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 Food Safety of Proteins
in Agricultural Biotechnology

Copyright 2008 by Taylor and Francis Group, LLC

3967_C000.indd 1 10/20/07 12:25:43 PM

 FOOD SCIENCE
AND TECHNOLOGY

Editorial Advisory Board

Gustavo V. Barbosa-Cánovas Washington State University–Pullman
P. Michael Davidson University of Tennessee–Knoxville
Mark Dreher McNeil Nutritionals, New Brunswick, NJ
Richard W. Hartel University of Wisconsin–Madison
Lekh R. Juneja Taiyo Kagaku Company, Japan
Marcus Karel Massachusetts Institute of Technology
Ronald G. Labbe University of Massachusetts–Amherst
Daryl B. Lund University of Wisconsin–Madison
David B. Min The Ohio State University
Leo M. L. Nollet Hogeschool Gent, Belgium
Seppo Salminen University of Turku, Finland
John H. Thorngate III Allied Domecq Technical Services, Napa, CA
Pieter Walstra Wageningen University, The Netherlands
John R. Whitaker University of California–Davis
Rickey Y. Yada University of Guelph, Canada

Copyright 2008 by Taylor and Francis Group, LLC

3967_C000.indd 2 10/20/07 12:25:43 PM

 Food Safety of Proteins
in Agricultural Biotechnology

Edited by Bruce G. Hammond

Boca Raton London New York

CRC Press is an imprint of the

Taylor & Francis Group, an informa business

Copyright 2008 by Taylor and Francis Group, LLC

3967_C000.indd 3 10/20/07 12:25:44 PM

 CRC Press
Taylor & Francis Group
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Boca Raton, FL 33487-2742
© 2008 by Taylor & Francis Group, LLC
CRC Press is an imprint of Taylor & Francis Group, an Informa business

No claim to original U.S. Government works

Printed in the United States of America on acid-free paper
10 9 8 7 6 5 4 3 2 1

International Standard Book Number-13: 978-0-8493-3967-7 (Hardcover)

This book contains information obtained from authentic and highly regarded sources. Reprinted
material is quoted with permission, and sources are indicated. A wide variety of references are
listed. Reasonable efforts have been made to publish reliable data and information, but the author
and the publisher cannot assume responsibility for the validity of all materials or for the conse-
quences of their use.

No part of this book may be reprinted, reproduced, transmitted, or utilized in any form by any
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Trademark Notice: Product or corporate names may be trademarks or registered trademarks, and
are used only for identification and explanation without intent to infringe.

Library of Congress Cataloging-in-Publication Data

Food safety of proteins in agricultural biotechnology / editor, Bruce G.

Hammond. -- 1st ed.
p. cm. -- (Food science and technology ; 172)
Includes bibliographical references and index.
ISBN 978-0-8493-3967-7 (alk. paper)
1. Agricultural biotechnology--Risk assessment. 2. Bacterial proteins. 3.
Food--Safety measures. I. Hammond, Bruce G. (Bruce George), 1947- II. Series:
Food science and technology (Taylor & Francis) ; 172.

S494.5.B563S24 2008
363.19’2--dc22 2007021159

Visit the Taylor & Francis Web site at

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and the CRC Press Web site at
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Copyright 2008 by Taylor and Francis Group, LLC

3967_C000.indd 4 10/20/07 12:25:47 PM

 Dedication

This book is dedicated to my family who are most dear to

me. I am grateful to my wife who was always understanding
of the extra hours it took to complete the book. I am
thankful for my parents who had the vision and sacrificed
to enable their children to get an education. Lastly, I
speak to my posterity — those who are here and others yet
to come. Remember, all things are possible to those who
believe and work to make their dreams come true. This
grandpa wondered at times whether he would ever complete
this book but he never gave up, and now it’s done.

Copyright 2008 by Taylor and Francis Group, LLC

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 Contents
Chapter 1 Protein Structure and Function in Plants and Animals........................1
Peter J. Garlick

Chapter 2 The Mode of Action of Bacterial Protein Toxins:

The Role of Conformational Changes in the Life Cycle
of a Protein Toxin................................................................................ 31
Jeffrey W. Seale and Leigh English

Chapter 3 Safety Assessment of Bacillus thuringiensis and Bt Crops

Used in Insect Control......................................................................... 45
Brian A. Federici and Joel P. Siegel

Chapter 4 Ecological Safety Assessment of Insecticidal Proteins

Introduced into Biotech Crops.......................................................... 103
Jeffrey D. Wolt, Jarrad R. Prasifka, and Richard L. Hellmich

Chapter 5 The Safety of Microbial Enzymes Used in Food Processing........... 127

Michael W. Pariza

Chapter 6 Safety Assessment of Biotechnology-Derived

Therapeutic Drugs............................................................................. 133
Barbara J. Mounho, Jeanine L. Bussiere,
and Andrea B. Weir

Chapter 7 The Food Safety Assessment of Bovine Somatotropin (bST).......... 167

Bruce Hammond

Chapter 8 Assessment of Food Proteins for Allergenic Potential.....................209

Scott McClain, Stefan Vieths, and Gary A. Bannon

Chapter 9 Methods for Estimating the Intake of Proteins in Food.................... 223

Barbara J. Petersen

Copyright 2008 by Taylor and Francis Group, LLC

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 Chapter 10 Safety Assessment of Proteins Used in Crops Developed
through Agricultural Biotechnology: Industry Perspective.............. 237
Elena A. Rice, Thomas C. Lee, Glen Rogan,
and Gary A. Bannon

Chapter 11 The Safety Assessment of Proteins Introduced into Crops

Developed through Agricultural Biotechnology: A Consolidated
Approach to Meet Current and Future Needs................................... 259
Bruce Hammond and Andrew Cockburn

Copyright 2008 by Taylor and Francis Group, LLC

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 Preface
The editor has been involved with the safety assessment of proteins used in food pro-
duction for more than 20 years. During that time, I have answered many questions
regarding the safety of proteins developed by Monsanto. Some of the questions were
asked by those who were familiar with the safety assessment of small-molecular-
weight chemicals (pesticides and food additives). They would sometimes ask why
we had not carried out classical toxicology studies with proteins as is done for pesti-
cides. At the time, I wished there had been a general text available that I could refer
questioners to that discussed how toxicology testing of proteins should be accom-
plished. Although many of the safety questions have since been resolved, there is
still a need today for a comprehensive reference text that addresses how to carry
out protein safety assessments. Therefore, several internationally recognized experts
on protein safety assessment accepted the invitation to contribute to the creation of
this book, which should serve as a needed reference text. The book may also be of
general interest to those who want to learn more about the safety assessment of bio-
technology-derived products.
The first chapter provides a background on protein biology and addresses
some of the fundamental differences between proteins and small-molecular-weight
chemicals that impact their safety assessment. The second chapter discusses the life
cycle of protein toxins and explains why some protein toxins exert toxic effects when
ingested whereas others do not. The third and fourth chapters provide a comprehen-
sive background on the safety assessment and environmental impact of insect-pro-
tected Bt crops and answers many of the safety questions that have been raised. These
crops are now widely grown in the United States and increasingly in other countries.
Chapter 5 reviews the safety assessment process developed for enzymes, which is
one of the earliest applications of proteins used in food processing and production.
Chapters 6 and 7 address the safety assessment of protein pharmaceuticals. Chapter
6 discusses the unique challenges of testing protein therapeutics in humans. Chapter
7 reviews the safety assessment of bST used in dairy cows to increase milk produc-
tion and summarizes some of the controversies that arose and how safety questions
were answered. Chapter 8 discusses how to confirm that an introduced protein does
not fit the profile of known protein food allergens. Chapter 9 provides direction on
how to carry out dietary exposure assessments for proteins introduced into food
crops, and sources of food consumption databases that are available internationally.
Chapter 10 provides four case studies on the safety assessment of proteins of differ-
ent structure and function to be introduced into biotechnology-derived agricultural
crops. The final chapter distills the conclusions about protein safety assessment from
the preceding 10 chapters that have been used to develop a comprehensive safety
assessment strategy that is applicable to existing and next-generation biotechnology-
derived crops.

Copyright 2008 by Taylor and Francis Group, LLC

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 Acknowledgments
The editor gratefully acknowledges the contributions of the many authors who have
contributed so much of their time to make this book possible. Appreciation is also
expressed to my colleagues at Monsanto who have provided helpful comments on
the book and have contributed over the years to the development of a comprehensive
protein safety assessment strategy that is discussed in this book.

Copyright 2008 by Taylor and Francis Group, LLC

3967_C000.indd 11 10/20/07 12:25:50 PM

 Editor
Dr. Bruce Hammond was born in Canada and received a B.S. in chemistry at
Brigham Young University and a Ph.D. in pharmacology at the University of Illinois
Medical Center, Chicago. He completed postdoctoral training with Robert Metcalfe at
the Institute of Environmental Studies, University of Illinois, Urbana-Champaign.
He is the father of seven children and, at last count, has seven grandchildren.
Dr. Hammond joined Monsanto in 1978 and has worked in various divisions during
those years, including industrial chemicals, pharmaceuticals, nutritional chemicals,
and agricultural chemicals. He first became involved with biotechnology in the
1980s, as he managed the food safety assessment program for sometribove (rbST).
As the plant biotechnology program progressed, he had the opportunity to help
design and manage the human food safety studies on improved crop varieties devel-
oped through biotechnology. He has published a number of papers on biotech food
safety assessments and presented results at several conferences and symposia. Dr.
Hammond was also appointed to the Monsanto Science Fellow Program and cur-
rently serves as manager of food toxicology in the Monsanto Product Safety Center.
He is also serving a one-year term as president of the Food Safety Specialty Section
of the Society of Toxicology. His current research interests also include evaluating
the reduction of mycotoxin contamination of grain from insect-protected (Bt) corn
varieties grown around the world.

Copyright 2008 by Taylor and Francis Group, LLC

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 Contributors
Gary A. Bannon Scott McClain
Monsanto Company Product Characterization Center
St. Louis, Missouri Monsanto Company
St. Louis, Missouri
Jeanine L. Bussiere
Amgen, Inc.
Thousand Oaks, California Barbara J. Mounho
Amgen, Inc.
Andrew Cockburn Thousand Oaks, California
Monsanto UK Ltd.
Trumpington
Michael W. Pariza
Cambridge, United Kingdom
Food Research Institute
Leigh English University of Wisconsin
Monsanto Company Madison, Wisconsin
St. Louis, Missouri
Barbara J. Petersen
Brian A. Federici
Exponent, Inc.
Department of Entomology & Graduate
Washington, D.C.
Programs in Genetics & Microbiology
University of California, Riverside
Riverside, California Jarrad R. Prasifka
Corn Insects and Crop Genetics
Peter J. Garlick Research
Animal Sciences Iowa State University
University of Illinois Ames, Iowa
Urbana, Illinois

Bruce Hammond Elena A. Rice

Monsanto Company Product Characterization Center
St. Louis, Missouri Monsanto Company
St. Louis, Missouri
Richard L. Hellmich
Entomology Department Glen Rogan
Iowa State University Regulatory Affairs
Ames, Iowa Monsanto Company
St. Louis, Missouri
Thomas C. Lee
Product Characterization Center Jeffrey W. Seale
Monsanto Company Monsanto Company
St. Louis, Missouri Chesterfield, Missouri

Copyright 2008 by Taylor and Francis Group, LLC

3967_C000.indd 15 10/20/07 12:25:51 PM

 Joel P. Siegel Andrea B. Weir
Research Entomologist Charles River Laboratories, Navigators
USDA ARS Sparks, Nevada
Parlier, California
Jeffrey D. Wolt
Stefan Vieths Biosafety Institute for Genetically
Department of Allergology Modified Agricultural Products
Paul-Ehrlich-Institut Iowa State University
Langen, Germany Ames, Iowa

Copyright 2008 by Taylor and Francis Group, LLC

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 1 Protein Structure
and Function in
Plants and Animals
Peter J. Garlick

Contents
1.1 Introduction.......................................................................................................1
1.2 Amino Acids.....................................................................................................2
1.3 Protein Function: Animals, Including Humans................................................4
1.4 Protein Functions: Plants..................................................................................5
1.5 Protein Synthesis..............................................................................................6
1.6 Protein Structure............................................................................................. 13
1.7 Protein Degradation in the Cell...................................................................... 23
1.8 Digestion of Proteins Consumed as Food.......................................................25
1.9 Summary......................................................................................................... 27
References.................................................................................................................28

1.1 INTRODUCTION
Proteins are macromolecules composed of polymeric chains of amino acids linked
together in a sequence that is unique for each protein. They provide much of the struc-
ture of the cell and comprise the largest percentage of the cell mass.1 The amino acid
building blocks that make up proteins are drawn from a standard repertoire of 20 amino
acids that are the common for all living cells.1 Millions of proteins of diverse structure
and function are found in all living organisms. The amino acid sequences of more than
2.3 million proteins have been determined, or predicted based on DNA sequence, and
have been catalogued in searchable protein databases.2 Approximately 74% of the cata-
logued proteins are organized into 7677 different families according to their relatedness
in structure and function.2 The same families of proteins whose structure and function
are related can be found across different orders in plant and animal kingdoms. “For
distantly related species, nature doesn’t reinvent the wheel. Similar proteins involved
in essential cellular functions are often similar across species.”3 For example, a recent
comparison of the protein–protein interactions for three distantly related species (yeast,
worm, fly) found some conservation in the proteins and patterns of interactions, although
differences were also noted.4 Humans share proteins with similar amino acid sequence
and function with other organisms, as observed for the hemoglobin a chain where the

Copyright 2008 by Taylor and Francis Group, LLC

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  Food Safety of Proteins in Agricultural Biotechnology

percentage of identical amino acids (human/animal) ranges from 35% for lamprey to
56% for frog and 70% for chicken.5 Genome sequences reveal that vertebrates have
inherited nearly all of their protein domains from invertebrates; only 7% of identified
human protein domains are vertebrate-specific.1

1.2 Amino Acids

Amino acids all possess a carboxylic acid group and an amino group, both linked
to a single car­bon atom called the a-carbon (Figure 1.1). The differences between
amino acids result from the side chain attached to the a-carbon atom, which can be

The Amino Acid Optical Isomers The α-carbon atom is asymmetric, which
The general formula of an amino acid is allows for two mirror image (or stereo-)
isomers, L and D.
α-carbon Atom
H
Amino Carboxyl
H N C COOH
Group 2 Group
+ COO– COO– +
R NH3 NH3
Side-chain Group
R is commonly one of 20 different side chains. L Cα Cα D
At pH 7 both the amino and carboxyl groups
are ionized.
H R R H
H
+ –
H3N C COO

R
Proteins consist exclusively or L-amino acids.

Families of Basic Side Chains

Amino Acids Lysine Arginine Histidine
The common amino acids (Lys, or K) (Arg, or R) (His, or H)
are grouped according to
whether their side chains H O H O H O
are N C C N C C N C C
Acidic H CH2 H CH2 H CH2
Basic
Uncharged polar CH2 CH2 C
Nonpolar HN CH
CH2 This group is CH2
These 20 amino acids
very basic HC NH+
CH2 because its NH
are given both three-letter These nitrogens have a
+ positive charge
and one-letter abbreviations. NH3 C relatively weak affinity for an
is stabilized by
resonance. +H N NH2 H+ and are only partly positive
Thus: alanine = Ala = A 2
at neutral pH.

Peptide Bonds
Amino acids are commonly joined together by an amide linkage, Peptide bond: The four atoms in each gray box form a rigid
called a peptide bond. planar unit. There is no rotation around the C–N bond.

H2O
H H O H R O H O R
H O
N C C + N C C N C C N C C
H R OH H H OH H OH
R H H
SH
Amino- or Carboxyl- or
Proteins are long polymers N-terminus H O CH2 H H C-terminus
of amino acids linked by +H N
3 C C N C C N C COO–
peptide bonds, and they
are always written with the CH2 H O CH
N-terminus toward the left.
The sequence of this tripeptide C CH3 CH3
is histidine-cysteine-valine. HN CH These two single bonds allow rotation, so that long chains of
amino acids are very flexible.
HC NH+

Figure 1.1  The 20 amino acids found in proteins.

Copyright 2008 by Taylor and Francis Group, LLC

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 Protein Structure and Function in Plants and Animals 

Acidic Side Chains Nonpolar Side Chains

Alanine Valine
Aspartic Acid Glutamic Acid (Ala, or A) (Val, or V)
(Asp, or D) (Glu, or E) H O H O
H O H O N C C N C C
N C C N C C H CH3 H CH
H CH2 H CH2 CH3 CH3

C CH2
O O– C Leucine Isoleucine

O O– (Leu, or L) (Ile, or I)

H O H O

N C C N C C

H CH2 H CH

CH CH3 CH2
Uncharged Polar Side Chains CH3 CH3 CH3

Asparagine Glutamine Proline Phenylalanine

(Asn, or N) (Gln, or Q) (Pro, or P) (Phe, or F)

H O H O H O H O

N C C N C C N C C N C C
H CH2 H CH2 CH2 CH2 H CH2

C CH2 (actually an CH2

imino acid)
O NH2 C
O NH2
Methionine Tryptophan
(Met, or M) (Trp, or W)

H O H O
Although the amide N is not charged at N C C N C C
neutral pH, it is polar.
H CH2 H CH2

CH2

S CH3 N
Serine Threonine Tyrosine
H
(Ser, or S) (Thr, or T) (Tyr, or Y)

H O H O H O Glycine Cysteine

N C C N C C N C C (Gly, or G) (Cys, or C)

H CH2 H CH CH3 H CH2 H O H O

OH OH N C C N C C

H H H CH2
OH SH

The –OH group is polar. Disulfide bonds can form between two cysteine side chains in proteins.

CH2 S S CH2

Figure 1.1  Continued

aliphatic or aromatic in nature and can include extra amino, imino, or carboxylic
acid functional groups (Figure 1.1). All amino acids except glycine can exist as opti-
cal isomers in D- and L-forms (Figure 1.1), but only L-forms are found in living
organisms (with the exception of D amino acids in certain bacterial cell wall pro-
teins).6 The chemical versatility provided by the 20 common amino acids is critically
important to the function of proteins. Five of the 20 amino acids have side chains that
can form ions in solution and impart polar and hydrophilic properties to the protein.

Copyright 2008 by Taylor and Francis Group, LLC

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  Food Safety of Proteins in Agricultural Biotechnology

Other amino acids have aliphatic side chains that are nonpolar and are therefore hydro-
phobic. Structures for the various amino acids are presented in Figure 1.1. The collec-
tive prop­erties of the amino acid side chains underlie the diverse and sophisticated
functions that proteins perform.1
Amino acids are connected together via covalent peptide bonds formed between
the amino functional group on the a-carbon of one amino acid and the carboxyl
functional group attached to the a-carbon on the adjacent amino acid. The forma-
tion of a covalent “peptide bond” occurs through the action of enzymes resulting in
the loss of water (dehydration reaction) and the formation of an amide bond between
adjacent amino acids (Figure 1.1). Proteins are polymers of amino acids joined head-
to-tail in a long chain that is then folded into a three­-dimensional structure unique to
each protein. When several amino acids (less than 50) are linked together covalently
in a chain, the resulting molecule is called a “polypeptide” or peptide.1 When the
amino acid chains are composed of more than 50 amino acids connected together,
the polymer is considered a protein.1 All polypeptides and proteins have an amino
(NH2) group at one end (N-terminus) and a carboxyl (COOH) group at the other end
(C-terminus). This gives it a definite directionality — a structural (as opposed to an
electrical) polarity.

1.3 Protein Function: Animals, Including Humans

In the human body, it is estimated that there are more than 250,000 unique proteins
that fulfill a variety of biological functions.6 Examples of biological functions that
proteins fulfill within mammalian cells are as follows:

• Structural: proteins that provide the scaffold for tissues, cells, and sub-
celluar organelles (e.g., skin, muscle, bone, blood vessels, cytoskeleton).
Examples are collagen, a-keratin, actin and myosin, fibronectin, etc.
• Regulatory: protein hormones that carry messages from one part of the
body to the other to help maintain homeostasis. Examples are insulin,
thyrotropin, somatotropin, follicle-stimulating hormone, etc.
• Osmotic: proteins help regulate osmotic and pH balance in biological flu-
ids. Examples are plasma albumins, immunoglobulins, lipoproteins, etc.
• Metabolism: protein enzymes catalyze a multitude of chemical reactions
within cells. Examples are proteases that break down proteins, polymer-
ases (which catalyze the synthesis of DNA and RNA), ATPases (which
hydrolyze ATP, providing energy to support cellular reactions), etc.
• Transport: proteins that transport substances (lipids, vitamins, oxygen,
etc.) throughout the body and into and out of cells. Examples are hemo-
globin (which transports oxygen in the blood) and transferrin (which car-
ries iron in the blood to various body tissues).
• Defense: coagulation proteins (which prevent blood loss) and immuno-
globulins (which defend against invading pathogens such as viruses and
bacteria). Examples are fibrin (which prevents blood loss following injury
to the vascular system), and immunoglobulins and interferon (which pro-
tect the body against bacterial or viral infection).

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 Protein Structure and Function in Plants and Animals 

• Motor function: motile proteins that allow cells to move, contract, or change
shape; and permit muscle contraction, movement of chromosomes during
cell division, and nerve axon transport. Examples are actin and myosin
(which are involved in the contraction of muscle tissue), kinesin, and dynein
motor proteins involved in movement of chromosomes and flagella.

1.4 Protein functions: plants

Proteins also comprise a significant percentage of the plant cell by weight; it has been
estimated that a typical plant cell contains 5000 to 10,000 different polypeptides
and millions of individual protein molecules.7 Some proteins are structurally and/or
functionally related to mammalian proteins as they fulfill similar biochemical roles
in the plant cell. Examples of biological functions fulfilled by proteins within plant
cells are as follows:
• Structural: structural proteins maintain the integrity of plant cell walls,
cytoskeleton, etc. Examples are actin microfilaments and microtubules of
tubulin that form the cytoskeleton, glycoproteins in the cell wall, etc.
• Defense: plants have developed a sophisticated array of pathogenesis pro-
teins that defend the plant against bacterial, fungal, or viral infection. Some
of these proteins also are effective in protecting plants against insect feeding
or infection by plant pathogens. Examples of pathogenesis-proteins include
protease inhibitors, defensins, thionins, chitinases, lectins, ribosomal inac-
tivating proteins, etc.8 A few members of these pathogenesis-proteins have
the distinction of being toxic to mammals and will be discussed in later
chapters.
• Motor function: although plants do not contain skeletal muscle com-
posed of complexes of actin/myosin, they do contain myosin, kinesin, and
dynein proteins that facilitate movement of chromosomes during cell divi-
sion and transport of molecules through the cytoplasm and the movement
of vesicles along microtubules.9
• Metabolism: as in mammals, protein enzymes catalyze a myriad of bio-
chemical reactions in plant cells. Some of these reactions are similar to
those that occur in mammalian cells, whereas others are different, such as
enzymes like sucrase, desaturases, nitrogenase, cellulose synthase, etc.

Certain biochemical functions are unique to plant cells and have no correlates in
mammals; these include:

• Photosynthesis: plant proteins that facilitate transfer of energy from light

into plant cell metabolism.10,11 The enzyme called rubisco (ribulose 1,5-
biphosphate carboxylase/oxygenase) is one of the most abundant proteins
in the world, as it is present in nearly all plant cells.12 It is enzyme-involved
in photosynthesis by helping to convert CO2 to sugars that are essential to
plant survival. Some have considered this enzyme the most important of
all enzymes since it is involved in the first step in photosynthesis, which
sustains the plant life other organisms depend upon for food.9

Copyright 2008 by Taylor and Francis Group, LLC

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  Food Safety of Proteins in Agricultural Biotechnology

Table 1.1
Molecular Weights of Various Mammalian and Plant Proteins
Molecular Weight
Protein Source (Daltons)1,6
Insulin Mammal 6000
Lysozyme Mammal 15,000
Albumin Mammal 69,000
IgG immunoglobulin Mammal 150,000
Factor VIII (coagulation) Mammal 285,000
IgM immunoglobulin Mammal 950,000
Plant
Zeins Plant (maize) 10,000–58,000
Vicilin Plant (garden pea) 186,000
Glycinin Plant (soybean) 330,000
Rubisco Plant 560,000
Pyruvate dehyrdrogenase Plant 5,086,000
protein complex

• Storage proteins: provide a reserve of food (proteins) to support the ger-

mination of the seed and growth of the plant during early growth. Seed
proteins have been divided into four classes based on their water solubil-
ity: albumins (barley, oats, wheat, etc.), globulins (wheat, maize, etc.), glu-
telins (wheat), and prolamins (barley, wheat, maize, etc.). Storage proteins
also provide essential food for humans and farm animals.11

Proteins are considered to be macromolecules since their size and molecular

weight are quite large compared to other small molecules such as glucose and indi-
vidual amino acids, whose molecular weight ranges from 75 to 300 Daltons. Most
proteins consist of 50 to 2000 amino acids.1 The molecular weight of mammalian
and plant cell proteins ranges considerably, as shown in Table 1.1.

1.5 Protein synthesis

Although there is considerable diversity in the kinds of proteins produced in ani-
mal and plants cells, all of these proteins are made from the same 20 amino acids
common to all living organisms. The template used to make the diverse proteins
found in all living organisms resides within the genes present in each organism. In
mammalian cells, the DNA is found in the nucleus of each cell. Genes are composed
of four different nucleic acids: adenine (A), cytosine (C), guanine (G), and thymine
(T). These nucleic acids are also common to all living organisms and are the primary
constituents of DNA, which provides the master code for the synthesis of all proteins

Copyright 2008 by Taylor and Francis Group, LLC

3967_C001.indd 6 10/24/07 10:48:49 AM

 Protein Structure and Function in Plants and Animals 

(a) Building Block of DNA (d) Double-stranded DNA

Phosphate
Sugar

+ G
Sugar Base G A C T G G C A A T G
Phosphate Nucleotide
T G A C C G T T A C

(b) DNA Strand

Sugar-phosphate Hydrogen-bonded
G T A A C G G T C A Backbone Base Pairs

(e) DNA Double Helix

(c) Templated Polymerization of New Strand

Nucleotide
Monomers C
C A T A
C G
A A T
G
G G
C G
T G
C A T T G
C
A C A
G T A A C G G T C A C

Figure 1.2  DNA and its building blocks. (A) DNA is made from simple subunits, called
nucleotides, each consisting of a sugar-phosphate molecule with a nitrogen-containing side-
group, or base, attached to it. The bases are of four types (adenine, guanine, cytosine, and
thymine), corresponding to four distinct nucleotides, labeled A, G, C, and T. (B) A single
strand of DNA consists of nucleotides joined together by sugar-phosphate linkages. Note
that the individual sugar-phosphate units are asymmetric, giving the backbone of the strand
a definite directionality, or polarity. This directionality guides the molecular processes by
which the information in DNA is interpreted and copied in cells: the information is always
“read” in a consistent order, just as written English text is read from left to right. (C) Through
templated polymerization, the sequence of nucleotides in an existing DNA stand controls
the sequence in which nucleotides are joined together in a new DNA strand; T in one strand
pairs with A in the other, and G in one strand with C in the other. The new strand has a
nucleotide sequence complementary to that of the old strand, and a backbone with opposite
directionality: corresponding to the GTAA… of the original strand, it has …TTAC. (D) A
normal DNA molecule consists of two such complementary strands. The nucleotides within
each strand are linked by strong (covalent) chemical bonds; the complementary nucleotides
on opposite strands are held together more weakly, by hydrogen bonds. (E) The two strands
twist around each other to form a double helix—a robust structure that can accommodate any
sequence of nucleotides without altering its basic structure.

produced in the cell. Each nucleic acid is linked to a sugar molecule (deoxyglucose),
which is in turn connected to a phosphate molecule to form what is called a nucleo-
tide (Figure 1.2). The four different nucleotides are linked together by phosphodi-
ester bonds that form very long chains composed of millions of nucleotides that
make up DNA (Figure 1.3). As will be discussed shortly, the order of the nucleotide
sequences in the DNA chain specifies the amino acid sequence of the proteins for
which it codes. Two chains or strands of nucleotides make up DNA, each strand
forming a ribbonlike structure that winds around the other strand to form a double
helix (Figure 1.4). One strand of DNA is complementary to the other strand since
adenine in one strand is linked by hydrogen bonding to thymine in the other strand,

Copyright 2008 by Taylor and Francis Group, LLC

3967_C001.indd 7 10/24/07 10:48:53 AM

  Food Safety of Proteins in Agricultural Biotechnology

5´ end

–O P O
O
O N
NH
G
5´ CH2 O N N NH2
4´ 1´
3´ 2´
O
–
O P O NH2

O N N
A
CH2 O N N

O
–O O
P O
H3C NH
O T
CH2 O N O

O
–O P NH2
O

O N
C
5´ CH2 O N O

4´ 1´

3´ 2´
O

3´ end

Figure 1.3  A small part of one chain of a deoxyribonucleic acid (DNA) molecule. Four
nucleotides are shown. Nucleotides are linked together by a phosphodiester linkage between
specific carbon atoms of the ribose, known as the 5′ and 3′ atoms. For this reason, one end
of a polynucleotide chain, the 5′ end, will have a free phosphate group and the other, the 3′
end, a free hydroxyl group. The linear sequence of nucleotides in a polynucleotide chain is
commonly abbreviated by a one-letter code, and the sequence is always read from the 5′ end.
In the example illustrated the sequence is G–A–T–C.

Copyright 2008 by Taylor and Francis Group, LLC

3967_C001.indd 8 10/24/07 10:48:56 AM

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