free form,
C
E
Figure 31.9 Variation of rate of reaction catalyzed by three‐sited enzyme, a...
Figure 31.10 Michaelis and Menten's mechanism involving enzyme
E
(possessing...
Figure 31.11 Variation of rate of reaction catalyzed by
N
-sited enzyme as pr...
Figure 31.12 Michaelis and Menten's mechanism involving enzyme
E
(possessing...
Figure 31.13 Variation of fractional concentration of enzyme in free forms, ...
Figure 31.14 Variation of rate of reaction catalyzed by two‐sited enzyme as ...
Figure 31.15 Variation of rate of reaction catalyzed by two‐sited enzyme as ...
Figure 31.16 Variation of rate of reaction catalyzed by
N
-sited enzyme, as p...
Figure 31.17 Variation of rate of reaction catalyzed by
N
‐sited enzyme as pr...
Figure 31.18 Variation of logarithm of product of reciprocal of rate of reac...
Figure 31.19 Variation of rate of reaction catalyzed by
N
-sited enzyme as pr...
Figure 31.20 Variation of (a) rate of reaction catalyzed by N-sited enzyme a...
Figure 31.21 Variation of rate of reaction catalyzed by
N
-sited enzyme as pr...
Figure 31.22 Molecular mechanism – via Michaelis and Menten’s approach, asso...
Guide
Cover Page
Series Page
Title Page
Copyright
Dedication
About the Author
Series Preface
Preface
Series Page
Title Page
Copyright Page
Dedication
About the Author
Series Preface
Preface
Table of Contents
Begin Reading
Further Reading
Further Reading
Index
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Enzyme Reactor Engineering
Published Titles
MATHEMATICS FOR ENZYME REACTION KINETICS AND REACTOR PERFORMANCE
Volume 1
1. Basic Concepts of Algebra
Volume 2
2. Basic Concepts of Calculus
3. Basic Concepts of Statistics
Analysis of Enzyme Reaction Kinetics
Volume 1
F. Xavier Malcata
Department of Chemical Engineering & LEPABE/ALiCE
University of Porto
Portugal
The universe is like a safe to which there is a combination, but the combination is locked up in the safe.
Peter de Vries
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Library of Congress Cataloging‐in‐Publication Data
Names: Malcata, F. Xavier, author.Title: Analysis of enzyme reaction kinetics / F. Xavier Malcata, Department of Chemical Engineering, University of Porto, Portugal.Description: Hoboken, N.J. : Wiley, 2019. | Series: Enzyme reactor engineering | Includes bibliographical references and index. |Identifiers: LCCN 2018055911 (print) | LCCN 2018056498 (ebook) | ISBN 9781119490234 (AdobePDF) | ISBN 9781119490098 (ePub) | ISBN 9781119490241(hardback)Subjects: LCSH: Enzyme kinetics. | BISAC: TECHNOLOGY & ENGINEERING / Chemical & Biochemical.Classification: LCC QP601.3 (ebook) | LCC QP601.3.M347 2019 (print) | DDC 572/.744–dc23LC record available at https://lccn.loc.gov/2018055911
Cover Design: WileyCover Images: © Zarya Maxim Alexandrovich/Shutterstock,© Laguna Design/Getty Images, Courtesy of F. Xavier Malcata
To my family: António, Mª Engrácia, Ângela, Filipa, and Diogo.For their everlasting understanding, unselfish support, and endless love.
About the Author
Par est scientia laboris.
(Work is the ever mate of science.)
Prof. F. Xavier Malcata was born in Malange (Angola) in 1963, and earned: a BSc degree in Chemical Engineering (5‐year program), by the College of Engineering of University of Porto (UP, Portugal) in 1986 (with first class honors); a PhD degree in Chemical Engineering (with a distributed minor in Food Science, Statistics, and Biochemistry), by the University of Wisconsin – Madison (UW, USA) in 1991; an equivalence Doctoral degree in Biotechnology – food science and technology, by the Portuguese Catholic University (UCP, Portugal) in 1998; and a Habilitation degree in Food Science and Engineering, also by UCP, in 2004.
Prof. Malcata held academic appointments as: Teaching Assistant at UCP in 1985–1987 and at UW in 1988; Lecturer at UW in 1989; Assistant Professor at UCP in 1991–1998; Associate Professor at UCP in 1998–2004; and Full Professor at UCP in 2004–2010, Superior Institute of Maia (ISMAI, Portugal) in 2010–2012, and UP from 2012 on. He also held professional appointments as: Dean of the College of Biotechnology of UCP in 1998–2008; President of the Portuguese Society of Biotechnology in 2003–2008; Coordinator of the Northern Chapter of Chemical Engineering of the Portuguese Engineering Accreditation Board in 2004–2009; Official Delegate, in 2002–2013, of the Portuguese Government to the VI and VII Framework R&D Programs by the European Union – in such key areas as Food quality and safety, and Food, agriculture (including fisheries) and biotechnology, respectively; Chief Executive Officer of the University/Industry Extension (non‐profit) Associations AESBUC in 1998–2008 and INTERVIR+ in 2006–2008; and Chief Executive Officer of the Entrepreneurial Biotechnological Support Associations CiDEB in 2005–2008 and INOVAR&CRESCER in 2006–2008. Prof. Malcata is currently a senior researcher at Laboratory for Process Engineering, Environment, Biotechnology, and Energy (LEPABE, Portugal).
Over the years, the author received several national and international public recognitions and awards, including: Cristiano P. Spratley Award by UP, in 1985; Centennial Award by UP, in 1986; election for membership in Phi Tau Sigma – honor society of food science (USA), in 1990; election for Sigma Xi – honor society of scientific and engineering research (USA), in 1990; election for Tau Beta Pi – honor society of engineering (USA), in 1991; Ralph H. Potts Memorial Award by American Oil Chemists' Society (AOCS, USA), in 1991; election for New York Academy of Sciences (USA), in 1992; Foundation Scholar Award – dairy foods division by American Dairy Science Associaton (ADSA, USA), in 1998; decoration as Chevalier dans l'Ordre des Palmes Académiques by French Government, in 1999; Young Scientist Research Award by AOCS, in 2001; Canadian/International Constituency Investigator Award in Physical Sciences and Engineering by Sigma Xi, in 2002 and 2004; Excellence Promotion Award by Portuguese Foundation for Science and Technology (Portugal), in 2005; Danisco International Dairy Science Award by ADSA, in 2007; Edgar Cardoso Innovation Award by the Mayor of Gaia, in 2007; Scientist of the Year Award by European Federation of Food Science and Technology (Netherlands), in 2007; Samuel C. Prescott Award by Institute of Food Technologists (IFT, USA), in 2008; International Leadership Award by International Association of Food Protection (IAFP, USA), in 2008; election for Fellow by IFT, in 2011; Elmer Marth Educator Award by IAFP, in 2011; election for Fellow by International Academy of Food Science and Technology (IAFoST), in 2012; Distinguished Service Award by ADSA, in 2012; J. Dairy Sci. Most Cited Paper Award by ADSA, in 2012; election for Fellow by ADSA, in 2013; William V. Cruess Award for excellence in teaching by IFT, in 2014; election for Fellow by AOCS, in 2014; and International Dairy Foods Association Teaching Award in Dairy Manufacturing by ADSA, in 2020.
Among his many scientific interests, Prof. Malcata has focussed his research chiefly on four major areas: theoretical simulation and optimization of enzyme reactors; theoretical optimization of thermodynamically‐ and kinetically‐controlled processes; production and immobilization of oxidoreductases and hydrolases for industrial applications; and design and optimization of bioreactors to produce and process edible oils. In addition, he has developed work on: microbiological and biochemical characterization, and technological improvement of traditional foods; development of nutraceutical ingredients and functional foods; rational application of unit operations to specific agri‐food processing; and design and development of novel photobioreactors for cultivation of microalgae, aimed at biofuel or high added‐value compound production. To date, he has published 425+ papers in peer-reviewed international journals that received more than 15,500 official citations in all (w/o self‐citations), corresponding to an h-index of 62; he has supervised 31 PhD dissertations successfully concluded; he wrote 15 monographic books and edited 5 multiauthored books; and he authored more than 50 chapters in edited books and 35 papers in trade journals, besides more than 50 technical publications. He was also a member of ca. 60 peer reviewing committees of research projects and fellowships; he acted as supervisor of 92 individual fellowships, most at PhD and postdoctoral levels, and collaborated in 61 R&D projects – of which he has served as principal investigator in 37; he participated in 51 organizing/scientific committees of professional meetings; he delivered 150+ invited lectures worldwide, besides almost 600 volunteer presentations in congresses and workshops; he has served in the editorial board of 5 major journals in the applied biotechnology, and food science and engineering areas; and he reviewed several hundred manuscripts for journals and encyclopediae. He has been a longstanding member of American Institute of Chemical Engineers, American Chemical Society, IFT, American Association for the Advancement of Science, AOCS, IAFP, and ADSA.
Series Preface
Ad augusta per angusta.
(Toward the top, through hard work.)
Comprehensive mathematical simulation – using mechanistic models as far as possible, constitutes an essential contribution to rationally characterize performance, as well as support design and drive optimization of any enzyme reactor. However, too often studies available in the literature – including text and reference books, deal with extensive modelling of chemical reactors that employ inorganic catalysts, or instead present extensive kinetic analysis of enzymes acting only (and implicitly) in batch apparatuses. Although constraining from an engineering perspective, this status quo is somewhat expected – because chemical engineers typically lack biochemical background, while biochemists miss engineering training. Meanwhile, rising environmental concerns and stricter legislation worldwide have urged the industry to resort to more sustainable, efficient, and cleaner processes – which tend to mimic natural (i.e. enzyme‐mediated) pathways; they generate essentially no polluting effluents or residues, require mild conditions of operation, and exhibit low‐energy requirements – while taking advantage of the extremely high activity and unique substrate selectivity of enzymes. The advent of genetic engineering has also dramatically contributed to drop the unit price, and widen the portfolio of enzymes for industrial purposes, via overexpression in transformed microorganisms and development of sophisticated purification techniques; and advances in molecular engineering have further permitted specific features, in terms of performance and stability, be imparted to enzymes for tailored uses – besides overcoming their intrinsic susceptibility to decay.
An innovative approach is thus in order, where fundamental and applied aspects pertaining to enzyme reactors are comprehensively tackled – built upon mathematical simulation, and encompassing various ideal and nonideal configurations, presented and discussed in a consistent and pragmatic way. Enzyme Reactor Engineering pursues this goal, and accordingly conveys the most integrated and complete treatment of the subject of enzyme reactors to date; it will likely materialize a qualitative leap toward more efective strategies of describing, designing, and optimizing said reactors. More than a mere description of technology, true engineering aspects departing from first principles are put forward, and their rationale is systematically emphasized – with special attention paid to stepwise derivation of the underlying equations, so as to permit a self‐paced learning program by any student possessing elementary knowledge of algebra, calculus and statistics. A careful selection of mathematical tools deemed useful for enzyme reactors is also provided in dedicated volumes, for the more inquisitive students and practitioners – in a straightforward, yet fully justified manner. Furthermore, appropriate examples, based (at least) on Michaelis and Menten's enzymatic kinetics and first order enzyme decay, are worked out in full – for their being representative of industrial situations, while exhibiting a good compromise between practical applicability and mathematical simplicity. In this regard, the present book collection represents an unparalleled way of viewing enzyme reactors – clearly focused on the reactor component but prone to build an integrated picture, including mixture via momentum and mass transfer, and subsequent transformation via chemical reaction, with underlying enthalpic considerations as found necessary.
In a word, Enzyme Reactor Engineering
