INDUSTRIAL UNIVERSITY OF HO CHI MINH CITY

INSTITUTE OF BIOTECHNOLOGY AND FOOD TECHNOLOGY

Course: ADVANCED ENGLISH FOR BIOLOGY

Credits gain: 03
Study duration: 45 periods (5pds/session)
Requirements:
Class attendance is compulsory;
No chatting, and eating in class;
Discussion related to the study subject is allowed. Inter-group discussion and
teacher-student interactions are encouraged. Q&A are also recommended.
Assessment: Graded through:
Midterm test
Final exam
Group work
Individual performance
Course syllabus/Study plan:
Including 7 units.
Unit 1: Bacteria Are Simple Cells (done by teacher/5 periods)
Unit 2 Unit 7: done by students.
Class will be divided into 6 groups, each being in charge of 1 unit via
drawing lots.
Group members have to translate 1 unit into Vietnamese in front of class,
and also make a presentation (using PowerPoint) about the topic they have
drawn.
While the group in charge is translating, the other groups have to listen to
their translation and notice the improper parts. Teacher will ask anyone
about the presented topic, meaning that all groups are supposed to prepare
and translate the topic prior to its date of presentation.
Each unit will be studied in about 6-7 periods, including:
Translation by students
Correction by teacher (pronunciation, reading comprehension, translation,
related grammatical points, exercises, )
Presentation by students
Lexical games (designed by students)
Listening to biologically related topics (if it can be managed)
Lesson reinforcement

Email: huyentrang14200@yahoo.com
Website: https://sites.google.com/a/foodtech.edu.vn/huyentrang/
 UNIT 1
BACTERIA ARE SIMPLE CELLS
Prokaryotes, the bacteria, are the simplest organisms. Prokaryotic cells are small, consisting
of cytoplasm surrounded by a plasma membrane and encased within a rigid cell wall, with
no distinct interior compartments (figure 5.5). A prokaryotic cell is like a one room cabin in
which eating, sleeping, and watching TV all occur in the same room. Bacteria are very
important in the economy of living organisms. They harvest light in photosynthesis, break
down dead organisms and recycle their components, cause disease, and are involved in
many important industrial processes.

Strong Cell Walls

Most bacteria are encased by a strong cell wall composed of peptidoglycan, which consists
of a carbohydrate matrix (polymers of sugars) that is cross-linked by short polypeptide
units. No eukaryotes possess cell walls with this type of chemical composition. With a few
exceptions like TB and leprosy-causing bacteria, all bacteria may be classified into two
types based on differences in their cell walls detected by the Gram staining procedure. The
name refers to the Danish microbiologist Hans Christian Gram, who developed the
procedure to detect the presence of certain disease-causing bacteria. Gram-positive
bacteria have a thick, single-layered cell wall that retains a violet dye from the Gram stain
procedure, causing the stained cells to appear purple under a microscope. More complex
cell walls have evolved in other groups of bacteria.
In them, the wall is multilayered and does not retain the purple dye after Gram staining;
such bacteria exhibit the background red dye and are characterized as gram - negative.
The susceptibility of bacteria to antibiotics often depends on the structure of their cell
walls. Penicillin and vancomycin, for example, interfere with the ability of bacteria to cross-
link the peptide units that hold the carbohydrate chains of the wall together. Like removing
all the nails from a wooden house, this destroys the integrity of the matrix, which can no
longer prevent water from rushing in, swelling the cell to bursting.

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Cell walls protect the cell, maintain its shape, and prevent excessive uptake of water. Plants,
fungi, and most protists also have cell walls of a different chemical structure, which we will
discuss in later chapters. Long chains of sugars called polysaccharides cover the cell walls of
many bacteria. They enable a bacterium to adhere to teeth, skin, foodpractically any
surface that will support their growth. Many disease-causing bacteria secrete a jellylike
protective capsule of polysaccharide around the cell.
Rotating Flagella
Some bacteria use a flagellum (plural, flagella) to move. Flagella are long, threadlike
structures protruding from the surface of a cell that are used in locomotion and feeding.
Bacterial flagella are protein fibers that extend out from a bacterial cell. There may be one
or more per cell, or none, depending on the species. Bacteria can swim at speeds up to 20
cell diameters per second by rotating their flagella like screws. A motor unique to bacteria
that is embedded within their cell walls and membranes powers the rotation. Only a few
eukaryotic cells have structures that truly rotate.
Simple Interior Organization
If you were to look at an electron micrograph of a bacterial cell, you would be struck by the
cells simple organization. There are few, if any, internal compartments, and while they
contain simple structures like ribosomes, most have no membrane-bounded organelles, the
kinds so characteristic of eukaryotic cells. Nor do bacteria have a true nucleus. The entire
cytoplasm of a bacterial cell is one unit with no internal support structure. Consequently,
the strength of the cell comes primarily from its rigid wall (see figure 5.5).
The plasma membrane of a bacterial cell carries out some of the functions organelles
perform in eukaryotic cells. When a bacterial cell divides, for example, the bacterial
chromosome, a simple circle of DNA, replicates before the cell divides. The two DNA
molecules that result from the replication attach to the plasma membrane at different
points, ensuring that each daughter cell will contain one of the identical units of DNA.
Moreover, some photosynthetic bacteria, such as cyanobacteria and Prochloron, have an
extensively folded plasma membrane, with the folds extending into the cells interior. These
membrane folds contain the bacterial pigments connected with photosynthesis. Because a
bacterial cell contains no membrane-bounded organelles, the DNA, enzymes, and other
cytoplasmic constituents have access to all parts of the cell. Reactions are not
compartmentalized as they are in eukaryotic cells, and the whole bacterium operates as a
single unit.

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 UNIT 2 ENZYMES
The chemical reactions within living organisms are regulated by controlling the points at
which catalysis takes place. Life itself is, therefore, regulated by catalysts. The agents that
carry out most of the catalysis in living organisms are proteins called enzymes. (There is
increasing evidence that some types of biological catalysis are carried out by RNA
molecules.) The unique three-dimensional shape of an enzyme enables it to stabilize a
temporary association between substrates, the molecules that will undergo the reaction.
By bringing two substrates together in the correct orientation, or by stressing particular
chemical bonds of a substrate, an enzyme lowers the activation energy required for new
bonds to form. The reaction thus proceeds much more quickly than it would without the
enzyme. Because the enzyme itself is not changed or consumed in the reaction, only a small
amount of an enzyme is needed, and it can be used over and over. As an example of how an
enzyme works, lets consider the reaction of carbon dioxide and water to form carbonic
acid. This important enzyme-catalyzed reaction occurs in vertebrate red blood cells:
CO2 + H2O H2CO3
This reaction may proceed in either direction, but because it has a large activation energy,
the reaction is very slow in the absence of an enzyme: perhaps 200 molecules of carbonic
acid form in an hour in a cell. Reactions that proceed this slowly are of little use to a cell.
Cells overcome this problem by employing an enzyme within their cytoplasm called
carbonic anhydrase (enzyme names usually end in ase). Under the same conditions, but
in the presence of carbonic anhydrase, an estimated 600,000 molecules of carbonic acid
form every second! Thus, the enzyme increases the reaction rate more than 10 million
times. Thousands of different kinds of enzymes are known, each catalyzing one or a few
specific chemical reactions. By facilitating particular chemical reactions, the enzymes in a
cell determine the course of metabolismthe collection of all chemical reactionsin that
cell. Different types of cells contain different sets of enzymes, and this difference
contributes to structural and functional variations among cell types. The chemical reactions
taking place within a red blood cell differ from those that occur within a nerve cell, in part
because the cytoplasm and membranes of red blood cells and nerve cells contain different
arrays of enzymes.

FIGURE 1: How the enzyme lysozyme works. (a) A groove runs through lysozyme that fits the shape of the
polysaccharide (a chain of sugars) that makes up bacterial cell walls. (b) When such a chain of sugars, indicated in yellow,
slides into the groove, its entry induces the protein to alter its shape slightly and embrace the substrate more intimately.
This induced fit positions a glutamic acid residue in the protein next to the bond between two adjacent sugars, and the
glutamic acid steals an electron from the bond, causing it to break.

How Enzymes Work

Most enzymes are globular proteins with one or more pockets or clefts on their surface
called active sites (figure 1). Substrates bind to the enzyme at these active sites, forming an
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enzyme-substrate complex. For catalysis to occur within the complex, a substrate
molecule must fit precisely into an active site. When that happens, amino acid side groups
of the enzyme end up in close proximity to certain bonds of the substrate. These side
groups interact chemically with the substrate, usually stressing or distorting a particular
bond and consequently lowering the activation energy needed to break the bond. The
substrate, now a product, then dissociates from the enzyme. Proteins are not rigid. The
binding of a substrate induces the enzyme to adjust its shape slightly, leading to a better
induced fit between enzyme and substrate (figure 2). This interaction may also facilitate the
binding of other substrates; in such cases, the substrate itself activates the enzyme to
receive other substrates.

FIGURE 2: The catalytic cycle of an enzyme. Enzymes increase the speed with which chemical reactions occur, but they
are not altered themselves as they do so. In the reaction illustrated here, the enzyme sucrase is splitting the sugar sucrose
(present in most candy) into two simpler sugars: glucose and fructose. (1) First, the sucrose substrate binds to the active
site of the enzyme, fitting into a depression in the enzyme surface. (2) The binding of sucrose to the active site forms an
enzyme-substrate complex and induces the sucrose molecule to alter its shape, fitting more tightly around the sucrose. (3)
Amino acid residues in the active site, now in close proximity to the bond between the glucose and fructose components of
sucrose, break the bond. (4) The enzyme releases the resulting glucose and fructose fragments, the products of the
reaction, and is then ready to bind another molecule of sucrose and run through the catalytic cycle once again. This cycle is
often summarized by the equation: E + S [ES] E + P, where E = enzyme, S = substrate, ES = enzyme-substrate complex,
and P = products.

Factors Affecting Enzyme Activity

Temperature
Increasing the temperature of an uncatalyzed reaction will increase its rate because the
additional heat represents an increase in random molecular movement. The rate of an
enzyme-catalyzed reaction also increases with temperature, but only up to a point called
the temperature optimum. Below this temperature, the hydrogen bonds and hydrophobic
interactions that determine the enzymes shape are not flexible enough to permit the
induced fit that is optimum for catalysis. Above the temperature optimum, these forces are
too weak to maintain the enzymes shape against the increased random movement of the
atoms in the enzyme. At these higher temperatures, the enzyme denatures.
pH
Ionic interactions between oppositely charged amino acid residues, such as glutamic acid (-
) and lysine (+), also hold enzymes together. These interactions are sensitive to the
hydrogen ion concentration of the fluid the enzyme is dissolved in, because changing that
concentration shifts the balance between positively and negatively charged amino acid

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residues. For this reason, most enzymes have a pH optimum that usually ranges from pH 6
to 8.
Inhibitors and Activators
Enzyme activity is sensitive to the presence of specific substances that bind to the enzyme
and cause changes in its shape. Through these substances, a cell is able to regulate which
enzymes are active and which are inactive at a particular time. This allows the cell to
increase its efficiency and to control changes in its characteristics during development. A
substance that binds to an enzyme and decreases its activity is called an inhibitor. Very
often, the end product of a biochemical pathway acts as an inhibitor of an early reaction in
the pathway, a process called feedback inhibition (to be discussed later).
Enzyme inhibition occurs in two ways: competitive inhibitors compete with the substrate
for the same binding site, displacing a percentage of substrate molecules from the enzymes;
noncompetitive inhibitors bind to the enzyme in a location other than the active site,
changing the shape of the enzyme and making it unable to bind to the substrate.
Enzyme Cofactors
Enzyme function is often assisted by additional chemical components known as cofactors.
For example, the active sites of many enzymes contain metal ions that help draw electrons
away from substrate molecules. The enzyme carboxypeptidase digests proteins by
employing a zinc ion (Zn++) in its active site to remove electrons from the bonds joining
amino acids. Other elements, such as molybdenum and manganese, are also used as
cofactors. Like zinc, these substances are required in the diet in small amounts. When the
cofactor is a nonprotein organic molecule, it is called a coenzyme. Many vitamins are parts
of coenzymes.

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 UNIT 3
THE EVOLUTION OF METABOLISM
Metabolism has changed a great deal as life on earth has evolved. This has been particularly
true of the reactions organisms use to capture energy from the sun to build organic
molecules (anabolism), and then break down organic molecules to obtain energy
(catabolism). These processes, the subject of the next two chapters, evolved in concert with
each other.
Degradation
The most primitive forms of life are thought to have obtained chemical energy by
degrading, or breaking down, organic molecules that were abiotically produced. The first
major event in the evolution of metabolism was the origin of the ability to harness chemical
bond energy. At an early stage, organisms began to store this energy in the bonds of ATP, an
energy carrier used by all organisms today.
Glycolysis
The second major event in the evolution of metabolism was glycolysis, the initial
breakdown of glucose. As proteins evolved diverse catalytic functions, it became possible to
capture a larger fraction of the chemical bond energy in organic molecules by breaking
chemical bonds in a series of steps. For example, the progressive breakdown of the six
carbon sugar glucose into three-carbon molecules is performed in a series of 10 steps that
results in the net production of two ATP molecules. The energy for the synthesis of ATP is
obtained by breaking chemical bonds and forming new ones with less bond energy, the
energy difference being channeled into ATP production. This biochemical pathway is called
glycolysis. Glycolysis undoubtedly evolved early in the history of life on earth, since this
biochemical pathway has been retained by all living organisms. It is a chemical process that
does not appear to have changed for well over 3 billion years.
Anaerobic Photosynthesis
The third major event in the evolution of metabolism was anaerobic photosynthesis. Early
in the history of life, some organisms evolved a different way of generating ATP, called
photosynthesis. Instead of obtaining energy for ATP synthesis by reshuffling chemical
bonds, as in glycolysis, these organisms developed the ability to use light to pump protons
out of their cells, and to use the resulting proton gradient to power the production of ATP, a
process called chemiosmosis. Photosynthesis evolved in the absence of oxygen and works
well without it. Dissolved H2S, present in the oceans beneath an atmosphere free of oxygen
gas, served as a ready source of hydrogen atoms for building organic molecules. Free sulfur
was produced as a by-product of this reaction.
Nitrogen Fixation
Nitrogen fixation was the fourth major step in the evolution of metabolism. Proteins and
nucleic acids cannot be synthesized from the products of photosynthesis because both of
these biologically critical molecules contain nitrogen. Obtaining nitrogen atoms from N2 gas,
a process called nitrogen fixation, requires the breaking of an NN triple bond. This
important reaction evolved in the hydrogen-rich atmosphere of the early earth, an
atmosphere in which no oxygen was present. Oxygen acts as a poison to nitrogen fixation,
which today occurs only in oxygen-free environments, or in oxygen-free compartments
within certain bacteria.

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Oxygen-Forming Photosynthesis
The substitution of H2O for H2S in photosynthesis was the fifth major event in the history of
metabolism. Oxygen forming photosynthesis employs H2O rather than H2S as a source of
hydrogen atoms and their associated electrons. Because it garners its hydrogen atoms from
reduced oxygen rather than from reduced sulfur, it generates oxygen gas rather than free
sulfur.
More than 2 billion years ago, small cells capable of carrying out this oxygen-forming
photosynthesis, such as cyanobacteria, became the dominant forms of life on earth. Oxygen
gas began to accumulate in the atmosphere. This was the beginning of a great transition
that changed conditions on earth permanently. Our atmosphere is now 20.9% oxygen,
every molecule of which is derived from an oxygen-forming photosynthetic reaction.
Aerobic Respiration
Aerobic respiration is the sixth and final event in the history of metabolism. This cellular
process harvests energy by stripping energetic electrons from organic molecules. Aerobic
respiration employs the same kind of proton pumps as photosynthesis, and is thought to
have evolved as a modification of the basic photosynthetic machinery. However, the
hydrogens and their associated electrons are not obtained from H2S or H2O, as in
photosynthesis, but rather from the breakdown of organic molecules. Biologists think that
the ability to carry out photosynthesis without H2S first evolved among purple nonsulfur
bacteria, which obtain their hydrogens from organic compounds instead. It was perhaps
inevitable that among the descendants of these respiring photosynthetic bacteria, some
would eventually do without photosynthesis entirely, subsisting only on the energy and
hydrogens derived from the breakdown of organic molecules. The mitochondria within all
eukaryotic cells are thought to be their descendants.

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 UNIT 4
THE DIVERSITY OF LIFE CAN BE ARRANGED
INTO THREE DOMAINS
Rain forests abound with the sights, sounds, and scents of living things. Ants, mosquitoes,
beetles, and other insects are literally everywhere flying, crawling, jumping and you
hear them day and night. In a tropical rain forest, the sweet fragrance of showy orchids
often hangs in the air, and the loud calls of parrots, toucans, and other colorful birds
compete with the hoots and howls of monkeys.
The richness of life in a rain forest the vast diversity of species can be almost
overwhelming. To make diversity somewhat more comprehensible, scientists have devised
ways of grouping (classifying) organisms. Today, biologists generally favor classification
schemes with at least eight kingdoms, which are themselves classified into three higher
groups called domains.
The organisms representing the three domains could all be found in one small area of a
tropical rain forest. The microscopic organisms are called prokaryotes. Found literally
everywhere there is life, from rain forests and polar oceans to your own skin and intestines,
prokaryotes are the most widespread of all living organisms. Prokaryotes are distinguished
from all other forms of life by their structure. Every living being is composed of cells, but
only prokaryotes have cells without a nucleus, a discrete internal structure that controls
cellular activities. There are two very different groups of prokaryotes, which make up two
of the three domains: Bacteria and Archaea. All organisms except prokaryotes are members
of a third domain, the Eukarya, organisms made of cells with a nucleus and discrete internal
structures called organelles.
Most pools of water containing prokaryotes would also support members of Domain
Eukarya commonly called protists. One group of protists, commonly called algae, make
their own food molecules by the process of photosynthesis. Another group, commonly
called protozoan, are single celled and are animal like in that they eat other organisms,
including algae and prokaryotes.
The large, irregular, bluish cell is an amoeba (a protozoan) and the smaller cells are mostly
single-celled algae. Also present are considered algae (the long rodlike filaments), protists
because of their similarities to single-celled algae. Until recently, protists were classified in
a single kingdom, but evidence from molecular studies now indicates that they are more
diverse than any other group of eukaryotes. As we will see when we study them in more
detail, protists comprise several kingdoms within the domain Eukarya.
Organisms in the remaining three groups (kingdoms) of the Eukarya are all multicellular.
Kimdom Plantae, the plants, are photosynthetic and consist of cells with strong walls made
of cellulose. Kingdom Fungi is a diverse group that includes the molds, yeasts, and
mushrooms. Fungi decompose the remains of dead organisms and absorb nutrients from
the leftovers.
Representing the kingdom Animalia (animals), the sloth resides in tropical rain forest
canopies. Animals eat other organisms and are made of cells that lack rigid walls. Most
animals are motile. The sloth is a slow moving animal that spends most of its time hanging
upside down eating leaves.

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There are actually members of three major groups. The sloth is clinging to one of the tall
trees (kingdom Plantae) dominating the rain forest. And the greenish tinge in the animals
hair is a luxuriant growth of photosynthetic prokaryotes (Domain Bacteria). The sloth
depends on trees for food and shelter, the prokaryotes gain access to the sunlight necessary
for photosynthesis by living on the sloth, and the tree uses some chemical nutrients
supplied mainly by prokaryotes.
Lifes diversity and its interconnectedness are evident almost everywhere. You can find
representatives of the major group on many city streets. There the most obvious examples
of Animalia are likely to be people, with trees, shrubs, and grass representing Plantae. With
the help of a microscope, you can find prokaryotes, fungi and protists in any puddle of
water or patch of most soil. Less obvious, but just as significant, are signs of the basic
similarities shared by all organisms. Lifes great paradox is the unity in its diversity the
fact that the million of species of organisms are all variations on a relatively small set of
basic features.
LIFES LEVELS OF ORGANIZATION DEFINE THE SCOPE OF BIOLOGY
A forest researcher mentions the dialogue between trees and the atmosphere. What does
this mean? The word dialogue refers to interactions between living organisms and
nonliving matters the gases in the atmosphere. Such interactions are a fundamental
property of ecosystems, the highest of several structural levels into which life is organized.
An ecosystem (for example, a rain forest) consists of all the organisms living in a particular
area, as well as all the nonliving, physical components of the environment that affect the
organisms, such as air, soil, and sunlight. The ecosystem and the structural levels below its
form a hierarchy, with each level building on the ones below it. Below the ecosystem level,
all the organisms in a rain forest are collectively called a community. Below the community,
an interacting group of individuals of one species, flying squirrels in our example, is called a
population. Below population in the hierarchy is the organism, an individual living thing.
Below the organism level, lifes hierarchy unfolds within the individual organism. The flying
squirrelss body consists of several organ systems, such as a circulatory excretory system,
and a nervous system, shown here. Each organ system consists of organs. For instance, the
main organs of the nervous system are the brain, the spinal cord, and the nerves, which
transmit messages between the spinal cord and other parts of the body.
As we continue downward through the hierarchy, each organ is made up of several
different tissues, each of which consists of a group of similar cells. A cell is a unit of living
matter separated from its environment by a boundary called a membrane. Each tissue has a
specific function, which is performed by the cells that compose it. The nervous tissue that
makes up most of the brain, for example, consists of nerve cells. The nervous tissue in the
squirrelss brain has millions of microscopic nerve cells organized into a communication
network of spectacular complexity. The nerve cells transmit signals that coordinate the
squirrels body parts, such as the muscles that stretch out its legs during a glide.
Finally, we reach the molecular level in the hierarchy. We show as our example DNA
(deoxyribonucleic acid). DNA molecules provide the blueprints for constructing the
organisms other important molecules and transmit this information, as genes, from
parents to offspring. A molecule is a cluster of atoms, the smallest particles of ordinary
matter. Each of the spheres represents an atom. Each DNA molecule is a very long double
helix, two chains coiled around each other.
As we discuss lifes hierarchy builds from molecules to ecosystems. It takes many
molecules to make a cell, many cells to make a tissue, several skins of tissues to make an
organ, and so on. Most biologists specialize in the study of life at a particular level. For
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instance, a researcher analyzing the body postures of a gliding squirrel focuses on the
organism level. However, understanding gliding posture may require studying, at the organ
system level the interaction between muscles and bones, so the same researcher often
works at more than one level. The full spectrum of lifes hierarchy, from molecules to
ecosystems, encompasses the scope of biology. With this in mind, lets see how biological
scientists go about their work. Although we focus on examples of outdoor research in
forest ecosystems, the same scientific approach is used in all types of biological research.

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 UNIT 5
GENETICALLY MODIFIED CROPS

Ethics and Regulation

The advantages afforded by genetic engineering are revolutionizing our lives. But what are
the disadvantages, the potential costs and dangers of genetic engineering? Many people,
including influential activists and members of the scientific community, have expressed
concern that genetic engineers are playing God by tampering with genetic material. For
instance, what would happen if one fragmented the DNA of a cancer cell, and then
incorporated the fragments at random into vectors that were propagated within bacterial
cells? Might there not be a danger that some of the resulting bacteria would transmit an
infective form of cancer? Could genetically engineered products administered to plants or
animals turn out to be dangerous for consumers after several generations? What kind of
unforeseen impact on the ecosystem might improved crops have? Is it ethical to create
genetically superior organisms, including humans?
How Do We Measure the Potential Risks of Genetically Modified Crops?
While the promise of genetic engineering is very much in evidence, this same genetic
engineering has this summer been the cause of outright war between researchers and
protesters in England. In June 1999, British protesters attacked an experimental plot of
genetically modified (GM) sugar beets; the following August they destroyed a test field of
GM canola (used for cooking oil and animal feed). The contrast could not be more marked
between American acceptance of genetically modified crops on the one hand, and European
distrust of genetically modified foods, on the other. The intense feelings generated by this
dispute point to the need to understand how we measure the risks associated with the
genetic engineering of plants. Two sets of risks need to be considered. The first stems from
eating genetically modified foods, the other concerns potential ecological effects.
Is Eating Genetically Modified Food Dangerous?
Protesters worry that genetically modified food may have been rendered somehow
dangerous. To sort this out, it is useful to bear in mind that bioengineers modify crops in
two quite different ways. One class of gene modification makes the crop easier to grow; a
second class of modification is intended to improve the food itself. The introduction of
Roundup-resistant soybeans to Europe is an example of the first class of modification. This
modification has been very popular with farmers in the United States, who planted half
their crop with these soybeans in 1999. They like GM soybeans because the beans can be
raised without intense cultivation (weeds are killed with Roundup herbicide instead),
which both saves money and lessens soil erosion. But is the soybean that results
nutritionally different? No. The gene that confers Roundup resistance in soybeans does so
by protecting the plant's ability to manufacture so-called "aromatic" amino acids. In
unprotected weeds, by contrast, Roundup blocks this manufacturing process, killing the
weed. Because humans don't make any aromatic amino acids anyway (we get them in our
diets), Roundup doesn't hurt us. The GM soybean we eat is nutritionally the same as an
"organic" one, just cheaper to produce.
In the second class of modification, where a gene is added to improve the nutritional
character of some food, the food will be nutritionally different. In each of these instances, it
is necessary to examine the possibility that consumers may prove allergic to the product of
the introduced gene. In one instance, for example, addition of a methionine-enhancing gene
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from Brazil nut into soybeans (which are deficient in this amino acid) was discontinued
when six of eight individuals allergic to Brazil nuts produced antibodies to the GM
soybeans, suggesting the possibility of a reverse reaction. Instead, methionine levels in GM
crops are being increased with genes from sunflowers. Screening for allergy problems is
now routine. On both scores, then, the risk of bioengineering to the food supply seems to be
very slight. GM foods to date seem completely safe.
Are GM Crops Harmful to the Environment?
What are we to make of the much-publicized report that Monarch butterflies might be
killed by eating pollen blowing out of fields planted with GM corn? First, it should come as
no surprise. The GM corn (so-called Bt corn) was engineered to contain an insect-killing
toxin (harmless to people) in order to combat corn borer pests. Of course it will kill any
butterflies or other insects in the immediate vicinity of the field. However, focus on the fact
that the GM corn fields do not need to be sprayed with pesticide to control the corn borer.
An estimated $9 billion in damage is caused annually by the application of pesticides in the
United States, and billions of insects and other animals, including an estimated 67 million
birds, are killed each year. This pesticide-induced murder of wildlife is far more damaging
ecologically than any possible effects of GM crops on butterflies.
Will pests become resistant to the GM toxin? Not nearly as fast as they now become
resistant to the far higher levels of chemical pesticide we spray on crops. How about the
possibility that introduced genes will pass from GM crops to their wild or weedy relatives?
This sort of gene flow happens naturally all the time, and so this is a legitimate question.
But so what if genes for resistance to Roundup herbicide spread from cultivated sugar beets
to wild populations of sugar beets in Europe? Why would that be a problem? Besides, there
is almost never a potential relative around to receive the modified gene from the GM crop.
There are no wild relatives of soybeans in Europe, for example. Thus, there can be no gene
escape from GM soybeans in Europe, any more than genes can flow from you to other kinds
of animals. On either score, then, the risk of bioengineering to the environment seems to be
very slight. Indeed, in some cases it lessens the serious environmental damage produced by
cultivation and agricultural pesticides.
Should We Label Genetically Modified Foods?
While there seems little tangible risk in the genetic modification of crops, public assurance
that these risks are being carefully assessed is important. Few issues manage to raise the
temperature of discussions about plant genetic engineering more than labeling of
genetically modified (GM) crops. Agricultural producers have argued that there are no
demonstrable risks, so that a GM label can only have the function of scaring off wary
consumers. Consumer advocates respond that consumers have every right to make that
decision, and to the information necessary to make it.
In considering this matter, it is important to separate two quite different issues, the need
for a label, and the right of the public to have one. Every serious scientific investigation of
the risks of GM foods has concluded that they are safeindeed, in the case of soybeans and
many other crops modified to improve cultivation, the foods themselves are not altered in
any detectable way, and no nutritional test could distinguish them from "organic" varieties.
So there seems to be little if any health need for a GM label for genetically engineered foods.
The right of the public to know what it is eating is a very different issue. There is
widespread fear of genetic manipulation in Europe, because it is unfamiliar. People there
don't trust their regulatory agencies as we do here, because their agencies have a poor track
record of protecting them. When they look at genetically modified foods, they are haunted
by past experiences of regulatory ineptitude. In England they remember British regulators'
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failure to protect consumers from meat infected with mad cow disease. It does no good
whatsoever to tell a fearful European that there is no evidence to warrant fear, no trace of
data supporting danger from GM crops. A European consumer will simply respond that the
harm is not yet evident, that we don't know enough to see the danger lurking around the
corner. "Slow down," the European consumers say.
"Give research a chance to look around all the corners. Lets be sure." No one can argue
against caution, but it is difficult to imagine what else researchers can look into safety
has been explored very thoroughly. The fear remains, though, for the simple reason that no
amount of information can remove it. Like a child scared of a monster under the bed,
looking under the bed again doesn't help the monster still might be there next time. And
that means we are going to have GM labels, for people have every right to be informed
about something they fear. What should these labels be like? A label that only says "GM
FOOD" simply acts as a brand like a POISON label, it shouts a warning to the public of
lurking danger. Why not instead have a GM label that provides information to the
consumer, that tells the consumer what regulators know about that product? (For Bt corn):
The production of this food was made more efficient by the addition of genes that made
plants resistant to pests so that less pesticides were required to grow the crop. (For
Roundup-ready soybeans): Genes have been added to this crop to render it resistant to
herbicidesthis reduces soil erosion by lessening the need for weed removing cultivation.
(For high beta-carotene rice): Genes have been added to this food to enhance its beta-
carotene content and so combat vitamin A deficiency. GM food labels that in each instance
actually tell consumers what has been done to the gene-modified crop would go a long way
toward hastening public acceptance of gene technology in the kitchen.

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 UNIT 6
MICROBIAL CELLULOSE
The Significant Biomedical Potential of Microbial Cellulose Stems from Its
Unique Structure and Properties
Cellulose synthesis by Acetobacter is a complex process and involves (A) the
polymerization of single glucose residues into linear -1,4-glucan chains, (B) the
extracellullar secretion of these linear chains, and (C) the assembly and crystallization of
the glucan chains into hierarchically composed ribbons. As a result of these processes, a
three-dimensional, gelatinous structure is formed on the surface of a liquid medium. The
physical and mechanical properties of microbial cellulose (MC) membranes arise from
their unique structure, which differs significantly from the structure of plant cellulose.
Basically, well-separated nano- and microfibrils of microbial cellulose create an extensive
surface area which allows it to hold a large amount of water while maintaining a high
degree of conformability. The hydrogen bonds between these fibrillar units stabilize the
whole structure and give it a great deal of mechanical strength. Even though plant cellulose
is composed of microfibrils which are similar to those found within microbial cellulose, the
plant cellulose microfibrils are part of a larger aggregation of the cell wall. Thus, microbial
cellulose can absorb much higher volumes of liquids than plant-derived cellulose materials.
On the basis of its recent clinical performance and according to the results of other
research on the properties of this particular biomaterial, MC can be considered an ideal
material for high-quality wound dressings. Interestingly, many Acetobacter strains display
significant differences in the cellulose production process (i.e., the rate of cellulose ribbon
extrusion from a single cell may significantly vary between strains), as well as in the
structure of the synthesized polymer. Figure 1 presents SEM images of cellulose structures
synthesized by two different strains of Acetobacter. The differences in the size of the
cellulose ribbons can be clearly seen. From a bioengineering point of view, these structural
differences are of great importance since they can be used to create hybrid materials with
desired properties consisting of cellulose products synthesized by different Acetobacter
strains.
The given medical application should dictate the choice of the particular cellulose structure
(specific Acetobacter strain). For example, implantable cellulose for artificial skin should
ideally display high porosity, with interconnected pores of 50- 150 m, in order to facilitate
skin cell integration into the cellulose scaffold, whereas temporary wound dressings should
have a nanoporous structure and should keep the wound moist during the healing process.

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One of the main requirements of any biomedical material is that it must be biocompatible,
which is the ability to remain in contact with living tissue without causing any toxic or
allergic side effects. A material composed of porous plant cellulose has been shown to be
biocompatible with bone tissue and hepatocytes. Research conducted on an implanted
cellulose sponge showed that it can be regarded as a slowly degradable material. As
mentioned by the same authors, this material can be considered nondegradable if used as a
temporary wound coverage for a short period of time. Unlike plant-originated cellulose,
microbial cellulose is free of lignin and hemicelluloses. However, microbial cellulose is
treated with strong bases in order to completely remove bacterial cells embedded in the
polymer net. There are several in vivo biocompatibility studies that used MC on animal
models. For example, Kolodziejczyk and Pomorski implanted pieces of microbial cellulose
(1 cm in diameter) into subcutaneous pockets on rabbits and periodically examined them
after 1 and 3 weeks. The implants did not cause any macroscopic inflammatory responses,
and histological observations showed only a small number of giant cells and a thin layer of
fibroblasts at the interface between the cellulose and the tissue. Positive results were also
obtained by Oster et al. in an in vitro study using mouse fibroblasts cells. A specific in vivo
biocompatibility study of microbial cellulose has also been conducted by Klemm et al., who
implanted cellulose in the form of a hollow tube as an interposition segment of the carotid
arteries of rats. In a recent, very systematic study by Helenius et al., pieces of microbial
cellulose were implanted into rats. Those implants evaluated after 1, 4, and 12 weeks
showed no macroscopic or histologic signs of inflammation and no presence of giant cells.
Also, according to the authors, no chronic inflammatory responses were observed
throughout the course of the studies. Instead, they observed the formation of new blood
vessels around and inside the implanted cellulose. Interestingly, the authors also noticed
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that cells, mostly fibroblasts, were able to significantly penetrate the more porous bottom
side of a microbial cellulose membrane. The newly formed tissue, integrated with MC,
contained fibroblasts and newly synthesized collagen.
Microbial Cellulose as a Wound-Healing System: Temporary Wound Coverage
Wound healing is a dynamic process that involves the complex interaction of various cell
types, extracellular matrix (ECM) molecules, and soluble compounds. Typically, normal
wound healing progresses through a series of processes including homeostasis,
inflammation, granulation tissue formation, and remodeling. Chronic wounds, such as
ulcers, do not heal because one or more of these processes fail to function properly. Thus,
successful wound treatments improve the tissue repair process by counteracting the
inherent abnormalities of the chronic wound. Once the barriers to normal tissue repair are
removed, the healing process can begin, which involves autolytic debridement, granulation
tissue formation, and re epithelization.
In order to eliminate the hostile environment within the chronic wound and to facilitate
proper healing, wound dressings of various types have been developed and administered.
For example, ulcers are typically treated with dressings such as hydrogels, hydrocolloids,
synthetic and biological membranes, and alginate. In 1962, George Winter discovered that
healing, and specifically re-epithialization, was accelerated if the wound was kept moist.
Since then, almost all effective wound dressings are designed to maintain a moist
environment within the affected region. In fact, proteolytic activity may be elevated in a
moist environment, resulting in the stimulation and accumulation of growth factors. Moist
dressings are permeable to water, and this property has advantages for wound healing. For
example, high water vapor permeable dressings show enhanced healing, probably due to
an increased concentration of growth-promoting factors within the exudate and to the
creation of a more extensive ECM of fibrin(ogen) and fibronectin.
Burns are very complex injuries, causing extensive damage to skin tissues. The healing
process involves the regeneration of the epidermis and the repair of the dermis, both of
which result in the formation of scar tissue. One of the major goals of burn therapy is to
quickly accomplish effective wound closure so as to increase the rate of healing and to
provide immediate pain relief. In addition, proper wound management must prohibit the
wound from becoming infected and dehydrated. Despite the fact that many different
biological and synthetic wound dressings have already been developed, the search for an
ideal wound dressing is still in progress. According to the modern approaches in the field of
wound healing, an ideal wound dressing system must be structurally and functionally
similar to autograft skin.

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 UNIT 7
DNA VACCINES
Traditional vaccines consist of either live organisms with attenuated virulence, killed
organisms, or inactivated toxins. Usually, only minor genetic alterations distinguish virulent
organisms from the attenuated vaccine strains, which therefore have the potential to revert
to the virulent state. With killed or inactivated vaccines, there is always a danger that their
inactivation might have been incomplete. Furthermore, they often produce undesirable side
effects because they are likely to contain extraneous toxic components that are not needed
to produce the protective immunity. These and other shortcomings of traditional vaccines
can be avoided by the use of subunit vaccines, which contain only the immunity-conferring
protective antigen, most often a single protein component of the pathogenic organism.
Such an antigen may be produced from the pathogens by the traditional technology, as with
a cellular pertussis vaccine and conjugate polysaccharide vaccines of H. influenzae and
pneumococci. It may also be produced safely and inexpensively by introducing, into
harmless organisms such as E. coli or yeast, recombinant DNA molecules containing the
appropriate gene. Recombinant hepatitis B vaccine, composed of the major capsid protein
of the virus, is a successful commercial product of the latter class and is now used widely.
The subunit vaccines, however, are not always as effective as the traditional vaccines
because the vertebrate immune system is optimized to recognize features of the whole
pathogen, such as the presence of multiple copies of the same antigen on its surface and the
presence of certain components, such as LPS or peptidoglycan, that occur commonly in
foreign, invading microorganisms but not in host cells. Therefore, to obtain a better
immune response with a subunit vaccine may require an administration strategy that
causes the vaccine to mimic the appearance of antigen in the whole pathogen or that
combines the vaccine with chemicals that act as adjuvants. One of the subunit vaccines is
DNA vaccines. These are plasmids that contain the gene for the protective antigen behind a
promoter able to drive an efficient expression in vertebrate cells. Although DNA vaccines
were shown to be effective in mice, human trials have rarely produced significant
protection, presumably because in humans, it is difficult to achieve the dosage level that is
needed for strong immunity.
In a 1990 experiment, the injection of 100 g of naked plasmid DNA into mice resulted in
the detectable expression of foreign genes cloned downstream from a strong promoter
active in animal cells. This research, which suggested much potential for gene therapy, was
followed in a few years by reports that similar injection of plasmid DNA including genes
coding for antigens led to the production of immunity in mice. Because DNA vaccines are
easy to modify in the laboratory, these findings seemed to promise that even small
laboratories and small companies could produce effective new vaccines. Most steps
necessary for the production of recombinant protein vaccines, such as ensuring the good
expression and correct folding of the protein, protein purification, and removal of the
potentially toxic contaminants, would not be necessary with DNA vaccines, because the
antigen gene could be expressed within the APCs. Furthermore, the expression of the
antigenic protein within the cytoplasm of APCs meant that the immune response would be
tilted toward the production of cytotoxic CD8 T cells, a result that is difficult to achieve with
conventional vaccines. Since then, an enormous amount of research has gone into the
development of DNA vaccines that are effective in humans. Limited success has been
achieved, indicated by increases in antibody titer or T cell proliferation, but the general
consensus seems to be that DNA vaccines are usually not potent enough for use in humans.
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Current efforts are focused on increasing the potency by improving the method of
introduction of DNA (electroporation, use of adjuvants, etc.) and by combining the initial
administration of DNA vaccine with subsequent booster shots containing recombinant
viral. Even when followed by such boosters, however, the antimalarial DNA vaccine was
found to have no effect in the recent clinical trial.
Why were DNA vaccines so effective in mice but so disappointing in humans? A major
reason appears to be the dosage. The initial 1990 gene expression study in mice used 100
g/mouse and showed that the expression level of the foreign gene goes down tenfold if
only 10gDNAis injected. Thus 100 g DNA/mouse appears to be the minimum dosage
required, and subsequent DNA vaccine studies in mice all used that amount or even more
per animal. On the basis of human body weight, which is nearly 10,000-fold higher than
that of a laboratory mouse, this dosage would translate roughly into 1 g DNA/person. It is
impossible to inject this much DNA into humans, and besides, manufacturing such a large
amount would be quite expensive. Thus human trials have so far used between 1 and 3 mg
DNA/person, a dosage that is obviously far from adequate. Novel approaches seem
necessary if effective DNA vaccines are ever to be available for human use. In addition to
the issue of dosage, there is a very low yet theoretically possible chance that the foreign
plasmid DNA may become incorporated into the human chromosome. Experiments using
cultured animal cells showed that such an outcome should be extremely rare. Nevertheless,
any successful vaccine will be administered to millions, even billions, of people, and thus
even the unlikely adverse effects must be taken seriously.

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