Unit-1

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Biological Molecules-The molecules of Life

The large molecules necessary for life that are built from smaller organic molecules are called
biological macromolecules. There are four major classes of biological macromolecules
(carbohydrates, lipids, proteins, and nucleic acids), and each is an important component of the
cell and performs a wide array of functions. Combined, these molecules make up the majority
of a cell’s mass. Biological macromolecules are organic, meaning that they contain carbon. In
addition, they may contain hydrogen, oxygen, nitrogen, phosphorus, sulfur, and additional
minor elements.

Carbon

It is often said that life is “carbon-based.” This means that carbon atoms, bonded to other
carbon atoms or other elements, form the fundamental components of many, if not most, of the
molecules found uniquely in living things. Other elements play important roles in biological
molecules, but carbon certainly qualifies as the “foundation” element for molecules in living
things. It is the bonding properties of carbon atoms that are responsible for its important role.

Carbon Bonding

Carbon contains four electrons in its outer shell. Therefore, it can form four covalent bonds
with other atoms or molecules. The simplest organic carbon molecule is methane (CH4), in
which four hydrogen atoms bind to a carbon atom.

Fig. 1.1: Carbon can form four covalent bonds to create an organic molecule. The simplest carbon molecule
is methane (CH4).

However, structures that are more complex are made using carbon. Any of the hydrogen atoms
can be replaced with another carbon atom covalently bonded to the first carbon atom. In this
way, long and branching chains of carbon compounds can be made (Figure 1.2a). The carbon

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atoms may bond with atoms of other elements, such as nitrogen, oxygen, and phosphorus
(Figure 1.2b). The molecules may also form rings, which themselves can link with other rings
(Figure 1.2c). This diversity of molecular forms accounts for the diversity of functions of the
biological macromolecules and is based to a large degree on the ability of carbon to form
multiple bonds with itself and other atoms.

Fig.1.2: These examples show three molecules (found in living organisms) that contain carbon atoms
bonded in various ways to other carbon atoms and the atoms of other elements. (a) This molecule of stearic
acid has a long chain of carbon atoms. (b) Glycine, a component of proteins, contains carbon, nitrogen, oxygen,
and hydrogen atoms. (c) Glucose, a sugar, has a ring of carbon atoms and one oxygen atom.

Biological molecules are polymers, constructed from the covalent binding of smaller
molecules called monomers

Carbohydrates As Provision of Energy

Carbohydrates include both sugars and polymers of sugars.The simplest carbohydrates are the
monosaccharides, or simple sugars; these are the monomers from which more complex
carbohydrates are constructed. Disaccharides are double sugars, consisting of two
monosaccharides joined by a covalent bond. Carbohydrates also include macromolecules
called polysaccharides, polymers composed of many sugar building blocks.

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Sugars

Monosaccharides (from the Greek monos, single, and sacchar, sugar) generally have molecular
formulas that are some multiple of the unit CH2O. Glucose (C6H12O6), the most common
monosaccharide, is of central importance in the chemistry of life.

In the structure of glucose, we can see the

trademarks of a sugar: The molecule has a
carbonyl group (CO) and multiple hydroxyl
groups (—OH) (Figure 1.3). Depending on the
location of the carbonyl group, a sugar is either
an aldose (aldehyde sugar) or a ketose (ketone
sugar). Glucose, for example, is an aldose;
fructose, an isomer of glucose, is a ketose.
(Most names for sugars end in -ose.) Another
criterion for classifying sugars is the size of the
carbon skeleton, which ranges from three to
seven carbons long. Glucose, fructose, and
other sugars that have six carbons are called
hexoses. Trioses (three-carbon sugars) and
pentoses (five-carbon sugars) are also common.

Still another source of diversity for simple

sugars is in the spatial arrangement of their
parts around asymmetric carbons. (Recall that
an asymmetric carbon is a carbon attached to
four different atoms or groups of atoms.)
Glucose and galactose, for example, differ only
in the placement of parts around one
asymmetric carbon (see the purple boxes in
Figure 1.3). What seems like a small difference
is significant enough to give the two sugars distinctive shapes and behaviors.

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Although it is convenient to draw glucose with a linear carbon skeleton, this representation is
not completely accurate. In aqueous solutions, glucose molecules, as well as most other five-
and six-carbon sugars, form rings (Figure 1.4).

Fig.1.4: Linear and ring forms of glucose. Chemical equilibrium between the linear and ring structures greatly
favors the formation of rings. The carbons of the sugar are numbered 1 to 6, as shown. To form the glucose ring,
carbon 1 bonds to the oxygen attached to carbon 5.

Monosaccharides, particularly glucose, are major nutrients for cells. In the process known as
cellular respiration, cells extract energy in a series of reactions starting with glucose
molecules. Simple-sugar molecules are not only a major fuel for cellular work, but their
carbon skeletons also serve as raw material for the synthesis of other types of small organic
molecules, such as amino acids and fatty acids. Sugar molecules that are not immediately used
in these ways are generally incorporated as monomers into disaccharides or polysaccharides.

A disaccharide consists of two monosaccharides joined by a glycosidic linkage, a covalent

bond formed between two monosaccharides by a dehydration reaction. For example, maltose
is a disaccharide formed by the linking of two molecules of glucose (Figure 1.5a). Also known
as malt sugar, maltose is an ingredient used in brewing beer. The most prevalent disaccharide
is sucrose, which is table sugar. Its two monomers are glucose and fructose (Figure 1.5b).
Plants generally transport carbohydrates from leaves to roots and other non-photosynthetic
organs in the form of sucrose. Lactose, the sugar present in milk, is another disaccharide, in
this case a glucose molecule joined to a galactose molecule.

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Fig.1.5: Examples of disaccharide synthesis.

Polysaccharides

Polysaccharides are macromolecules, polymers with a few hundred to a few thousand

monosaccharides joined by glycosidic linkages. Some polysaccharides serve as storage
material, hydrolyzed as needed to provide sugar for cells. Other polysaccharides serve as
building material for structures that protect the cell or the whole organism. The architecture
and function of a polysaccharide are determined by its sugar monomers and by the positions of
its glycosidic linkages.

Storage Polysaccharides

Both plants and animals store sugars for later use in the form of storage polysaccharides.
Plants store starch, a polymer of glucose monomers, as granules within cellular structures
known as plastids, which include chloroplasts. Synthesizing starch enables the plant to
stockpile surplus glucose. Because glucose is a major cellular fuel, starch represents stored
energy.

The sugar can later be withdrawn from this carbohydrate “bank” by hydrolysis, which breaks
the bonds between the glucose monomers. Most animals, including humans, also have
enzymes that can hydrolyze plant starch, making glucose available as a nutrient for cells.
Potato tubers and grains—the fruits of wheat, maize (corn), rice, and other grasses—are the
major sources of starch in the human diet.

Most of the glucose monomers in starch are joined by 1–4 linkages (number 1 carbon to
number 4 carbon), like the glucose units in maltose (see Figure 1.5a). The simplest form of
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starch, amylose, is unbranched. Amylopectin, a more complex starch, is a branched polymer

with 1–6 linkages at the branch points. Both of these starches are shown in Figure 1.6a.

Animals store a polysaccharide called glycogen, a polymer of glucose that is like amylopectin
but more extensively branched (Figure 1.6b). Humans and other vertebrates store glycogen
mainly in liver and muscle cells. Hydrolysis of glycogen in these cells releases glucose when
the demand for sugar increases. This stored fuel cannot sustain an animal for long, however. In
humans, for example, glycogen stores are depleted in about a day unless they are replenished
by consumption of food. This is an issue of concern in low-carbohydrate diets.

Fig.1.6: Storage polysaccharides of plants and animals. These examples, starch and glycogen, are composed
entirely of glucose monomers, represented here by hexagons. Because of the angle of the 1–4 linkages, the
polymer chains tend to form helices in unbranched regions.

Structural Polysaccharides

Organisms build strong materials from structural polysaccharides. For example, the
polysaccharide called cellulose is a major component of the tough walls that enclose plant
cells. On a global scale, plants produce almost 1014 kg (100 billion tons) of cellulose per year;
it is the most abundant organic compound on Earth. Like starch, cellulose is a polymer of
glucose, but the glycosidic linkages in these two polymers differ.

The difference is based on the fact that there are actually two slightly different ring structures
for glucose (Figure 1.7a). When glucose forms a ring, the hydroxyl group attached to the
number 1 carbon is positioned either below or above the plane of the ring. These two ring
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forms for glucose are called alpha (α) and beta (β), respectively. In starch, all the glucose
monomers are in the α configuration (Figure 1.7b), the arrangement we saw in Figures 5.4
and 5.5. In contrast, the glucose monomers of cellulose are all in the β configuration, making
every glucose monomer “upside down” with respect to its neighbors (Figure 1.7c).

Fig.1.7: Starch and cellulose structures.

The differing glycosidic linkages in starch and cellulose give the two molecules distinct three-
dimensional shapes. Whereas certain starch molecules are largely helical, a cellulose molecule
is straight. Cellulose is never branched, and some hydroxyl groups on its glucose monomers
are free to hydrogen-bond with the hydroxyls of other cellulose molecules lying parallel to it.
In plant cell walls, parallel cellulose molecules held together in this way are grouped into units
called microfibrils (Figure 1.8). These cable-like microfibrils are a strong building material for
plants and an important substance for humans because cellulose is the major constituent of
paper and the only component of cotton.
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Fig.1.8: The arrangement of cellulose in plant cell walls.

Enzymes that digest starch by hydrolyzing its α linkages are unable to hydrolyze the β
linkages of cellulose because of the distinctly different shapes of these two molecules. In fact,
few organisms possess enzymes that can digest cellulose. Animals, including humans, do not;
the cellulose in our food passes through the digestive tract and is eliminated with the feces.
Along the way, the cellulose abrades the wall of the digestive tract and stimulates the lining to
secrete mucus, which aids in the smooth passage of food through the tract.

Thus, although cellulose is not a nutrient for humans, it is an important part of a healthful diet.
Most fresh fruits, vegetables, and whole grains are rich in cellulose. On food packages,
“insoluble fiber” refers mainly to cellulose.

Some microorganisms can digest cellulose, breaking it down into glucose monomers. A cow
harbors cellulose digesting prokaryotes and protists in its stomach. These microbes hydrolyze
the cellulose of hay and grass and convert the glucose to other compounds that nourish the
cow. Similarly, a termite, which is unable to digest cellulose by itself, has prokaryotes or
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protists living in its gut that can make a meal of wood. Some fungi can also digest cellulose,
thereby helping recycle chemical elements within Earth’s ecosystems.

Another important structural

polysaccharide is chitin, the
carbohydrate used by arthropods
(insects, spiders, crustaceans, and
related animals) to build their
exoskeletons (Figure 1.9). An
exoskeleton is a hard case that
surrounds the soft parts of an animal.
Pure chitin is leathery and flexible, but
it becomes hardened when encrusted
with calcium carbonate, a salt. Chitin is
also found in many fungi, which use
this polysaccharide rather than
cellulose as the building material for
their cell walls. Chitin is similar to
cellulose, with β linkages, except that
the glucose monomer of chitin has a

nitrogen-containing appendage

Bioplastics: derived from biopolymers such as cellulose and starch.

h
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Biofuels

• Companies dedicated to chemistry of renewable biomass to produce chemicals for use in a wide variety of
everyday products including plastics

• Biomaterials: matter, surface, or construct that interacts with biological systems.

Medicine: Artificial ligaments and tendons, Dental implants..

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PROTEINS

All proteins are the polymers of α-amino acids linked by peptide linkage (derived from Greek
“Proteios” = primary or prime importance).

Amino acid: Amino acids are colourless, crystalline, water soluble soild containing both amino and
carboxyl functional groups.

Twenty different amino acids are linked in different order to build various types of proteins.

Classification:

It is classified based on the number of animo and carboxyl groups into acidic, basic and neutral
amino acids.
Essential amino acids: Cannot be synthesized in the body and obtained from the diet.
Non-essential amino acids: Synthesized in the body.
Zwitterion: The carboxyl group can lose a proton and amino group can accept a proton in aqueous
solution, giving rise to a dipolar ions, known as zwitterion. In zwitterionic form, aminoacids show
amphoric behavoiur as they react both with acids and bases.
Isoelectric pH (pI): The pH at which I a molecule has zero net charge is known as isoelectic point
(pI). All amino acids, peptides have net positive charge at pH below the pI and a net negative charge at
a pH above pI. The solubility is minimal and do not migrate in an electric field.

Figure: Twenty natural amino acids

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Peptide bond: Peptide linkage is an amide formed between –COOH group and –NH2 groupUnit-1

The reaction between two different amino acids (a.a), proceeds through the combination of –NH2
group of one a.a with –COOH group of the other a.a resulting in the elimination of a H2O molecule and

formation of a peptide bond –CO-NH-.

Classification: Protein are classified on the basic of their molecular shape into two types.
1. Fibrous proteins: These proteins are insoluble in water and formed as fibre like structure when the
polypeptide chains run parallel and are held together by hydrogen and disulphide bonds. Eg. Keratin
( hair, wool, silk), Myosin (muscle)

2. Globular proteins: These protins are soluble in water and formed as spherical structure when the chains of
 Structure and shape of proteins can be studied at 4 different organization. They are primary, secondary,
tertiary and quaternary.
Primary structure: Proteins may have one or more polypeptide chains. It is a unique sequence of amino
acids dictated by the DNA in a linear fashion.
Secondary structure: Refers to local twisting and folding of polypeptide due to hydrogen bonds, creates α-
helices and and β-pleated sheets
Teritary structure: Represents the global folding of the polypeptide chains due to chemical interaction
between R-groups (Hydrogen bonds, disulphide linkage, van der waals and electrostatic interactions
Quarternary Structure: A few proteins are composed of one or more polypeptide chains referred to as subun
its. Subunits with respect to each other is known as quaternary structure.

Figure: Structural organization of proteins

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Conjugated protein: Proteins combined with other organic molecules are catgorized in this type Eg.
Glycoproteins, lipoporteins and proteoglycan

Protein Denaturation: Protein found in a biological system with a unique three dimensional structurre
and biological activity is called a native conformation. When a protein in a native form is subjected to
physical change like change in temperature and pH, the H-bonds are disturbed resulting in globules
unfold and helix get uncoiled and protein loses its biological activity. This is called denaturation of
protein.

Importance of proteins:
● Used to build cells
● Act as hormones and enzymes
● Perform much of the work in a cell

Protein fiber with exceptional mechanical properties, 1.absorb a lot of energy before breaking; 2. able to stretch
up to five times their relaxed length without breaking

Artificially synthesize spider silk into fibers- Genetically modified

organisms (bacteria,silkworms, goat ) to express spider proteins then purified

● 2013 : fibers produced by German company

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The lipids are a heterogeneous group of compounds related to fatty acids and include fats, oils, waxes
and other related substances. They are hydrophobic in nature and variously known as Lipins or
Lipiods.
Lipids were defined as compounds containing in their molecules an aliphatic chain (consisting of
–CH2–) of at least eight carbon atoms.
The principal compounds of most lipids is Fatty acid

Fatty Acids (FA): The lipid building blocks. Fatty acids are composed of a chain of methylene groups
(–CH2–) with a carboxyl functional group at one end. The fatty acid chains are usually between 10 and
20 Carbon atoms long. The fatty "tail" is non-polar (Hydrophobic) while the Carboxyl "head" is a
little polar (Hydrophillic).
Most of the fatty acid have an even number of carbon atoms arranged in an unbranched chain.
Fatty acids can be saturated - they have no double bonds between the carbon atom and have general
formula CH3(CH2)nCOOH, where n is an even number or unsaturated – contains one or more double
bonds. Unsaturated fatty acids exist in geometric form. Unsaturated FA further classified as
monounsaturated FA have one site of unsaturation, eg. Palmitoleic acid and oleic acid.

Polyunsaturated fatty acids have two or more double bonds which are separated atleast by one
methylene group. Eg. Linoleic acid and Linolenic acid.
CH3(CH2)4CH=CHCH2CH=CH(CH2)7COOH (C18:2∆9,12)- Linoleic acid
CH3CH2CH=CHCH2CH=CHCH2CH=CH(CH2)7COOH (C18:3∆9,12,15)- Linolenic acid

Classification:
Lipids can be classified into three major types:
1. Simple lipids: Esters of fatty acids with various types of alcohols
2. Complex lipids: Esters of fatty acids with alcohols complexed with a non-lipid moiety.
3. Derived lipids: includes diverse group of compounds (prostaglandins, fat- soluble vitamins,
steroids, etc)
Simple lipids:
a. Triglycerides: Monomer of lipids containing three fatty acids linked by a molecule of glycerol.
These are energy storage molecules.

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b. Waxes: Waxes are composed of a single, highly complex alcohol joined to a long chain fatty acid
via a typical ester linkage. Waxes are important structural lipids often found as protective coatings on
the surfaces of leaves, stems, hair, skin, etc. They provide effective barriers against water loss and in
some situations make up the rigid architecture of complex structures such as the honeycomb of the
beehive.
Complex lipids: consist of a lipid moiety and a non-lipid component that may be a small molecule or
a macromolecule.
Major classes of complex lipids are glycerophospholipids, sphingophospholipids, glycolipids,
lipoproteins and proteolipids.
a. Glycerophospholipids: It is membrane lipids, in which two fatty acids are attached in ester linkage
to C1 and C2 of glycerol and a high polar group is attached to the C3 through a phosphodiester
linkage. The main building block of phospholipids is phosphatidic acid.

Hydrogen in phosphatidic acid can be substituted by a number of alcohols. The common alcohols are
ethanolamine, choline and L-serine.

b. Sphinophospholipids: Membrane lipids composed of one molecule of sphingosine, a long chain

amino alcohol, one molecule of long chain fatty acid and a polar head group, joined together by
glycosidic linkage or by phosphodiester linkage. When a fatty acid is attached the resulting compound
is ceramide. Sphingophospholipids are formed from ceramide by esterification of phosphoric acid by
either serine, ethanolamine or choline.
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c. Glycolipids: are the derivatives of carbohydrates and glycerides and do not contain phosphate. Eg.
Gangliosides- oligosaccharides derivatives of ceramide that contain atleast one residue of N-acetyl
neuraminic acid.
c. Lipoprotein: It consists of lipids components, triacyl glycerol, phospholipids and cholesterol or
cholesterol ester. The protein components have a relatively high proportion of non-polar amino acid
residues responsible for binding of lipids. Plasma proteins have been classified on the basis of density
into chylomicrons, very low density lipoprotein (VLDL), Intermediate density lipoprotein (IDL), low
density lipoprotein (LDL) and high density lipoprotein (HDL).
Derived Lipids:
Steroids: A steroid is a type of organic compound that contains a specific arrangement of four
cycloalkane rings that are joined to each other.
Ex: Cholesterol, the sex hormones estradiol and testosterone.

Importance of the lipids:

● Long term storage of energy,
● Constituents of biological membrane and Steroid hormones etc.,

Nucleic acids are the important organic substances found in nucleus and cytoplasm. They control the
important biosynthetic activities of the cell and carry hereditary information from generation to
generation.
Nucleic acids are long chain polymers of nucleotides, so they are also called polynucleotides.
There are two types of nucleic acids present in the living system.
1. Deoxyribonucleic acid (DNA) (nucleus)
2. Ribonucleic acid (RNA) (cytoplasm)
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Composition of Nucleic acid: DNA or RNA composed of nucleotides. In turn, nucleotide is made up
of nucleoside units (Base + Sugar).
Upon hydrolysis, DNA/RNA yield pentose sugar, phosphoric acid and nitrogeneous bases.

In DNA, the sugar moiety is D-deoxyribose whereas in RNA, it is D-ribose.

DNA contains four bases such as adenine (A), guanine (G), cytosine (C) and thymine (T) whereas in
RNA, the first three bases are same but fourth bases is uracil.

Structure of nucleic acid:

● Nucleoside: A unit formed by the attachment of a base to 1’ position of sugar.
● Nucleotide: Nucleoside is linked to phosphoric acid at 5’ position of sugar moiety result in the
formation of nucleotide.
● Nucleotides are joined together by phosphodiester linkage between 5’ and 3’ carbon atoms of the
pentose sugar.
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Watson-Crick model or Double helical structure for DNA

The sequence of nucleotides in the chain of a nucleic acid is called its primary structure.
James Waston and Francis Crick proposed a double strand helix structure for DNA.

The characteristics features of this model are

1. It consists of two helical DNA chains wound around the same axis to form a right handed double
helix.
2. The two strands are complementary to each other because of hydrogen bonds between specific pairs
of bases. A = T; G = C
3. The hydrophilic backbones of alternating deoxyribose and phosphate groups are on the periphery of
the double helix.
4. The Purines and pyridimines bases of both strands are stacked inside the double helix.
5. The hydrophobic planar ring structure very close together and perpendicular to the long axis.
6. The offset pairing of two strands creates a major groove and minor groove on the surface of the
duplex.
7. Each nucleotide base of one strand is paired in the same plane with a base of the other strand.
8. The distance between successive base pair s is 3.4 Aᵒ.
9. The every turn of the helix measures 34A and contains 10 base pairs.
10. According to this model, DNA is antiparallel which was confirmed by X-ray analysis.
Chargaff’s rule of base equivalence: This rule states that the amount of purines is equal to the
amount of pyrimidines A=T and G=C.
RNA- Ribonucleic acid
● Single stranded linear molecule
● Backbone- composed of ribose and phosphate
● Bases: A, U, G, C
● RNA Types: There are three types
1. mRNA: messenger RNA serve as a template for a protein synthesis
2. rRNA: ribosomal RNA forms ribosomes and factory for protein synthesis
3. tRNA: Transfer RNA functions as a carrier to bring amino acids to the ribosomes
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Figue: Double helical structure of DNA

Difference between DNA and RNA

Biological importance of nucleic acids:

● DNA is the chemical basis of heredity and considered as a reserve of genetic information.
● DNA is responsible for maintaining the identity of different of different species of organisms
over millions of years
● DNA molecule is capable of self duplication during cell division and identical DNA
strands are transferred to daughter cells
● RNA is involved in the protein synthesis.
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ENZYMES

Enzymes are biological catalyst. All the enzymes are globular proteins.
Enzymes are produced within the living organisms which speed up chemical reactions, by lowering the
activation energy, in the living organisms but themselves remain unchanged at the end of the
reaction.
Activation energy is the energy required to make the substances react.
The enzyme combines with the substrate molecules to form an enzyme-substrate complex. In such
close contact the substrate molecules may be distorted and hence easily react to form an enzyme-
product complex which then split to release the product molecule and the enzyme. In this way, the
activation energy is lowered. Since they are not altered by the reactions they catalyse, so that they
can be reused. In other words they are effective in very small amount.
At some point in the progress of the reaction, the energy reaches a maximum value. This state is
temporary, short-lived configuration of atoms called the transition state. The amount of energy
required to reach the transition state is called the activation energy.

How does an enzyme increase the rate of a reaction?

When substrates bind to an enzyme’s active site, interactions with the enzyme change the shape of the
substrates (and enzyme) to a configuration that lowers the energy of the transition state (relative to an
un-catalyzed reaction).
Active site: Enzymes are normally larger than the substrate molecules they act upon. The part of the
enzyme molecule actually comes into contact with the substrate is called active site.

There are six major classes of enzymes. They are listed in below table.
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Mechanism of enzyme actions:

1. Lock and key hyopthesis (Fischer, 1890)
The active site of the enzyme molecule has a distinctive configuration due to the unusual folding of the
protein molecule and position of different chemical groups within it. Only the specific substrate
molecules with the right shape can fit into the active site to form enzyme-substrate complex, thus the
substrate and enzyme molecules act as the lock and key respectively.

Figure: Lock and Key Hypothesis

2. Induced Fit Theory (Koshland, 1959):

In the presence of substrate the active site of the enzyme may change shape to fit the substrate i.e. the
enzyme is flexible and moulds to fit the substrate molecule. This theory is stated based on the nature of
enzyme --- protein molecule is flexible enough to allow conformational changes.

Figure: Induced Fit Theory

Co-factors: It is a non-protein substance which is essential for some enzymes to function efficiently.
There are three types:
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a) Activators: are substances which are necessary for the functioning of certain enzymes. They may
assist in forming the E-S complex by moulding either the enzyme or substrate molecule into a more
suitable shape. e.g.
i) Enzyme thrombokinase, which converts prothrombin into thrombin during blood clotting, is
activated by Calcium ions.
ii) Salivary amylase requires the presence of chloride ions before it converts starch into maltose.
b) Coenzymes: are non-protein organic substances which are essential to the efficient functioning of
some enzymes, but are not themselves bound to the enzyme.
Many coenzymes are derived from vitamins. e.g. Nicotinamide adenine dinucleotide (NAD) act as a
coenzyme to dehydrogenases by acting as a hydrogen acceptor in the Krebs Cycle.
c) Prosthetic groups: are organic , non-protein molecules and bound to the enzyme themselves. e.g.
Heme is an iron-containing prosthetic group. it may function as electron carrier and oxygen carrier in
haemoglobin. It is also found in catalases and peroxidases, which catalyse the decomposition of
hydrogen peroxide to water and oxygen.
Factors affecting enzymatic action:
1. Temperature
2. pH
3. Enzyme concentration
4. Substrate concentration
5. Product concentration
6. Inhibition

Application of enzymes:
There are three main advantages of using enzymes in industrial processes.
1. They are specific in their action and are therefore less likely to produce unwanted by-products.
2. They are biodegradable and therefore cause less environmental pollution.
3. They work in mild conditions, i.e. low temperatures, neutral pH and normal atmospheric pressure,
and are therefore energy-saving.
Commerical enzymes are produced by micro-organisms such as yeasts and bacteria.
Sometimes naturally occurring strains are usued, but increasingly nowadays special strains are
developed by genetic engineering to produce particular enzymes.
(i) Biological washing powders:- contain enzymes, usually proteases - remove 'biological' stains such
as food, blood and so on - as to reduce allergic reactions to man, the enzymes are encapsulated in wax
from which they are released only when in the wash
(ii) Meat tenderizers:- contain protease, made by Bacillus subtilis - as the main component of meat is
protein, so the protease may digest some peptide bonds of the meat, this tenderizes the meat.
Some of the important enzymes and their function are listed below in the table.

https://docs.google.com/document/d/1yAKcq2ojEQGTOtGSe-tDQ1ZE-mreUF7YbEpY87gLwD0/edit?ts=5bf5e92c 25/54
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