Biochemistry Slides

1st Prof

Sir Zahid Ali

Compiled by : Muhammad Huzaifa

Batch 2020-25
 Biochemistry
Biochemistry
Biochemistry can be defined as the science concerned with the
chemical basis of life (bios “life”).
Cell is the structural unit of living systems. Thus, biochemistry can
also be described as the science concerned with the chemical
constituents of living cells and with the reactions and processes
theyundergo.
By this definition, biochemistry encompasses large areas of cell
biology, of molecular biology, and of molecular genetics.
 Biochemistry, also called as biological chemistry or physiological
chemistry is the study of chemical processes in the living
organisms.
Simply biochemistry deals with the chemical components
and chemical processes in living organism.
Biochemistry teaches how the biological molecules like
carbohydrates, proteins, lipids, nucleic acids gives rise to
different chemical processes in the living cell which in turn
gives rise to the complexity of life.
It is a laboratory based science that brings together biology
and chemistry. By using chemical knowledge and
techniques, biochemists can understand and solve
biological problems.
Biochemistry focuses on processes happening at a
molecular level. It focuses on what’s happening inside our
cells, studying components like proteins, lipids and
organelles. It also looks at how cells communicate with
each other, for example during growth or fighting illness.
The Aim of Biochemistry
•The major objective of biochemistry is the complete
understanding, at the molecular level, of all of the
chemical processes associated with living cells.
•To achieve this objective, biochemists have sought to
isolate the numerous molecules found in cells,
determine their structures, and analyze how they
function.
A Knowledge of Biochemistry Is Essential to All
Life Sciences
• Genetics: The biochemistry of the nucleic acids lies at the heart of
genetics; in turn, the use of genetic approaches has been critical for
elucidating many areas of biochemistry.
• Physiology, the study of body function, overlaps with biochemistry
almost completely.
• Immunology employs numerous biochemical techniques, and many
immunologic approaches have found wide use by biochemists.
• Pharmacology and Pharmacy rest on a sound knowledge of
biochemistry and physiology; in particular, most drugs are metabolized
by enzyme-catalyzed reactions.
• Toxicology: Poisons act on biochemical reactions or
processes.
• Pathology: Biochemical approaches are being used
increasingly to study basic aspects of pathology (the study
of disease), such as inflammation, cell injury, and cancer.
• Many workers in microbiology, zoology, and botany
employ biochemical approaches almost exclusively.
• These relationships are not surprising, because life as we
know it depends on biochemical reactions and processes.
In fact, biochemistry is increasingly becoming their
common language.
Relationship Between Biochemistry & Medicine
The two major concerns for healthcare professionals particularly
physicians are
1. The understanding and maintenance of health and 2.
The understanding and effective treatment of diseases.
Biochemistry impacts enormously on both of these fundamental
concerns of medicine. Biochemical studies have illuminated many
aspects of health and disease, and conversely, the study of various
aspects of health and disease has opened up new areas of biochemistry.
Biochemistry & Medicine is a Two-way Street
How Two-way street
• For instance, a knowledge of protein structure and function was
necessary to elucidate the single biochemical difference between
normal hemoglobin and sickle cell hemoglobin. On the other hand,
analysis of sickle cell hemoglobin has contributed significantly to
our understanding of the structure and function of both normal
hemoglobin and other proteins.
• Another example is the pioneering work of Archibald Garrod, a physician
in England during the early 1900s. He studied patients with a number of
relatively rare disorders (alkaptonuria, albinism, cystinuria, and
pentosuria) and established that these conditions were genetically
determined. Garrod designated these conditions as inborn errors of
metabolism. His insights provided a major foundation for the
development of the field of human biochemical genetics.
Alkaptonuria is a rare inherited disorder. It occurs when your body can't produce
enough of an enzyme called homogentisic dioxygenase (HGD). This enzyme is
used to break down a toxic substance called homogentisic acid. When you don't
produce enough HGD, homogentisic acid builds up in your body.
Albinism is a genetic condition where people are born without the usual pigment
(color) in their bodies. Their bodies aren't able to make a normal amount of
melanin, the chemical that is responsible for eye, skin, and hair color.
Cystinuria is a cause of persistent kidney stones. It is a disease involving the
defective transepithelial transport of cystine and dibasic amino acids in the
kidney and intestine, and is one of many causes of kidney stones.
Pentosuria is a condition where the sugar xylitol, a pentose, presents in the urine
in unusually high concentrations. It was characterized as an inborn error of
carbohydrate metabolism in 1908. It is associated with a deficiency of Lxylulose
reductase, necessary for xylitol metabolism.
More recent efforts to understand the basis of the genetic
disease known as familial hypercholesterolemia, which results
in severe atherosclerosis at an early age, have led to dramatic
progress in understanding of cell receptors and of
mechanisms of uptake of cholesterol into cells.
Studies of oncogenes in cancer cells have directed attention to
the molecular mechanisms involved in the control of normal
cell growth.

These and many other examples emphasize how the study of

disease can open up areas of cell function for basic biochemical
research.
NORMAL BIOCHEMICAL PROCESSES ARE
THE BASIS OF HEALTH
• The World Health Organization (WHO) defines health as a state of
“complete physical, mental and social well-being and not merely the
absence of disease and infirmity.”

• According to biochemical viewpoint, health may be considered that

situation in which all the intra- and extracellular reactions that occur in
the body are proceeding at rates corresponding with the organism’s
maximal survival in the physiologic state.
Biochemical Research Has Impact on Nutrition
& Preventive Medicine
• One major requirement for the maintenance of health is the optimal
dietary intake of a number of chemicals; the chief of these are
vitamins, certain amino acids, certain fatty acids, various minerals, and
water.
• Because much of the subject matter of both biochemistry and nutrition
is concerned with the study of various aspects of these chemicals,
there is a close relationship between these two sciences. Moreover,
more emphasis is being placed on on preventive medicine. Thus,
nutritional approaches for example the prevention of atherosclerosis
and cancer are receiving increased emphasis. Understanding nutrition
depends to a great extent on a knowledge of biochemistry.
Most & Perhaps All Disease Has a Biochemical
Basis
Not all but majority of the diseases occurs due to abnormalities of
molecules, chemical reactions, or biochemical processes. Major causes
of disease are;
In most of the diseases, biochemical studies contribute to both the diagnosis and
treatment. Some major uses of biochemical investigations and of laboratory tests in
relation to diseases are;
Summary
• Biochemistry is the science concerned with studying the various
molecules that occur in living cells and organisms and with their
chemical reactions. Because life depends on biochemical
reactions, biochemistry has become the basic language of all
biologic sciences.
• Biochemistry is concerned with the entire spectrum of life
forms, from relatively simple viruses and bacteria to complex
human beings.
• Biochemistry and medicine are intimately related. Health
depends on a harmonious balance of biochemical reactions
occurring in the body, and disease reflects abnormalities in
biomolecules, biochemical reactions, or biochemical processes.
• Advances in biochemical knowledge have illuminated many areas of
medicine. Conversely, the study of diseases has often revealed previously
unsuspected aspects of biochemistry. The determination of the sequence
of the human genome, nearly complete, will have a great impact on all
areas of biology, including biochemistry, bioinformatics, and
biotechnology.
• Biochemical approaches are often fundamental in illuminating the
causes of diseases and in designing appropriate therapies.
• The judicious use of various biochemical laboratory tests is an integral
component of diagnosis and monitoring of treatment.
• A sound knowledge of biochemistry and of other related basic disciplines
is essential for the rational practice of medical and related health sciences.
Carbohydrates
Carbohydrates-Overview
Carbohydrates are polyhydroxylated compounds with at least
3 carbon atoms with potentially active carbonyl groups which
may either be aldehyde or ketone groups or those compounds
which yield them on hydrolysis.
They are also called saccharides which means sugar.
Carbohydrates are the most abundant biomolecules on the
earth, however in human beings they form only 1% of body
mass.
The empiric formula for many of the simpler carbohydrates is
(CH2O)n, hence the name “hydrate of carbon.”
Carbohydrates have a wide range of functions;
1. providing a significant fraction of the dietary calories for
most organisms,
2. acting as a storage form of energy in the body, and
3. serving as cell membrane components that mediate
some forms of intercellular communication.
4. also serve as a structural component of many organisms,
including the cell walls of bacteria, the exoskeleton of many
insects, and the fibrous cellulose of plants.
Classification of Carbohydrates
1. Monosaccharides
These are simple sugar and cannot be further hydrolyzed.
Empirical formula (CH2O)n where n=3 or some larger number.
They may be aldoses (when aldehyde group is present) or ketoses
(when ketone group is present). For example, glyceraldehyde is an
aldose, whereas dihydroxy acetone is a ketose.
Examples of some monosaccharides commonly found in humans
Mono saccharides can be linked by glycosidic bonds to create
larger structures.
Disaccharides
Contain two monosaccharides. For example:
Glucose + Glucose = Maltose
Glucose + Galactose = Lactose
Glucose + Fructose = Sucrose
These are linked together by glyosidic bond and by the
process of condensation.
Oligosaccharides
Consist of short chains of monosaccharides. Typically it contain less
than 20 monosaccharides.
Examples:
α-Dextrins: Polymer of about 8 glucose molecules
Maltotriose: 3 glucose molecules
Isomaltose: glucose dimer having α 1→6 linkage
Polysaccharides
As the name indicates, these carbohydrates contain a large number of
sugar units in their molecules. When >20 monosaccharides linked
together they form polysaccharides.
Mostly occurs in nature and are also known as glycans. They serve as
stores of fuel and also form structural elements of cell.
Types: consist of
1. Homopolysaccharides
2. Heteropolysaccharides
Homopolysaccharides
Consist of only one type of monosaccharide units. Examples includes
starch, glycogen, cellulose and dextrins all of which contain glucose
polymers.
Starch is the main storage of monosaccharides in plants and the main
carbohydrate in the diet.
Homopolysaccharides may be branched or unbranched. For example,
in starch, usually in a straight chain glucose are linked together by α
1→4 glycosidic bonds and that form is called unbranched form and is
called as amylose, while in branched form it contain α 1→4 glycosidic
bonds and α 1→6 glycosidic bonds. This form is called as amylopectin
Presentations
1. Glycogen-
2. Cellulose-
3. Dextrins-
4. Heteropolysaccharides-
Isomerism in Sugars
Isomers
Compounds that posses the same chemical formula are called isomers.
Glucose, fructose, galactose and mannose all have the same chemical
formula (C6H12O6), and therefore isomers of each other. The only
difference is the different arrangement of atoms in space. And such
type of isomers are called stereoisomers.
Epimers
These are two isomers which differ in configuration around one specific
carbon atom other than the carbon atom of the carbonyl group.
For example: Glucose and Galactose differ each other only in the
position of ─OH at carbon No.4 and are called carbon-4 epimers.
Glucose and Mannose??? Write their structures??
Anomers
These are isomers which differ in configuration around the anomeric
carbon atom (the carbon atom of carbonyl group) which is carbon No.1
in aldoses and carbon No.2 in ketoses. These forms are called α─ and β
anomers.

α-D-Glucose β-D-Glucose
D-and L Isomerism
Optical Isomerism in Sugars
• Optically Active Compounds
• When a beam of plane polarized light passes through a solution of
certain organic molecules, such as sugar or camphor, the plane of
polarization is rotated through an angle α. Not all organic substances
exhibit this property, but those that do are said to be optically active.
• The angle of rotation can be measured with an instrument called a
polarimeter. When a solution of known concentration of an optically
active material is placed in the polarimeter, the beam of light is
rotated either to the right (clockwise) or to the left (anti-clockwise).
So the compounds which rotate the plane polarized light (PPL) to the
right (clockwise) is said to be dextrorotatory, and those which rotate
the PPL to the left is said to be levorotatory. Dextrorotatory is
indicated by + sign, while Levorotatory by a minus sign (─).
Chiral Carbon Atom

A carbon atom which is bonded to four different groups. It is also termed as

handedness. Chiral carbon lacks the plane of symmetry and therefore
called as dissymmetric or Asymmetric.

A chiral object cannot be superimposed on its mirror image. For example, a

left hand does not posses a plane of symmetry, and its mirror image is not
another left hand but a right hand. The two are not identical and cannot be
superimposed. If we lay one hand on the other, the fingers and the thumbs
would clash.
Because of the presence of asymmetric carbons in the molecules of sugars,
the plane polarized light when passed through their solutions will be
rotated either to the left or right. So the sugars rotating light to the left are
levorotatory and those to the right are referred as dextrorotatory.
Levorotatory are denoted by l (–ve) sign while dextrorotatory by d (+ve)
sign.

It should be noted that there is no relationship between the D and L

signs, and d (+) and l (-) signs. A sugar may be D sugar and may be
levorotatory.
Cyclic/Ring structure of
Sugars
D-Glucose
It is a hexose and aldohexose due to its aldehyde group. Its open chain
formula was first suggested by Fischer in 1891.
Aldohexoses have 4 asymmetric carbons i.e., carbon 1 to carbon 5.
Therefore, the number of possible optical isomers are expected to be
16 according to Vant Hoff’s law
“the number of optical isomers are equal to 2n where n refers to the
number of optical isomers”.
However,
in aqueous solution, glucose show the property of Mutarotation in
which they behave as they have one more asymmetric carbon atom
than is shown by the open chain formula by Fischer. The carbon
responsible for this phenomena is the carbonyl carbon. Thus the
Mutarotation provides another asymmetric carbon and making the
number of optical isomers equals to 25=32. this is because that each of
the sixteen isomers can occur in two anomeric forms i.e., α─ and β.
Mutarotation
Mutarotation is the change in specific rotation of a chiral compound.
The monosaccharide D-glucose exists in two cyclic forms, α-D-glucose
([α]D25 = +112) and β-D-glucose ([α]D25 = +19), and are available as pure
compounds.
When D-glucose is added to water, it change from one
form to the other via the open-chain form, during which
the specific rotation of the solution changes gradually
until it reaches the equilibrium value +52.7º.
At equilibrium, about 1/3 of D-glucose is of the type
having specific rotation of +112, while 2/3 of it is that with a
specific rotation of +19. These two forms are termed as α─
and β forms of D-glucose.
Unlike D- and L glucose these α─ and β anomers are not mirror
images nor enantiomers but they only differ from each other in
respect to configuration around the anomeric carbon. Moreover,
they posses different degree of optical rotation though rotate the
plane polarized light to the same side.
Hemiacetal Formation
• The ring structure of an aldose is a hemiacetal, since it is formed by
combination of an aldehyde and an alcohol group. Hemiacetal is the
condensation between the aldehyde and hydroxyl group of the same
compound. Similarly, the ring structure of a ketose is a hemiketal.
• Amylene oxide ring structure of α─ and β Glucose. Here condensation
occurs between the carbon No.1 (aldehyde group) and hydroxyl group
of carbon no.5 that’s why also called as 1→5 ring.
• Glucose can also occur in butylene oxide ring structure having 1→4
ring
Hawarth’s Formula of Glucose
• The α─ and β forms of glucose can also be represented by showing
glucose as a pyran i.e., six membered ring with 5 carbons and one
oxygen.
Chair & Boat Confirmation of α-D-glucopyranose
Biomedical Importance of
Carbohydrates
Monosaccharides
Many Monosaccharides Are Physiologically Important
Derivatives of trioses, tetroses, and pentoses and of a
seven-carbon sugar (sedoheptulose) are formed as
metabolic intermediates in glycolysis and the pentose
phosphate pathway.
Pentoses are important in nucleotides, nucleic acids,
and several coenzymes.
Pentoses of Physiologic Importance
Physiologically the most Important Hexoses
Glucose, galactose, fructose, and mannose are physiologically the most
important hexoses.
Aldoses
Ketoses
Glycosides
Sugars form glycosides with other compounds & with each other.
Glycosides are formed by condensation between the hydroxyl group of
the anomeric carbon of a monosaccharide, or monosaccharide residue,
and a second compound that may—or may not (in the case of an
aglycone)—be another monosaccharide.
If the second group is a hydroxyl, the O-glycosidic bond is an acetal link
because it results from a reaction between a hemiacetal group (formed
from an aldehyde and an —OH group) and an other —OH group.
If the hemiacetal portion is glucose, the resulting compound is a
glucoside; if galactose, a galactoside; and so on. If the second group is
an amine, an N-glycosidic bond is formed, eg, between adenine and
ribose in nucleotides such as ATP
Glycosides are widely distributed in nature; the
aglycone may be methanol, glycerol, a sterol, a
phenol, or a base such as adenine. The glycosides that
are important in medicine because of their action on
the heart (cardiac glycosides) all contain steroids as
the aglycone. These include derivatives of digitalis and
strophanthus such as ouabain, an inhibitor of the Na+-
K+ ATPase of cell membranes.

Other glycosides include antibiotics such as

streptomycin.
Deoxy Sugars Lack an Oxygen Atom
Deoxy sugars are those in which a hydroxyl group has been replaced by
hydrogen. An example is deoxyribose in DNA. The deoxy sugar L-fucose
occurs in glycoproteins; 2-deoxyglucose is used experimentally as an
inhibitor of glucose metabolism.
Amino Sugars (Hexosamines)
The amino sugars include D-glucosamine, a constituent of hyaluronic
acid, D-galactosamine (chondrosamine), a constituent of chondroitin;
and D-mannosamine. Several antibiotics (eg, erythromycin) contain
amino sugars believed to be important for their antibiotic activity.

Glucosamine (2-amino-D-glucopyranose).
Galactosamine 2-amino-D-galactopyranose).

D-glucosamine
 Physiologically Important Disaccharides
The physiologically important disaccharides are maltose, sucrose, and
lactose.
Physiologically Important Polysaccharides
Polysaccharides include the following physiologically important
carbohydrates.
• Starch is a homopolymer of glucose forming an α-glucosidic chain,
called a glucosan or glucan. It is the most abundant dietary
carbohydrate in cereals, potatoes, legumes, and other vegetables. The
two main constituents are amylose (15–20%), which has a non-
branching helical structure; and amylopectin (80–85%), which
consists of branched chains composed of 24–30 glucose residues
united by 1 → 4 linkages in the chains and by 1 → 6 linkages at the
branch points.
Glycogen is the storage polysaccharide in animals. It is a more highly
branched structure than amylopectin, with chains of 12–14 α-D-
glucopyranose residues (in α[1 → 4]-glucosidic linkage), with
branching by means of α(1 → 6)-glucosidic bonds.

Inulin is a polysaccharide of fructose (and hence a fructosan) found in

tubers and roots of dahlias, artichokes, and dandelions. It is readily
soluble in water and is used to determine the glomerular filtration
rate.

Dextrins are intermediates in the hydrolysis of starch.

• Cellulose is the chief constituent of the framework of plants. It is
insoluble and consists of β-D-glucopyranose units linked by β(1 → 4)
bonds to form long, straight chains strengthened by cross-linked
hydrogen bonds. Cellulose cannot be digested by mammals because
of the absence of an enzyme that hydrolyzes the β linkage. It is an
important source of “bulk” in the diet. Therefore, it relives
constipation and decrease the absorption of glucose and cholesterol
from intestines. Microorganisms in the gut of herbivores can
hydrolyze the β linkage and ferment the products to short-chain fatty
acids as a major energy source. There is limited bacterial
metabolism of cellulose in the human colon.
• Chitin is a structural polysaccharide in the exoskeleton of crustaceans
and insects and also in mushrooms. It consists of N-acetyl-D-
glucosamine units joined by β (1 →4)-glycosidic linkages.
Glycosaminoglycans (mucopolysaccharides) are complex
carbohydrates characterized by their content of amino sugars
and uronic acids. When these chains are attached to a protein
molecule, the result is a proteoglycan.
Proteoglycans provide the ground or packing substance of
connective tissues. Their property of holding large quantities of
water and occupying space, thus cushioning or lubricating other
structures, is due to the large number of -OH groups and
negative charges on the molecules, which, by repulsion, keep the
carbohydrate chains apart. Examples are hyaluronic acid,
chondroitin sulfate, and heparin.
Glycoproteins (mucoproteins) occur in many different
situations in fluids and tissues, including the cell membranes.
They are proteins containing branched or unbranched
oligosaccharide chains.
The sialic acids are N- or O-acyl derivatives of neuraminic acid
(Figure 13–16).
Neuraminic acid is a nine-carbon sugar derived from mannosamine
(an epimer of glucosamine) and pyruvate.
Sialic acids are constituents of both glycoproteins and gangliosides.
Summary
• Carbohydrates are major constituents of animal food and animal
tissues. They are characterized by the type and number of
monosaccharide residues in their molecules.
• Glucose is the most important carbohydrate in mammalian
biochemistry because nearly all carbohydrate in food is converted to
glucose for metabolism.
• Sugars have large numbers of stereoisomers because they contain
several asymmetric carbon atoms.
• The monosaccharides include glucose, the “blood sugar”; and ribose,
an important constituent of nucleotides and nucleic acids.
• The disaccharides include maltose, an intermediate in the
digestion of starch; sucrose, important as a dietary constituent
containing fructose; and lactose, in milk.
• Starch and glycogen are storage polymers of glucose in plants
and animals, respectively. Starch is the major source of energy in
the diet.
• Complex carbohydrates contain other sugar derivatives such as
amino sugars, uronic acids, and sialic acids. They include
proteoglycans and glycosaminoglycans, associated with structural
elements of the tissues; and glycoproteins, proteins containing
attached oligosaccharide chains. They are found in many
situations including the cell membrane.
Amino Acids & Proteins
Proteins & its Function in the Body
Proteins are extremely complicated molecules and are the nitrogenous
compounds made up of variable number of amino acids joined to each other
by a specific covalent bond called peptide bond or peptide linkage.
Proteins are the most abundant and functionally diverse molecules in living
systems. Almost every life process depends on this class of molecules.
For example, enzymes and polypeptide hormones direct and regulate
metabolism in the body,
whereas contractile proteins in muscle permit movement.
In bone, the protein collagen forms a framework for the deposition of
calcium phosphate crystals, acting like the steel cables in reinforced
concrete.
In the bloodstream, proteins, such as hemoglobin and plasma
albumin, shuttle molecules essential to life, whereas immuno
globulins fight infectious bacteria and viruses.

In short, proteins display an incredible diversity of functions, yet all

share the common structural feature of being linear polymers of
amino acids.
More than 300 amino acids are known but only 20 take part in
the formation of all types of proteins. These amino acids are
commonly found in plants and animals.
Amino acids are the building blocks of proteins and are linked
together and form a specific protein. The number of the specific
number and sequence of amino acids are unique to each
protein.
Rather like the alphabet, the amino acid 'letters' can be arranged
in millions of different ways to create 'words' and an entire
protein 'language'. Depending on the number and sequence of
amino acids, the resulting protein will fold into a specific shape.
This shape is very important as it will determine the
protein’s function (e.g. muscle or enzyme). Every species,
including humans, has its own characteristic proteins.
What do proteins do for the body?
Our bodies are made up of thousands of different proteins, each with a
specific function. They make up the structural components of our cells and
tissues as well as many enzymes, hormones and the active proteins secreted
from immune cells.

These body proteins are continually being repaired and replaced throughout
our lives. This process (known as ‘protein synthesis’) requires a continuous
supply of amino acids. Although some amino acids can be recycled from the
breakdown of old body proteins, this process is imperfect. This means we
must eat dietary protein to keep up with our body’s amino acid demand.

As protein is essential for cell and tissue growth, adequate intake of protein
is particularly important during periods of rapid growth or increased
demand, such as childhood, adolescence, pregnancy, and breastfeeding.
Structure of Amino Acid
Although more than 300 different amino acids have been described in
nature, only 20 are commonly found as constituents of mammalian
proteins.
[Note: These are the only amino acids that are coded for by DNA, the
genetic material in the cell].
Each amino acid has a carboxyl group, a primary amino group, and a
distinctive side chain (“R-group”) bonded to the α-carbon atom except
proline, which has a secondary amino group.
At physiologic pH (approximately pH 7.4), the carboxyl group is dissociated,
forming the negatively
charged carboxylate ion (–COO–), and the amino group is protonated (–NH3+). In
proteins, almost all of these carboxyl and amino groups are combined through
peptide linkage and, in general, are not available for chemical reaction except
for hydrogen bond formation (Figure 1.1B). Thus, it is the nature of the side
chains that ultimately dictates the role an amino acids play in proteins.
It is, therefore, useful to classify the amino acids according to
the properties of their side chains, that is, whether they are
nonpolar (have an even distribution of electrons) or polar (have
an uneven distribution of electrons, such as acids and bases.
Amino acids with non-polar aliphatic side chains
These are present in glycine, alanine, valine, leucine, isoleucine and
proline.
Amino Acids with Aromatic Side Chains
These includes phenylalanine, tyrosine, and tryptophan. The
hydroxyl group of tyrosine can form hydrogen bonds and shows
polarity. Whereas, the N of imidazole ring in tryptophan gives
polarity. Phenylalanine shows little polarity.
Amino Acids with Uncharged Polar Side Chains
These are present in asparagine, glutamine, cysteine, methionine,
serine and threonine. Polarity of these amino acids is due to the
presence of functional groups that form H-bonds with water.
Amino Acids with Acidic Side Chains
These are present in glutamic acid and aspartic acid. These are
negatively charged at neutral pH and usually called as glutamate and
aspartate.
Amino Acids with Basic Side Chains
These are present in lysine, arginine and histidine. Lysine, and arginine
are strong bases with positive charge on them, while histidine is a weak
base.
Non-standard Amino Acids
These amino acids do not take part in protein synthesis but many of them
play important role in the body. Hundreds of non-standard amino acids are
known but few of which has important physiological functions. i.e.,
1. Citrulline
2. Ornithine
3. Β-Alanine
4. Pantothenic acid
5. Gamma-Aminobutyric acid (GABA)
6. Dihydroxyphenylalanine (DOPA)
7. Homocyestine
8. Iodinated Amino Acids
Citrulline
Citrulline is an amino acid that was first found in watermelon. It is
considered nonessential, meaning that your body can naturally
produce some on its own.
Ornithine
Ornithine is used for improving athletic performance, reducing
glutamine poisoning in the treatment of a brain condition due to
liver disease (hepatic encephalopathy), and for wound healing.
Both citrulline and ornithine occurs in the liver and take part
in the formation of urea from NH3.
Β-Alanine
It is a part of the molecule of a vitamin called pantothenic acid
Pantothenic acid
It is a widely distributed vitamin and forms a part of the molecule of
Coenzyme A which in turn take part in many metabolic reactions
Gamma-Aminobutyric Acid (GABA)
It occurs in brain and other tissues. It act as a neurotransmitter
Dihydroxyphenylalanine (DOPA)
It is formed in tissues during metabolism of phenylalanine and tyrosine.
L-Dopa is used in treating parkinsonism because in brain it give rise to a
neurotransmitter called dopamine. It is abbreviated as Dopa because it
is also called dioxyphenylalanine.
Homocysteine
Homocysteine is a common amino acid in your blood. You get it mostly
from eating meat. High levels of it are linked to early development of
heart disease. In fact, a high level of homocysteine is a risk factor for
heart disease. It is associated with low levels of vitamins B6, B12, and
folate, as well as renal disease
Iodinated Amino Acids
It includes mono- iodotyrosine (MIT), di-iodotyrosine (DIT), tri-
iodothyronine (T3) and tetra-iodothronine (T4). T3 and T4 are thyroid
hormones, while the MIT and DIT are intermediates molecules in their
synthesis.
Classification of Proteins
Proteins Classification
Based on physiochemical properties, proteins are classified into
following types:

1. Simple Proteins
2. Compound or Conjugated Proteins
3. Derived Proteins
Simple Proteins
• These proteins on hydrolysis yield only amino acids or their
derivatives.
• These includes
1. Albumins,
2. Globulins,
3. Globins
4. Prolamin
5. Histones
6. Protamines
7. Albuminoids
Albumin
• Albumin is a family of globular proteins, the most common of which
are the serum albumin. Other includes ovalbumin and lactalbumin.
• All the proteins of the albumin family are water-soluble, moderately
soluble in concentrated salt solutions, and experience heat
denaturation.
• They can also be precipitated by full saturation with ammonium
sulphate.
• Albumin is a protein made by your liver. It helps keep fluid in your
bloodstream so it doesn't leak into other tissues. It also carries
various substances throughout your body, including hormones,
vitamins, and enzymes. Low albumin levels can indicate a problem
with your liver or kidneys.
Globulins
• These are insoluble in water but soluble in dilute salt solution and are
heat coagulable.
• Found in animals (lactoglobulins, myosin, ovoglobulin, serum
globulins) and plants (legumin).
• These are easily coagulated compared to albumin and that’s why can
be precipitated by half-saturation with ammonium sulphate. This half-
saturation can be used to separate albumins from globulins-salting
out processes.
• They are made in your liver by your immune system. Globulins play
an important role in liver function, blood clotting, and fighting
infection
Globins
• The globins are a superfamily of heme-containing globular proteins,
involved in binding and/or transporting oxygen. Two prominent
members include myoglobin and hemoglobin.
• Globins are rich in histidine but are not basic
• They combine with heme to form hemoglobin. Hemoglobin of
different species are different only with respect to globin part, heme
part is same in all cases.
• Myoglobin is a small protein found in heart and skeletal muscles that
binds oxygen. It traps oxygen within muscle cells, allowing the cells to
produce the energy required for muscles to contract. When heart or
skeletal muscle is injured, myoglobin is released into the blood.
Prolamins
• Prolamins are a group of plant storage proteins having a high proline
amino acid content but deficient in lysine. They are found in plants,
mainly in the seeds of cereal grains such as wheat (gliadin), barley
(hordein), rye (secalin), corn (zein), sorghum (kafirin), and oats
(avenin).
• They are soluble in 70-80% ethanol but insoluble in water and
absolute alcohol.
Histones
• Histones are a family of basic proteins that associate with DNA in the
nucleus and help condense it into chromatin, they are alkaline (basic
pH) proteins, and their positive charges allow them to associate with
DNA.
• They are found inside the nucleus of eukaryotic cells. The association
of DNA and histones form a complex called nucleosomes (10 nm
diameter), in which DNA strand wind around a core of histone
molecule.
• These proteins are rich in arginine, contain little or no tryptophan but
tyrosine is present in their molecules.
• These are soluble in water but not in ammonium hydroxide.
Protamines
• These proteins are present in sperm cells and are small in size and
basic in nature.
• These resembles histones but unlike them are soluble in ammonium
hydroxide.
• Like histones, they form nucleoproteins with nucleic acids and are
rich in arginine.
• Protamines lack in both tyrosine and tryptophan.
Albuminoids
• These are called scleroproteins and occurs only in animals and do not
occurs in plants.
• These proteins include;
• Collagen (found in connective tissue)
• Elastin (found in connective tissue)
• Keratin (found in nails, hairs, hoofs, horns etc.)
Collagen
• Collagen is the most abundant protein in your body.
• It is the major component of connective tissues that make up several
body parts, including tendons, ligaments, skin, and muscles.
• Collagen has many important functions, including providing your skin
with structure and strengthening your bones.
• You can think of it as the “glue” that holds all these things together. In
fact, the word comes from the Greek word “kólla,” which means glue.
• There are also several foods you can eat to increase your collagen
intake, including bone broth.
• Consuming collagen may have a variety of health benefits, from
relieving joint pain to improving skin health
Important functions of collagen
1. Can improve skin health
Collagen may help slow the aging of your skin. However, stronger evidence is
needed from studies examining the effects of collagen on its own.
2. Helps relieve joint pain
• Collagen has been shown to reduce inflammation in the body. This may
help promote pain relief among people with joint disorders like
osteoarthritis.
• Collagen helps maintain the integrity of your cartilage, which is the rubber-
like tissue that protects your joints.
• As the amount of collagen in your body decreases as you get older, your
risk of developing degenerative joint disorders such as osteoarthritis
increases (9).
• Some studies have shown that taking collagen supplements may help
improve symptoms of osteoarthritis and reduce joint pain overall.
• In one study, 73 athletes who consumed 10 grams of collagen daily for
24 weeks experienced a significant decrease in joint pain while walking
and at rest, compared with a group that did not take it.
• In another study, adults took 2 grams of collagen daily for 70 days. Those
who took collagen had a significant reduction in joint pain and were
better able to engage in physical activity than those who did not take it.
• Researchers have theorized that supplemental collagen may accumulate
in cartilage and stimulate your tissues to make collagen.
• They have suggested this may lead to lower inflammation, better
support of your joints, and reduced pain.
• If you want to try taking a collagen supplement for its potential pain-
relieving effects, studies suggest you should start with a daily dosage of
8–12 grams.
3. Could prevent bone loss
• Your bones are made mostly of collagen, which gives them structure and helps
keep them strong.
• Just as the collagen in your body deteriorates as you age, so does bone mass. This
may lead to conditions like osteoporosis, which is characterized by low bone
density and linked to a higher risk of bone fractures.
• Studies have shown that taking collagen supplements may have certain effects in
the body that help inhibit the bone breakdown that leads to osteoporosis.
• In one study, women took either a calcium supplement combined with 5 grams of
collagen or a calcium supplement and no collagen daily for 12 months.
• By the end of the study, the women taking the calcium and collagen supplement
had significantly lower blood levels of proteins that promote bone breakdown
than those taking only the calcium.
• Another study found similar results in 66 women who took 5 grams of collagen
daily for 12 months.
• The women who took the collagen showed an increase of up to 7% in
their bone mineral density (BMD), compared with women who did
not consume collagen.
• BMD is a measure of the density of minerals, such as calcium, in your
bones. Low BMD is associated with weak bones and the development
of osteoporosis.
• These results are promising, but more human studies are needed
before the role of collagen supplements in bone health can be
confirmed.
4. Could boost muscle mass
• Between 1–10% of muscle tissue is composed of collagen. This protein is
necessary to keep your muscles strong and functioning properly.
• Studies suggest that collagen supplements help boost muscle mass in
people with sarcopenia, the loss of muscle mass that happens with age.
• In one study, 27 frail men took 15 grams of collagen while participating in
an exercise program daily for 12 weeks. Compared with men who exercised
but did not take collagen, they gained significantly more muscle mass and
strength.
• Researchers have suggested that taking collagen may promote the
synthesis of muscle proteins like creatine, as well as stimulate muscle
growth after exercise.
5. Promotes heart health
• Researchers have theorized that taking collagen supplements may help reduce
the risk of heart-related conditions.
• Collagen provides structure to your arteries, which are the blood vessels that
carry blood from your heart to the rest of your body. Without enough collagen,
arteries may become weak and fragile.
• This may lead to atherosclerosis, a disease characterized by the narrowing of the
arteries. Atherosclerosis has the potential to lead to heart attack and stroke.
• In one study, 31 healthy adults took 16 grams of collagen daily for 6 months. By
the end, they had experienced a significant reduction in measures of artery
stiffness, compared with before they started taking the supplement.
• Additionally, they increased their levels of HDL “good” cholesterol by an average
of 6%. HDL is an important factor in the risk of heart conditions, including
atherosclerosis.
• Nevertheless, more studies on the role of collagen supplements in heart health
are needed.
 6. Other health benefits
• Collagen supplements may have other health benefits, but these have not been studied
extensively.
• Hair and nails. Taking collagen may increase the strength of your nails by preventing
brittleness. Additionally, it may stimulate your hair and nails to grow longer.
• Gut health. Although there is no scientific evidence to support this claim, some health
practitioners promote the use of collagen supplements to treat intestinal permeability,
or leaky gut syndrome.
• Brain health. No studies have examined the role of collagen supplements in brain
health. However, some people claim they improve mood and reduce symptoms of
anxiety.
• Weight loss. Some believe that taking collagen supplements may promote weight loss
and a faster metabolism. There have not been any studies to support these claims.
• Although these potential effects are promising, more research is needed before formal
conclusions can be made.
Elastin
• Elastin is a key protein of the extracellular matrix. It is highly elastic
and present in connective tissue allowing many tissues in the body to
resume their shape after stretching or contracting.
• Elastin helps skin to return to its original position when it is poked or
pinched.
• Elastic tissues is a mixture of elastin, collagen and a carbohydrate
containing protein called elastomucin.
• Elastin has characteristic non-standard aminoacids called desmosin
and isodesmosin which are derived from lysine.
Keratin
• Keratin is the type of protein that makes up your hair, skin, nails, horns,
hoofs, feathers, tortoise shell etc.
• Keratin can also be found in your internal organs and glands.
• Keratin is a protective protein, less prone to scratching or tearing than
other types of cells your body produces.
• Unlike collagen and elstin which are extracellular, keratin is found within
the cell.
• It has high cysteine content and forming cross links between peptide
chains.
• It is insoluble in water, organic solvents, dilute acids and alkalies.
• Chemically, keratin is quite inert and resistant.
Compound or Conjugated Proteins
• In these molecules the protein is attached or conjugated to some
non-protein groups which are called prosthetic groups. For
example, phospho-proteins are conjugated with phosphoric
acid; lipoproteins are conjugated with lipid substances like lecithin,
cholesterol and fatty acids.
• Conjugated proteins are proteins that contain non-protein
constituents or prosthetic groups. The prosthetic groups are
permanently associated with the molecule, usually through covalent
and/or non-covalent linkages with the side chains of certain amino
acids
Major Classes of Conjugated Proteins
Conjugated proteins can be divided into three major classes:

(1) Chromo proteins

(2) Glycoproteins
(3) Lipoproteins
(4) Nucleoproteins
(5) Metalloproteins
Mucoproteins and glycoproteins
• The prosthetic groups in mucoproteins and glycoproteins are
oligosaccharides usually contain 4-12 sugar molecules;
• The most common sugars are galactose, mannose, glucosamine, and
galactosamine. Xylose, fucose, glucuronic acid, sialic acid, and other
simple sugars sometimes also occur.
• Some mucoproteins contain 20 percent or more of carbohydrate,
usually in several oligosaccharides attached to different parts of the
peptide chain.
• The designation mucoprotein is used for proteins with more than 3
to 4 percent carbohydrate; if the carbohydrate content is less than 3
percent, the protein is sometimes called a glycoprotein.
A number of very important proteins fall in this class, including
many of the blood plasma proteins and a large number of enzymes
and hormones.
The surfaces (i.e., plasma membranes)
of most cells also contain quantities of
glycoproteins, and these molecules serve
there as antigenic determinants and as
receptor sites. Virtually all of the
carbohydrate that is present in red blood
cells occurs as membrane glycoproteins.
Although more than 100 different sugars (or
mono-saccharides) are known, only about
nine occur as regular constituents of glyco-
proteins.
The amount of carbohydrate present in glycoproteins varies from less than
1% of the molecule’s total molecular weight to more than 85%. For example,
in egg white ovalbumin (molecular weight 45,000), there is only one
monosaccharide per protein molecule, whereas in mucin (a secretion of the
salivary glands having a molecular weight of about 1 million), about 800
mono-saccharides are present.
The carbohydrate moieties of glycoproteins are usually bound
to the protein through covalent bonds with either asparagine,
threonine, hydroxylysine, serine, or hydroxyproline.

The carbohydrate bonded at each site of the protein may

consist of a single monosaccharide unit OR a linear or
branched chain of several mono saccharides (called an
oligosaccharide).
Mucoproteins, highly viscous proteins originally called
mucins, are found in saliva, in gastric juice, and in other
animal secretions.
Mucoproteins occur in large amounts in cartilage, synovial
fluid (the lubricating fluid of joints and tendons), and egg
white.
The mucoprotein of cartilage is formed by the combination
of collagen with chondroitinsulfuric acid, which is a
polymer of either glucuronic or iduronic acid and
acetylhexosamine or acetylgalactosamine.
Lipoproteins
• Lipid-containing proteins are called lipoproteins. Lipid substances
includes; lecithin, cholesterol, triglycerides and fatty acids. This class
includes some of the blood plasma proteins’ and also a large number
of membrane proteins.
• The lipid content of lipoproteins is often very high, accounting for as
much as 40 to 90% of the total molecular weight of the complex.
• These occurs in blood plasma, cell membranes, nervous system, egg
yolk and milk. Bacterial antigens and viruses also contain lipoproteins.
In lipoproteins, the amount of lipid present markedly affects the
density of the molecule, and this property is often used as the
basis for lipoprotein classification and are usually classified as low-
and high-density lipoproteins (LDL and HDL). Un-complexed
proteins have a density in water of about 1.35, lipoproteins vary in
density down to 0.9 (i.e., a lipoprotein may be less dense than
water).
Metalloproteins
• Proteins in which heavy metal ions are bound directly to some of the side
chains of histidine, cysteine, or some other amino acid are called
metalloproteins.
• Two metalloproteins, transferrin and ceruloplasmin, occur in the globulin
fractions of blood serum; they act as carriers of iron and copper,
respectively. Carbonic anhydrase, carries zinc.
• Transferrin has a molecular weight of about 80,000 and consists of two
identical subunits, each of which contains one ferric ion (Fe3+) that seems
to be bound to tyrosine. Several genetic variants of transferrin are known
to occur in humans.
• Another iron protein, ferritin, which contains 20 to 22 percent iron, is the
form in which iron is stored in animals; it has been obtained in crystalline
form from liver and spleen. A molecule consisting of 20 subunits, its
molecular weight is approximately 480,000. The iron can be removed by
reduction from the ferric (Fe3+) to the ferrous (Fe2+) state. The iron-free
protein, apoferritin, is synthesized in the body before the iron is
incorporated.
• Ceruloplasmin is a copper-containing globulin that has a
molecular weight of 151,000; the molecule consists of eight
subunits, each containing one copper ion.
• Ceruloplasmin is the principal carrier of copper in organisms,
although copper can also be transported by the iron-containing
globulin transferrin.
Nucleoproteins
• When a protein solution is mixed with a solution of a nucleic acid,
the phosphoric acid component of the nucleic acid combines with the
positively charged ammonium groups (―NH3+) of the protein to form
a protein–nucleic acid complex. The nucleus of a cell contains
predominantly deoxyribonucleic acid (DNA) and
the cytoplasm predominantly ribonucleic acid (RNA); both parts of
the cell also contain protein. Protein–nucleic acid complexes,
therefore, form in living cells.
• Two types of proteins have been identified in nucleoproteins, the
histones and non-histones. Histones have a rather restricted amino
acid composition (containing about 25% arginine and lysine) and are
quite similar in all plant and animal cells.
Their highly basic nature accounts for the close associations they form
with the nucleic acids and are involved in the tight packing of DNA
molecules during the condensation of chromatin (i.e., chromosomes)
that precedes mitosis.

The non-histones are considerably more heterogeneous in amino acid

composition and have acidic properties. There is much evidence to
suggest that by selectively combining with certain stretches of nuclear
DNA, the non-histones are involved in the regulation of gene expres-
sion.
Nucleoprotamines, and nucleohistones are the examples.
Chromaproteins
• The chromo proteins are a heterogeneous group of conjugated
proteins related to each other only in that they all possess color.
• Simply these are compounds of proteins with pigments such as heme
and include hemoglobin and cytochromes. Some enzymes are also
included such as flavoproteins and rhodopsin containing riboflavin
and vitamin A prosthetic groups.
• The hemoglobin’s, myoglobin’s, and other heme-containing proteins
such as the cytochromes and hemerythrins belong to this group. The
prosthetic groups of the chromo proteins, such as the heme groups of
hemoglobin and the cytochromes, are bound to the polypeptide
portion of the molecule through a combination of covalent and non
covalent bonds.
Although the heme proteins contain iron, they are usually not
classified as metalloproteins, because their prosthetic group is an
iron-porphyrin complex in which the iron is bound very firmly.
The intense red or brown colour of the heme proteins is not caused
by iron but by porphyrin, a complex cyclic structure.

Another chromoprotein i.e., melanin, a pigment found in dark

skin, dark hair, and melanotic tumours, occurs in every major
group of living organisms and appears to be remarkably diverse in
structure. In humans, melanin produced by melanocytes may be
dark brown (eumelanin) or pale red or yellowish (phaeomelanin).
The different types are synthesized via different pathways, though
they share the same initial step—the oxidation of tyrosine.
Green chromoproteins called biliproteins are found in
many insects, such as grasshoppers, and also in the eggshells of
many birds.
The biliproteins are derived from the bile pigment biliverdin,
which in turn is formed from porphyrin; biliverdin contains
four pyrrole rings and three of the four methine groups of
porphyrin. Large amounts of biliproteins have been found
in red algae and blue-green algae; the red protein is called
phycoerythrin, the blue one phycocyanobilin.
Derived Proteins
• These are proteins derived by partial to complete hydrolysis from the
simple or conjugated proteins by the action of acids, alkalies or enzymes.
• As the word “derived” is showing that this class of protein includes
substances which are derived from simple and conjugated proteins.
• These are parts of the proteins. They are obtained by breaking or
denaturation of the peptide bonds.

• They include two types of derivatives,

• Primary-derived proteins
• Secondary-derived proteins
Primary-derived proteins

• Those proteins which are obtained by the denaturation. Denaturation

is usually done by using alkalies, acids or heat etc.
• Native proteins: Those proteins if its amino acid composition and
molecular confirmation are unchanged from that found in the natural
state. These properties control all the functions of a protein.
• Denatured Proteins: Some or all of the cross linkages which keep the
molecular structure of the protein intact are split, although there is
no hydrolysis of the protein molecule.
• These are the first derived products of protein denaturation. Called as
denatured or coagulated proteins.
Denaturation in most of the cases is not reversible. However, in some
cases it may be reversible (renaturation) i.e., ribonuclease, in this case
all the properties which have been lost due to denaturation are
restored.
Denaturation may be brought about by many physical and chemical
agents such as
Heat
X-rays
Ultrasonic waves
Shaking or stirring of protein for long time
Extremes of PH
Salts of heavy metals
Urea, alcohol and acetone
Secondary Derived Proteins
• These are the intermediate products formed during the
progressive hydrolysis of protein molecule.
• Examples are proteoses, peptones, polypeptides and
oligopolypeptides.
1. Proteoses: Soluble in water, not coagulated by heat and
precipitated from their solutions by full saturation with
ammonium sulfate. Proteoses with higher molecular
weight are called primary-proteoses, and those having
smaller mol.wt are called secondary proteoses.
2. Peptones
These have simple structure than proteoses. Soluble in water, not
coagulated by heat and not precipitated from their solutions by full
saturation with ammonium sulfate. But are precipitated by
phosphotungstic acid.

3. Polypeptides: These results from the further hydrolysis of peptones.

The polypeptides in turn give rise to fragments of shorter chain lengths
called oligopeptides.
4. Oligopeptides
• These are composed of relatively few amino acid residues. They are
named according to the number of amino acid groups present.
• For example: dipeptides, tripeptides etc.
• They are water soluble and not coagulated by heat, and not salted
out of solution but are often precipitated by phosphotungstic acid
Lipids
Lipids Facts
• Lipids are organic compounds which are insoluble in water but
soluble in organic solvents such as benzene, chloroform, ether,
acetone etc.
• Their primary building blocks are fatty acids, glycerol, sphingosine
and sterols.
• Lipids can be utilized by the living organism.
• Lipids belongs to a heterogeneous group of substances and occurs
both in plant and animal tissues.
Lipids Classification
Lipids are divided into three main groups;
1. Simple lipids
1. Waxes
2. Fats
2. Compound/Complex lipids
1. Phospholipids
2. Glycolipids
3. Sulfolipids
4. Lipoproteins
5. Gangliosides
3. Derived, Precursor and Associated Lipids:
1. Diglycerides
2. Fatty acids
3. Alcohols including glycerol
4. Sterols
5. Vitamin D, E, K
6. Caretenoids
7. Eicosanoids
1. Prostacyclins
2. Prostaglandins
3. Thromboxanes
4. Leukotrienes
5. Lipoxins
8. Terpenes
Simple Lipids
• These lipids includes fats and waxes. Fats are esters of fatty acids with
glycerol. Fats are also called neutral fat, or triglyceride
(triacylglycerol). Whereas,

• Waxes are esters of fatty acids with alcohol other than glycerol
(higher molecular weight monohydric alcohols)
Compound Lipids
These are esters of fatty acids containing groups in addition to an
alcohol and a fatty acid. For example, the additional group in
phospholipids are phosphoric acid residue.
• Phospholipids = Alcohol, fatty acid, and phosphoric acid residue.
Additional groups may also be N-containing bases and other
substituents. Based on alcohol, these can be divided into
glycerophospholipids and sphingophospholipids.
• Glycolipids = sphingosine, fatty acid and a carbohydrate
• Sulfolipids = sphingosine, fatty acid, sugar and sulfate group
• Gangliosides = sphingosine, fatty acid, sugar units, N-acetyl
hexosamine and N-acetylneuraminic acid.
• Lipoproteins = complexes of lipids with proteins.
Derived, precursor and associated lipids
• These are the hydrolytic products of simple and compound lipids
Fatty Acids
 Fatty Acids
• Fatty acids are long-chain carboxylic acids ranging mostly in chain length from 4-
24 carbon atoms. With some exceptions, they contain even number of carbon
atoms and the majority containing 16 and 18 carbon atoms.
• In waxes, fatty acids contain up to 34 carbon atoms, whereas waxes extracted
from a bacteria (Tubercle bacilli) have very complex fatty acids containing
around 90 carbon atoms.
• Fatty acids are insoluble in water, and may be saturated or unsaturated.
Naturally occurring saturated fatty acids below 8 carbons are liquid at room
temperature.

• Simply, Fatty acids are aliphatic carboxylic acids having a general formula R-
COOH, where R represents a hydrocarbon chain. Fatty acids are not found in a
free state in nature; commonly they exist in combination with glycerol (an
alcohol) in the form of triglyceride.
Fatty Acid Formulas
The formulas for fatty acids are written as
• Condensed formulas.
• Line-bond formulas.
• For example caprylic acid with 8 carbon atoms.
O

CH3—(CH2)6—COOH OH

CH3—CH2—CH2—CH2—CH2—CH2—CH2—COOH
Types of fatty acids

Fatty acids are classified on the basis of;

1. No of carbon atoms

2. Even and odd chain

3. Types of bonds in the chain

1. Saturated FA
2. Unsaturated FA
1. Monounsaturated FA
2. Polyunsaturated FA
Saturated Fatty acids
If the carbon atoms have a single bond between them and as many
hydrogen atoms as possible are bonded to the carbon atoms, then it is
said to be saturated. E.g. Palmitic acid and stearic acid.
Saturated fatty acids have
• Single C–C bonds.
• Fit closely together in a regular pattern.
• Strong attractions between fatty acid chains.
• High melting points that make them solids at room temperature.
Unsaturated Fatty Acids
If the bond between the carbon atoms is a double bond and the
molecule can absorb more hydrogen atoms. Or, in other words, those
fatty acid in which there are one or more double bonds in the
hydrocarbon chain. E.g. Linoleic acid and Linolenic acid.
Unsaturated fatty acids
• Have one or more double C=C bond
• Typically contain cis double bonds.
Properties of Unsaturated Fatty Acids
“kinks” in
Unsaturated fatty acids chain
• Have “kinks” in the fatty acid chains.
• Do not pack closely.
• Have few attractions between chains.
• Have low melting points.
• Are liquids at room temperature.
Monounsaturated Fatty Acid

Polyunsaturated Fatty Acid

Physical properties of fatty acids
Water-solubility
The length of the carbon chain in a fatty acid is important in
determining things like water-solubility and melting/boiling points.
• Long carbon chains are non-polar, and things with long carbon chains
on them do not dissolve in water.
• Short chain fatty acids are slightly water-soluble, because the carboxyl
group (-COOH) is polar.
Melting point
Melting points also increase with increasing molar mass, so the longer the
carbon chain, the higher the melting point of the fatty acid.
The presence of double bonds lowers the melting point (makes it easier for the
fatty acid to melt) because these double bonds cause the molecule to become
bent (less attractions between chains).
Comparing Melting Points of Some FA
Chemical Properties of Fatty Acids
Fatty acids are used not only in the production of numerous food
products but also in soaps, detergents, and cosmetics.
1. Formation of Salts-Soaps:
Soaps are the sodium, potassium, calcium and magnesium salts of fatty
acids. Fatty acids form salts when they are treated with alkali metals
and alkaline earth metals.
Soaps are sodium or potassium salts of long chain fatty acids. When
triglycerides in fat/oil react with aqueous NaOH or KOH, they are
converted into soap and glycerol. Since this reaction leads to
the formation of soap, it is called the Saponification process.
General Representation of Soap
The soap molecule has two parts:
• a polar group (-COO-Na+) and a non-polar group (R-hydrocarbon part).
• The polar group is called the head and the non-polar group is called
the tail. Thus, the soap molecule has a polar head and a non-polar
hydrocarbon tail. The polar head is hydrophilic in nature (water
loving) and the non-polar tail is hydrophobic (water repelling) in
nature.
The saponification reaction is exothermic in nature, because heat is
liberated during the process. The soap formed remains in suspension form
in the mixture. Soap is precipitated as a solid from the suspension by
adding common salt to the suspension. This process is called Salting out of
Soap.
Types of Soap
Depending upon the nature of alkali used in the production of soap, they
are classified into two types.
1. Hard soap: The sodium salt of long chain fatty acid is known as hard
soap. It is difficult to dissolve in water. It is used as laundry soap.
2. Soft soap: The potassium salt of long chain fatty acid is known as soft
soap, as it produces more lather. It is used as toilet soap and shaving
soap.
In aqueous solution, soap ionizes to form alkali ions.

Since soaps have free alkali ions, they are alkaline in nature.
Hence, the soap solutions are slippery to the touch.
Formation of detergents
• Reduction of carboxyl group of fatty acids produce alkyl alcohols which can
be sulfated or sulfonated to form alkyl sulfates or sulfonates which acts as
detergents.
• Unlike soaps, detergents are stable in acidic solutions and do not form
insoluble salts with calcium or magnesium. They can therefore be used for
washing clothes in hard water.
• Detergents are good cleansers because they are efficient wetting agents
and emulsifiers.
• Hard water... is water that contains an appreciable quantity of dissolved
minerals (like calcium and magnesium).
• Soft water... is treated water in which the only ion is sodium.
Formation of esters
• The most chemically reactive portion of fatty acids is the acidic
carboxyl group (COOH). It reacts with alcohols (R′OH) to form
products known as esters (RCOOR′) and releases water in the process.
This ester bond is the principal covalent bond linking fatty acid
moieties to other groups.

• In combination with alcohols, fatty acids form esters.

Formation of eicosanoids
The term eicosanoid is used to embrace those biologically active lipid
mediators derived primarily from three C20 polyunsaturated fatty
acids, and includes;
prostaglandins, thromboxanes, leukotrienes, and lipoxins.
Three C20 polyunsaturated fatty acids are;
1. Dihomo-gamma linoleic acid (eicosatrienoic acid 20:3 8, 11, 14.
2. Arachidonic acid (eicosatetraenoic acid 20:4 5, 8, 11, 14.
3. Eicosapentanoic acid 20:5 5, 8, 11, 14, 17.
Important Reactions of Unsaturated
Fatty Acids
Hydrogenation of unsaturated fatty acids
The hydrocarbon part of a fatty acid molecule is quite
resistant to chemical attack unless carbon-carbon double
bonds are present.
A number of different kinds of molecules react with such a
double bond.
For example, when a catalyst such as platinum is present,
hydrogen gas adds to the double bond to give a saturated
fatty acid.
Halogenation
Halogens (chlorine, bromine, and iodine) and their
derivatives such as hydroiodic acid (HI) also react with
the double bond to form saturated fatty acids.

But in these cases one or two atoms of the halogen

replace one or two of the hydrogens.
Oxidation
• Carbon-carbon double bonds can also react with oxygen in
either non-enzymatic processes or enzymatically catalyzed
oxidation reactions.
• This process generates a variety of products, some of which
contribute to the rancid smell in spoiled meat and vegetable
products.
• In general, the more highly unsaturated the fatty acid, the
more easily it is oxidized.
Essential & Non-Essential
Fatty Acids
Chemically, a fatty acid is an organic acid that has an acid group
at one end of its molecule, and a methyl group at the other end.
The term essential fatty acid refers to a fatty acid which the body
cannot manufacture, and must obtain from dietary sources.
These essential fatty acids were originally designated as Vitamin
F, until it was realized that they must be classified with the fats.
There are two fatty acids designated as essential fatty acids:
linoleic acid and alpha-linolenic acid.
It is important to note that nonessential fatty acids doesn’t mean
unimportant; the classification is based solely on the ability of the
body to synthesize the fatty acid.
Essential fatty acids must be obtained from food. They fall into two
categories—omega-3 and omega-6. The 3 and 6 refer to the position of
the first carbon double bond and the omega refers to the methyl end of
the chain. Omega-3 and omega-6 fatty acids are precursors to
important compounds called eicosanoids.
Eicosanoids are powerful hormones that control many other hormones
and important body functions, such as the central nervous system and
the immune system.
Eicosanoids derived from omega-6 fatty acids are known to increase
blood pressure, immune response, and inflammation.
In contrast, eicosanoids derived from omega-3 fatty acids are known to
have heart-healthy effects. Given the contrasting effects of the omega-
3 and omega-6 fatty acids, a proper dietary balance between the two
must be achieved to ensure optimal health benefits.
Essential fatty acids play an important role in the life and death
of cardiac cells, immune system function, and blood pressure
regulation.
Docosahexaenoic acid (DHA) is an omega-3 essential fatty acid
shown to play important roles in synaptic transmission in the
brain during fetal development.
Roles of essential fatty acids (EFAs)
• The body uses essential fatty acids (EFAs) for the formation of healthy
cell membranes, the proper development and functioning of the
brain and nervous system, and for the production of hormone-like
substances called eicosanoids (thromboxanes, leukotrienes,
prostaglandins). These chemicals regulate numerous body functions
including blood pressure, blood viscosity, vasoconstriction, immune
and inflammatory responses.
• Dietary sources of the omega 6 fatty acids include some leafy
vegetables, seeds nuts, grains, vegetable oils and meats.
• Dietary sources of the omega 3 fatty acids include some vegetable
oils, nuts and seeds, shellfish and fish.
Eicosapentaenoic acid (EPA) and docosahexanaeoic acid (DHA) are
omega 3 fatty acids (O3FA). Mostly found in oils of cold water fish:
Salmon, sardines, sardines, herring, and mackerel.
Therapeutic applications for O3FA includes;
• cardiovascular-enhancing and anti-inflammatory benefits.
• It reduces the risk of atherosclerosis, increases “good” HDL
cholesterol, while decrease “bad” LDL cholesterol and triglycerides,
• decreases high blood pressure.
• O3FA have also been shown to block the production of
certain inflammatory chemicals in our body and is used to
reduce inflammation in rheumatoid arthritis, asthma, colitis,
Crohn’s disease, and Lupus.
• In addition, O3FA have shown to reduce the symptoms of
other disorders including angina, migraine headaches,
psoriasis, and tinnitus.
Flax seed naturally contain a complex of different categories of fatty
acids, including alpha-linolenic acid (omega-3), linoleic acid (omega-
6), and oleic acid (omega-9).

Much of Flax seed’s benefits are a function of its alpha linolenic acid
(ALA) content, and the fact that ALA can be converted by the body
into EPA—the same omega-3 found in fish oil. As a matter of fact
research has found that supplementation with Flax seed oil can
effectively increase EPA concentrations in tissues.
Studies involving Flax seed have been conducted on its anti-
inflammatory properties, its anti-lupus properties, and its
cardiovascular enhancing properties.

Omega 9 fatty acid-oleic acid has been shown in research to

lower heart attack risk and arteriosclerosis, and aids in the
prevention of breast cancer.
Functions of Omega-3 Fatty Acids
1. Omega-3s Can Fight Depression and Anxiety
Omega-3 supplements may help prevent and treat depression and
anxiety. EPA seems to be the most effective at fighting depression.
2. Omega-3s Can Improve Eye Health
An omega-3 fatty acid called DHA is a major structural component of
your eyes’ retinas. It may help prevent macular degeneration, which
can cause vision impairment and blindness.
3. Promote Brain Health During Pregnancy and Early Life
DHA accounts for 40% of the polyunsaturated fatty acids in your brain
and 60% in the retina of your eye.
Getting enough omega-3s during pregnancy is associated with
numerous benefits for your child, including
•Higher intelligence
•Better communication and social skills
•Fewer behavioral problems
•Decreased risk of developmental delay
•Decreased risk of ADHD, autism and cerebral palsy
4. Improve Risk Factors for Heart Disease
Decreases triglycerides by 15-30%
Lowers blood pressure
Raises good “HDL” cholesterol
Keep blood from clumping together. Prevent clots
By keeping your arteries smooth and free from damage, omega-3s help
prevent the plaque that can restrict and harden your arteries
5. Reduce Symptoms of ADHD in Children
Attention deficit hyperactivity disorder (ADHD) is a behavioral disorder
characterized by inattention, hyperactivity and impulsivity. Omega-3
supplements can reduce the symptoms of ADHD in children. They improve
attention and reduce hyperactivity, impulsiveness and aggression.
6. Reduce Symptoms of Metabolic Syndrome
Metabolic syndrome is a collection of conditions. It includes central obesity
— also known as belly fat — as well as high blood pressure, insulin
resistance, high triglycerides and low “good” HDL cholesterol levels. It is a
major public health concern because it increases your risk of many other
illnesses, including heart disease and diabetes.
Omega-3s can have numerous benefits for people with metabolic syndrome.
They can reduce insulin resistance, fight inflammation and improve several
heart disease risk factors.
7. Can Fight Inflammation
Inflammation is a natural response to infections and damage in your body. Therefore, it is
vital for your health. However, inflammation sometimes persists for a long time, even
without an infection or injury. This is called chronic — or long-term — inflammation.
Long-term inflammation can contribute to almost every chronic Western illness, including
heart disease and cancer. Notably, omega-3 fatty acids can reduce the production of
molecules and substances linked to inflammation, such as inflammatory eicosanoids and
cytokines. Studies have consistently observed a connection between higher omega-3
intake and reduced inflammation.
8. Fight Autoimmune Diseases
In autoimmune diseases, your immune system mistakes healthy cells for foreign cells and
starts attacking them. Type 1 diabetes is one prime example, in which your immune
system attacks the insulin-producing cells in your pancreas. Omega-3s can combat some
of these diseases and may be especially important during early life.
Studies show that getting enough omega-3s during your first year of life is
linked to a reduced risk of many autoimmune diseases, including type 1
diabetes, autoimmune diabetes and multiple sclerosis. Omega-3s also help
treat lupus, rheumatoid arthritis, ulcerative colitis, Crohn’s disease and
psoriasis.
9. Improve Mental Disorders
People with mental disorders often have low blood levels of omega-3 fats.
Improving omega-3 status seems to improve symptoms. It also prevent age
related mental decline and Alzheimer’s disease.
10. Help Prevent Cancer
Omega-3 intake may decrease the risk of some types of cancer, including
colon, prostate and breast cancer. Interestingly, studies show that people
who consume the most omega-3s have up to a 55% lower risk of colon
cancer.
11. Omega-3s Can Reduce Asthma in Children
Asthma is a chronic lung disease with symptoms like coughing, shortness of
breath and wheezing.
Severe asthma attacks can be very dangerous. They are caused by
inflammation and swelling in the airways of your lungs. Omega-3 intake has
been associated with a lower risk of asthma in both children and young
adults.
12. Reduce Fat in Your Liver
Non-alcoholic fatty liver disease (NAFLD) However, supplementing with
omega-3 fatty acids effectively reduces liver fat and inflammation in people
with Non-alcoholic fatty liver disease (NAFLD)
13. Improve Bone and Joint Health
Omega-3s may improve bone strength and joint health, potentially reducing
your risk of osteoporosis and arthritis.

14. Alleviate Menstrual Pain

Menstrual pain occurs in your lower abdomen and pelvis and often radiates
to your lower back and thighs. It can significantly affect your quality of life.

However, studies repeatedly prove that women who consume the most
omega-3s have milder menstrual pain. One study even determined that an
omega-3 supplement was more effective than ibuprofen in treating severe
pain during menstruation.
15. Improve Sleep
Good sleep is one of the foundations of optimal health. Studies tie sleep
deprivation to many diseases, including obesity, diabetes and depression.
Low levels of omega-3 fatty acids are associated with sleep problems in
children and obstructive sleep apnea in adults. Low levels of DHA are also
linked to lower levels of the hormone melatonin, which helps you fall
asleep.
Studies in both children and adults reveal that supplementing with omega-3
increases the length and quality of sleep.

16. Omega-3 Fats Are Good For Your Skin

DHA is a structural component of your skin. It is responsible for the health of
cell membranes, which make up a large part of your skin. A healthy cell
membrane results in soft, moist, supple and wrinkle-free skin.
EPA also benefits your skin in several ways, including:
• Managing oil production and hydration of your skin.
• Preventing hyper keratinization of hair follicles, which appears as the
little red bumps often seen on upper arms.
• Reducing premature aging of your skin.
• Reducing the risk of acne.
• Omega-3s can also protect your skin from sun damage. EPA helps
block the release of substances that eat away at the collagen in your
skin after sun exposure.
Omega-3 fatty acids are vital for optimal health. Getting them from
whole foods — such as fatty fish two times per week — is the best
way to ensure robust omega-3 intake. However, if you don’t eat a lot
of fatty fish, then you may want to consider taking an omega-3
supplement. For people deficient in omega-3, this is a cheap and
highly effective way to improve health.
Omega Classification
This classification is based on the numbering of a fatty acid chain from
hydrocarbon chain. Means the numbering will starts from the hydrocarbon
chain side while not from the carboxylic end.
Classified into three classes
1. Omega-3 FA
1. α-Linolenic Acid (ALA)
2. Eicosapentaenoic acid (EPA)
3. Docosahexaenoic Acid (DHA)
2. Omega-6 FA
1. Gamma-linolenic acid (GLA)
2. Linoleic acid
3. Arachidonic acid
3. Omega-9 FA
1. Oleic Acid
What are omega-3 fatty acids?
• The term “polyunsaturated” refers to their chemical structure, as “poly”
means many and “unsaturated” refers to double bonds. Together they
mean that omega-3 fatty acids have many double bonds.
• “Omega-3” refers to the position of the final double bond in the chemical
structure, which is three carbon atoms from the “omega,” or tail end of the
molecular chain.
• Since the human body can’t produce omega-3s, these fats are referred to
as “essential fats,” meaning that you have to get them from your diet.
• The American Heart Association (AHA) recommends eating at least two
portions of fish per week, particularly oily fish, which is rich in omega-3
fatty acids.
1. Eicosapentaenoic acid (EPA): This 20-carbon fatty acid’s main
function is to produce chemicals called eicosanoids, which help
reduce inflammation. EPA may also help reduce symptoms of
depression.
2. Docosahexaenoic acid (DHA): A 22-carbon fatty acid, DHA makes
up about 8% of brain weight and contributes to brain
development and function.
3. Alpha-linolenic acid (ALA): This 18-carbon fatty acid can be
converted into EPA and DHA, although the process is not very
efficient. ALA appears to benefit the heart, immune system, and
nervous system.
Omega-3 fats are a crucial part of human cell membranes.
NOTE:

A low intake of omega-3 fatty acids compared with

omega-6s may contribute to inflammation and chronic
diseases, such as rheumatoid arthritis, diabetes,
atherosclerosis, and heart failure
What are omega-6 fatty acids?
• Like omega-3s, omega-6 fatty acids are polyunsaturated fatty acids.
However, the last double bond is six carbons from the omega end of the
fatty acid molecule.
• Omega-6 fatty acids are also essential, so you need to obtain them from
your diet. They mainly provide energy. The most common omega-6 fat is
linoleic acid, which the body can convert to longer omega-6 fats such as
arachidonic acid (AA).
• Like EPA, AA produces eicosanoids. However, the eicosanoids that AA
produces are more pro-inflammatory.
• Pro-inflammatory eicosanoids play a key role in the immune system.
However, when the body produces too many, they can increase the risk of
inflammation and inflammatory disease.
• A healthy ratio of omega-6 to omega-3 fatty acids appears to be between
1-to-1 and 4-to-1 but studies suggest that people who follow a typical
Western diet may consume a ratio of between 15-to-1 and almost 17-to-1.
Can Omega-6 be beneficial?
• Some omega-6 fatty acids have shown benefits in treating symptoms
of chronic disease.
• Gamma-linolenic acid (GLA) is an omega-6 fatty acid found in certain
oils, such as: evening primrose oil and borage oil
• When consumed, much of it is converted to another fatty acid called
dihomo-gamma-linolenic acid (DGLA).
• Research suggests that GLA and DGLA may have some health
benefits. For example, GLA may help reduce symptoms of
inflammatory conditions. However, more research is needed.
• The authors of one study concluded that taking supplements of
another form of omega-6 — conjugated linoleic acid (CLA) — may
help reduce fat mass in humans.
What are omega-9 fatty acids?
• Omega-9 fatty acids are monounsaturated, meaning they only have one
double bond. It’s located nine carbons from the omega end of the fatty
acid molecule.
• Oleic acid is the most common omega-9 fatty acid and the most common
monounsaturated fatty acid in the diet.
• Omega-9 fatty acids aren’t strictly “essential,” as the body can produce
them. However, consuming foods rich in omega-9 fatty acids instead of
other types of fat may have health benefits.
• A 2015 study found that feeding mice diets high in monounsaturated fat
improved insulin sensitivity and decreased inflammation.
• The same study found that humans who ate high monounsaturated fat
diets had less inflammation and better insulin sensitivity than those who
ate diets high in saturated fat.
Sources of EFAs
You can easily obtain omega-3, -6, and -9 fatty acids from your
diet, but you need the right balance of each. The typical Western
diet contains more omega-6 fats than necessary and not
enough omega-3 fats.
Foods high in omega-3 fats
Oily fish is the best source of omega-3s EPA and DHA. Other marine
sources include algal oils. ALA mainly comes from nuts and seeds.
There are no official standards for daily omega-3 intake, but experts
recommend an intake of 250–300 milligrams per day.

According to the Food and Nutrition Board of the U.S. Institute of

Medicine, the adequate intake of ALA omega-3s per day is 1.6 grams for
adult males and 1.1 grams for adult females aged 19 years and over.
Here are the amounts and types of omega-3s in one serving of
the following foods:

1. salmon: 4.0 grams EPA and DHA

2. mackerel: 3.0 grams EPA and DHA
3. sardines: 2.2 grams EPA and DHA
4. anchovies: 1.0 grams EPA and DHA
5. chia seeds: 4.9 grams ALA
6. walnuts: 2.5 grams ALA
7. flaxseeds: 2.3 grams ALA
Foods high in omega-6 fats
• High levels of omega-6 fats are present in refined vegetable oils and foods
cooked in vegetable oils. Nuts and seeds also contain significant amounts
of omega-6 fatty acids.
• According to the Food and Nutrition Board of the U.S. Institute of
Medicine, the adequate intake of omega-6s per day is 17 grams for males
and 12 grams for females ages 19–50 years.
Here are the amounts of omega-6s in 100 grams (3.5 ounces) of the following
foods:
• soybean oil: 50 grams
• corn oil: 49 grams
• mayonnaise: 39 grams
• walnuts: 37 grams
• sunflower seeds: 34 grams
• almonds: 12 grams
• cashew nuts: 8 grams
Foods high in omega-9 fats
Omega-9 fats are common in:
• vegetable and seed oils
• nuts
• seeds
There are no adequate intake recommendations for omega-9s since
they’re nonessential.
Here are the amounts of omega-9s in 100 grams of the following
foods:
1. olive oil: 83 grams
2. cashew nut oil: 73 grams
3. almond oil: 70 grams
4. avocado oil: 60 grams
5. peanut oil: 47 grams
6. almonds: 30 grams
7. cashews: 24 grams
8. walnuts: 9 grams
How to choose an omega 3-6-9 supplement
• Choose an omega-3 supplement instead of a combined omega-3-6-9 supplement. If
you’re buying a combined supplement, choose one with a high concentration of EPA and
DHA.
• Combined omega-3-6-9 supplements are popular, but they generally provide no
additional benefit over taking omega-3 alone.
• Omega-6s are essential in certain quantities, but they’re present in many foods. People
who follow a Western diet may already consume too many.
• Additionally, the body can produce omega-9 fats, and they’re easily obtained in the diet.
So you don’t need to take them in supplement form.
• Therefore, although combined supplements contain optimal omega 3-6-9 ratios, taking
just omega-3s will likely provide you with the most health benefits.
Western pattern diet
• The Western pattern diet (WPD) is a modern dietary pattern that is
generally characterized by high intakes of;
• red meat,
• processed meat,
• pre-packaged foods,
• butter,
• candy and sweets,
• fried foods, conventionally-raised animal products,
• high-fat dairy products, eggs, refined grains, potatoes, corn etc.
Neutral Fats OR Triglycerides
FATS OR TRIGLYCERIDES
• Also called as
• Neutral fats
• Triacylglycerol (TAG) or
• Triglycerides (TG)
• Chemically these are esters of fatty acids with glycerol.
• Most common and widespread class of lipids in nature and
represent the storage form of lipids.
• Abundant in fat depots of animals, nuts and seeds.
• Insoluble in water and non-polar character
Structure of Triglycerides
Fats primarily occur in adipose tissue. Adipocytes of adipose
tissue are specialized for storage of triacylglycerol.

The fat is stored in the form of globules dispersed in the entire

cytoplasm
Properties of Triglycerides
• Physical Properties depend on the fatty acid
components
• Melting point increases as the number of carbon in
hydrocarbon chain increases and as the number of double
bond decreases.
• Simply, greater the number of unsaturated fatty acids in
the fat molecule, lower will be the melting point.
• Pure fats possess no color, odor and taste.
• Specific gravity of fats is lower then water i.e., lower than
1.
Chemical Properties
Rancidity
It represent the deterioration of fats & oils resulting in an
unpleasant taste.
Fats containing unsaturated fatty acids are more susceptible to
rancidity.
Rancidity occurs when fats and oils are exposed to air, moisture,
light, bacteria etc
1. Hydrolytic rancidity occurs due to partial hydrolysis of TGs
by bacterial enzymes.
2. Oxidative rancidity is due to oxidation of unsaturated fatty
acids.
This results in the formation of unpleasant products such as
dicarboxylic acids, aldehydes, ketones etc.
Rancid fats and oils are unsuitable for human consumption.
The substances which can prevent the occurrence of
oxidative rancidity are known as antioxidants.
Iodine Number
Iodine number is used to measure the degree of unsaturation of a fat.
Simply, it is used to find unsaturated fatty acids content in a fat.
Iodine number: the number of grams of iodine absorbed by 100 grams
of a fat is termed as iodine number. Fats containing more unsaturated
fatty acids will have higher iodine number and vise versa.
Saponification Number
• Saponification value or saponification number (SV or SN) represents
the number of milligrams of potassium hydroxide (KOH) required
to saponify one gram of fat under the conditions specified. OR
• The number of mg of KOH required to neutralize the fatty acids
liberated from 1 gram of fat.
• It is a measure of the average molecular weight (or chain length) of all
the fatty acids present in triglycerides.
• Fats having short chain fatty acids have higher saponification number
than those containing fatty acids with longer chain lengths.
Waxes
Waxes
• Waxes are esters of fatty acids with alcohol other than
glycerol (higher molecular weight monohydric alcohols).
• Waxes are of two types
• True waxes
• Other waxes
• True waxes are esters of fatty acids with alcohol other than
glycerol or high mol. Weight alcohols, whereas, other waxes
includes esters of cholesterol, vitamin A & D.
• Common naturally occurring waxes includes beeswax
(honeycomb), lanolin (wool) and spermaceti (sperm of
whale).
• Waxes cannot be hydrolyzed by digestive enzyme lipases
therefore, waxes are of no nutritional importance.
• Lanolin waxes are widely used as base for ointment and
creams, and Spermaceti in cosmetics, pharmaceuticals and
in candle preparation.
• Waxes are widely distributed in nature. The leaves and fruits
of many plants have waxy coatings, which may protect them
from dehydration and small predators.
• The feathers of birds and the fur of some animals have
similar coatings which serve as a water repellent. Carnuba
wax is valued for its toughness and water resistance.
Compound Lipids
Compound Lipids
These are esters of fatty acids containing groups in addition to
an alcohol and a fatty acid. For example, the additional group
in phospholipids are phosphoric acid residue. Compound
lipids includes;

1. Phospholipids
2. Glycolipids
3. Sulfolipids
4. Gangliosides
Phospholipids

Phospholipids = Alcohol, fatty acid, and phosphoric acid residue.

Additional groups may also be N-containing bases and other
substituents. Based on alcohol, these can be divided into
glycerophospholipids and sphingophospholipids.

• Further classified into (1) Glycerophospholipids (2)

Sphingophospholipids
1. Glycerophospholipids
• Glycerol is the alcohol group
• Also called phosphoglycerides or glycerol phosphatides
• Contain glycerol, fatty acid, phosphoric acid and some cases
nitrogenous bases.
• Donot make true solutions in water but disperse forming micelles.
• They are good emulsifying agents.
• Further divided into (1) Phosphatidic acid (2) Lecithins (3) Cephalins
and (4) Plasmalogens
1. Phosphatidic Acid
• Phosphatidic acid is a parent compound of glycerophospholipids and
are present in small amount in cells.
• In these, one of the fatty acid of a triglyceride is replaced by
phosphoric acid (H3PO4).
2. Lecithins (Phosphatidylcholines)
Phosphatidic acid + Choline = Lecithin
Lecithins are composed of phosphoric acid, cholines, esters of glycerol,
and two fatty acids; the chain length, position, and degree of
unsaturation of these fatty acids vary, and this variation results in
different lecithins with different biological functions.
Pure lecithin is white and waxy and darkens when exposed to air.
Commercial lecithin is brown to light yellow, and its consistency varies
from plastic to liquid.
Lecithins are the most abundant phospholipids in serum and bile. They are
soluble in all fat-solvents but insoluble in acetone. These are good
emulsifying agents for fats.
Phospholipase A catalyze the conversion of lecithins into lysolecithins by
the removal of one of the fatty acid group attached to either carbon 1 or 2.
and is found in snake venoms. Three more phospholipases, called
phospholipase B, C, D are also known.
Lecithins are also an important part of a surfactant present in the lung
alveoli. These surfactants lowers surface tension and facilitates lungs
expansion at birth and later.
The potentiality of lungs to expand after birth can be predicted by a
chemical analysis of the amniotic fluid. The high ratio of lecithins to
sphingomyelin indicates normal condition.
(3) Cephalins (Phosphatidyl ethanolamine):
• Structurally similar to Lecithin with the exception that the
base Ethanolamine replaces choline.
• Brain and nervous tissue are rich in Cephalin.
• Cephalins are phosphoglycerides that contain ehtanolamine
or the amino acid serine attached to the phosphate group
through phosphate ester bonds. A variety of fatty acids make
up the rest of the molecule. Cephalins are found in most cell
membranes, particularly in brain tissues. They are also
important in the blood clotting process as they are found in
blood platelets.
Glycerophospholipids Structures
(4) Plasmalogens
• Plasmalogen is any of a class of phospholipids, found in cell
membranes, in which one of the fatty acids is replaced by an
aldehyde.
• Simply, they are lecithin or cephalin in which the fatty acid attached
to α-carbon is replaced by an aldehyde group.
• Plasmalogens are present in cardiac muscles, skeletal muscles, and
brain.

Cardiolipin:
• Abundantly found in mitochondrial membrane.
• This is the only phospholipid with antigenic properties.
• Cardiolipins are present in heart muscles and is used as an antigen for
detection of syphilis.
(B) Sphingolipids
Ceramide: If R= H
Cerebroside: If R= Glucose
As the name indicates it is found in the brain especially
in the myelin sheath
 Sphingomyelin: If R= Phosphocholine or
phosphoethanolamine
Sphingomyelin is found in axons
and Myelin sheath. Enriched in
CNS
2. Glycolipids
• Glycolipids are carbohydrate containing lipid molecules that
resembles sphingolipids because it contain sphingosine.
• Glycolipids = sphingosine, fatty acid and a carbohydrate.
• Also called ceramide sugars
• Fatty acids usually contain 22-26 carbon atoms
• Each molecule of glycolipid may
contain one to six sugar units
• They are also called glycosphingolipids or simply sphingolipids.
• It differs from sphingophospholipids in the respect that does not contain
Phosphocholine or phosphoethanolamine
• Found in white matter of brain and myelin sheath of nerves
• Glycolipids containing one sugar unit are called cerebrosides.
• Individual glycolipids are differentiated on the basis of kind of fatty acids or
sugar in the molecule. Four types are commonly observed)
a) Kerasin- contains Lignoceric acid
b) Cerebron- Contains cerebronic acid
c) Nervon- contains Nervonic acid
d) Oxynervon- contains hydroxy derivative of nervonic acid

Glycolipids are used to determine blood group antigens i.e., A and B

3. Sulfolipids
• Sulfolipids = sphingosine, fatty acid, sugar and sulfate group
• Ceramide-Galactose-Sulfate
• They are also called sulfatides and are sulfuric acid esters of
cerebrosides.
• Occurs chiefly in white matter of brain as well as in other tissues.
• It maintain stability of the cellular membrane and facilitate cell–cell
interactions. It also act as a receptor for viruses and pathogens
4. Gangliosides
• Gangliosides = sphingosine, fatty acid, sugar units, N-acetyl
hexosamine and N-acetylneuraminic acid (Sialic Acid).
• Sialic acids are a class of alpha-keto acid sugars with a nine-carbon
backbone.
• Gangliosides occurs in brain, red blood cells, spleen and nerve cells.
• In brain, it contribute 6% of lipids in gray matter.
• They are negatively charged at physiological pH. The negative charge
is imparted by N- acetyl Neuraminic acid(Sialic acid).
• It play important roles in the modulation of membrane proteins and
ion channels, in cell signaling and in the communication among cells.
Derived Lipids
Derived, precursor and associated lipids
• These are the hydrolytic products of simple and compound
lipids.
• Simply, these are the substances derived from simple &
compound by hydrolysis OR lipid like molecules e.g., steroids
etc. but they still possess the properties of general lipids.
• The most common derived lipids are steroids terpenes and
carotenoids.
3. Derived, Precursor and Associated Lipids:
1. Diglycerides
2. Fatty acids
3. Alcohols including glycerol
4. Sterols
5. Vitamin D, E, K
6. Carotenoids
7. Eicosanoids
1. Prostacyclins
2. Prostaglandins
3. Thromboxanes
4. Leukotrienes
5. Lipoxins
8. Terpenes
Derived Lipids
• Fatty acids
• Alcohols other than glycerol
• Glycerides

Substances Associated with Lipids

• Carotenoids
• Tocopherols
• Vitamins A, D, E and K
• Steroids (Cholesterol)
Steroids & Steroid Nucleus
• Steroid, any of a class of natural or synthetic organic compounds
characterized by a molecular structure of 17 carbon atoms arranged
in four rings (tetracyclic). It contain 3 6-membered rings and 1 5-
membered ring.
• Four interconnected rings of carbon atoms form the skeleton of all
steroids. In most of the natural steroids a methyl group is present at
carbon number 10 and 13. Do not contain fatty acids.
Sterols
• When an alcohol group (-OH) is attached to one of the steroid ring,
then the compound is called sterol such as cholesterol.
• Sterols are widely distributed in plasma membranes of animals, plants
and fungi. Bacteria does not contain sterols.
• Steroids vary from one another in the nature of attached groups, the
position of the groups, and the configuration of the steroid nucleus.
Small modifications in the molecular structures of steroids can
produce remarkable differences in their biological activities.
Cholesterol

• It is best known sterol. It contains steroid rings with a hydroxyl, two

methyl groups and a hydrocarbon tail. It is the most abundant animal
sterol. Isolated first in 1784 from gall stones.
• Normal plasma level ranges from 150-220 mg/dl, but a 200 mg/dl is
considered the maximum level.
• Normal human adult contain 140 grams of cholesterol.
• Cholesterol is essential for animal life, and is necessary for building
and maintenance of membranes.
• They are present in the lipid bilayer and prevent the compactness of
the membranes under low temperatures
• Cholesterol is also a precursor of all steroid hormones e.g., cortisol,
testosterone, estrogen and bile acids.
• It also helps in intracellular transport, cell signaling and nerve
conduction.
Good & Bad Cholesterol
Ergosterol
• Ergosterol, also called provitamin D2, a white crystalline organic solid of
the molecular formula C28H44O belonging to the steroid family.
• It is found only in fungi (e.g, Saccharomyces and other yeasts and Claviceps
purpurea) and is chemically related to cholesterol.
• Ergosterol is converted by ultraviolet irradiation into ergocalciferol, or
vitamin D2, a nutritional factor that promotes proper bone development in
humans and other mammals.
• Its relationship to vitamin D was established in 1927, when it was shown
that an irradiated sample of ergosterol could be used to alleviate rickets, a
deficiency disease of bone caused by lack of vitamin D in the diet.
Commercially, ergosterol is produced from yeast and then converted into
vitamin D2, which is used as a food supplement.
Dihydrocholesterol
• This sterol occurs in many tissues but in skin its presence has a special
role. It is converted into vitamin D3 when the skin is exposed to
sunlight. For this reason it is also called sunlight vitamin.
Enzymes
Introduction
• Enzymes are biological catalysts that speed up the rate of the
biochemical reaction.
• Most enzymes are three dimensional globular proteins. Some special
RNA species also act as enzymes and are called Ribozymes. Enzymes
in addition to proteins also require non-protein components for
proper enzymatic activity.
• The protein part is called apoenzyme, while the non-protein part is
called cofactor. Both parts must be present before the enzyme can
function.
Holoenzymes
• Some enzymes require molecules other than proteins for enzymic
activity. The term holoenzyme refers to the active enzyme with its
non-protein component, whereas the enzyme without its non-protein
moiety is termed an apoenzyme and is inactive.
• If the non-protein moiety is a metal ion such as Zn2+ or Fe2+, it is
called a cofactor. If it is a small organic molecule, it is termed a
coenzyme.
CO-FACTORS & COENZYMES
• Coenzymes and cofactors are molecules that help an enzyme or
protein to function appropriately.
• A cofactor is a non-protein chemical compound or metallic ion that is
required for an enzyme's activity as a catalyst. Cofactors can be
considered "helper molecules" that assist in biochemical
transformations.
• Co-factors are of two types:
1. Organic co-factors
2. Inorganic cofactors
INORGANIC CO-FACTORS
These are the inorganic molecules required for the proper
activity of enzymes. Cofactors do not bind the enzyme.
These are metal ions and are often required to increase the
rate of catalysis of a given reaction.
Examples: Alcohol dehydrogenase; Carbonic anhydrase; DNA
polymerase requires Zn ion for it’s activity.
Whereas, Glucose 6-phosphatase; Hexokinase; DNA
polymerase has co-factor Mg ion.
ORGANIC CO-FACTORS
These are the organic molecules required for the proper activity of
enzymes. Coenzymes are organic molecules and quite often bind
loosely to the active site of an enzyme and aid in substrate recruitment.
Example: Glycogen phosphorylase requires the small organic molecule
pyridoxal phosphate.
Prosthetic Group: If the coenzyme is permanently associated with the
enzyme and returned to its original form, it is called a prosthetic group.
It is a tightly bound organic cofactor e.g. Flavins, heme groups and
biotin.
Co-substrates: Coenzymes that only transiently associate with the
enzyme and dissociate in an altered state. e.g., NAD+
Coenzymes frequently are derived from vitamins.
PROPERTIES OF ENZYMES
Enzymes are protein catalysts that increase the velocity of a chemical
reaction, and are not consumed during the reaction.
Note: Some RNAs can act like enzymes, and are called ribozymes.
Ribozymes are much less commonly encountered than protein
catalysts.
A. Active sites
Enzyme molecules contain a special pocket or cleft called the active
site. The active site contains amino acid side chains that participate in
substrate binding and catalysis. The substrate binds the enzyme,
forming an enzyme–substrate (ES) complex.
Binding is thought to cause a conformational
change in the enzyme (induced fit) that
allows catalysis.
ES is converted to an enzyme–product (EP)
complex that subsequently dissociates to
enzyme and product.
B. Catalytic efficiency
Enzyme-catalyzed reactions are highly efficient, proceeding from 103–
108 times faster than un-catalyzed reactions. The number of molecules
of substrate converted to product per enzyme molecule per second is
called the turnover number, or kcat and typically is 102–104/sec.

C. Specificity
Enzymes are highly specific, interacting with one or a few substrates
and catalyzing only one type of chemical reaction.
Note: The set of enzymes made in a cell determines which metabolic
pathways occur in that cell.
D. Regulation
Enzyme activity can be regulated, that is, increased or decreased, so
that the rate of product formation responds to cellular need.
E. Location within the cell
Many enzymes are localized in specific organelles within the cell. Such
compartmentalization serves to isolate the reaction substrate or
product from other competing reactions. This provides a favorable
environment for the reaction, and organizes the thousands of enzymes
present in the cell into purposeful pathways.
HOW ENZYMES WORK
The catalytic efficiency of enzymes is explained by two perspectives:
Mechanism of Enzyme Action
The mechanism of enzyme action can be viewed from two different
perspectives.

• The first treats catalysis in terms of energy changes that occur during
the reaction, that is, enzymes provide an alternate, energetically
favorable reaction pathway different from the un-catalyzed reaction.
• The second perspective describes how the active site chemically
facilitates catalysis.
THERMODYNAMIC CHANGES
• All chemical reactions have energy barriers between reactants and
products.
• The difference in transitional state and substrate is called activational
barrier.
• Only a few substances cross the activation barrier and change
into products. That’s why rate of un-catalyzed reactions is
much slow.
• Enzymes provide an alternate pathway for conversion of
substrate into products.
• Enzymes accelerate reaction rates by forming transitional
state having low activation energy. Hence, the reaction rate is
increased many folds in the
presence of enzymes.
• The total energy of the system remains the same and
equilibrium state is not disturbed.
Alternate reaction pathway: An enzyme
allows a reaction to proceed rapidly under
conditions prevailing in the cell by providing
an alternate reaction pathway with a lower
free energy of activation.
The enzyme does not change the free
energies of the reactants or products and,
therefore, does not change the equilibrium
of the reaction. It does, however, accelerate
the rate with which equilibrium is reached.
Chemistry of the Active Site
The active site is not a passive receptacle for binding the substrate, but
rather is a complex molecular machine employing a diversity of chemical
mechanisms to facilitate the conversion of substrate to product. A number
of factors are responsible for the catalytic efficiency of enzymes, including
the following:
1. Transition-state stabilization:
The active site often acts as a flexible molecular template that binds the
substrate and initiates its conversion to the transition state, a structure in
which the bonds are not like those in the substrate or the product. By
stabilizing the transition state, the enzyme greatly increases the
concentration of the reactive intermediate that can be converted to product
and, thus, accelerates the reaction.
2. Other mechanisms
The active site can provide catalytic groups that enhance the
probability that the transition state is formed.
In some enzymes, these groups can participate in general acid-base
catalysis in which amino acid residues provide or accept protons.
In other enzymes, catalysis may involve the transient formation of a
covalent ES complex.
3. Visualization of the transition state

We can envision a parent acting as an

enzyme, first coming in contact with the
baby (forming ES), then guiding the
baby’s arms into an extended, vertical
position, analogous to the ES transition
state.
This posture (conformation) of the baby
facilitates the removal of the sweater,
forming the undressed baby, which here
represents product.
LOCK AND KEY MODEL
• Proposed by EMIL FISCHER in 1894.
• Lock and key hypothesis assumes the active site of an enzymes are
rigid in its shape. There is no change in the active site before and after
a chemical reaction.
• The specific action of an enzyme with a single substrate can be
explained using a Lock and Key analogy. In this analogy, the lock is
the enzyme and the key is the substrate. Only the correctly sized key
(substrate) fits into the key hole (active site) of the lock (enzyme).
Smaller keys, larger keys, or incorrectly positioned teeth on keys
(incorrectly shaped or sized substrate molecules) do not fit into the
lock (enzyme). Only the correctly shaped key opens a particular lock.
Which means only the specific enzyme reacts with the specific
substrate.
INDUCED FIT MODEL
More recent studies have revealed that the process is much more likely
to involve an induced fit model(proposed by DANIAL KOSH LAND in
1958).
According to this model, exposure of an enzyme to substrate cause a
change in enzyme, which causes the active site to change it’s shape to
allow enzyme and substrate to bind.
FACTORS AFFECTING REACTION VELOCITY
Enzymes can be isolated from cells, and their properties
studied in a test tube (that is, in vitro). Different enzymes
show different responses to changes in substrate
concentration, temperature, and pH.
This section describes factors that influence the reaction
velocity of enzymes. Enzymic responses to these factors give
us valuable clues as to how enzymes function in living cells
(that is, in vivo).
A. Substrate concentration
1. Maximal velocity:
The rate or velocity of a reaction (v) is the number of substrate
molecules converted to product per unit time; velocity is usually
expressed as μmol of product formed per minute.
The rate of an enzyme-catalyzed reaction increases with substrate
concentration until a maximal velocity (Vmax) is reached.
The leveling off of the reaction rate at high substrate concentrations
reflects the saturation with substrate of all available binding sites on the
enzyme molecules present.
B. Temperature
1. Increase of velocity with temperature: The reaction velocity
increases with temperature until a peak velocity is reached. This
increase is the result of the increased number of molecules having
sufficient energy to pass over the energy barrier and form the products
of the reaction.
2. Decrease of velocity with higher temperature: Further elevation of
the temperature results in a decrease in reaction velocity as a result of
temperature-induced denaturation of the enzyme.
C. pH
1. Effect of pH on the ionization of the active site:
The concentration of H+ affects reaction velocity in several ways. First, the
catalytic process usually requires that the enzyme and substrate have
specific chemical groups in either an ionized or un-ionized state in order to
interact. For example, catalytic activity may require that an amino group of
the enzyme be in the protonated form (–NH3+). At alkaline pH, this group is
deprotonated, and the rate of the reaction, therefore, declines.
2. Effect of pH on enzyme denaturation:
Extremes of pH can also lead to denaturation of the enzyme, because the
structure of the catalytically active protein molecule depends on the ionic
character of the amino acid side chains.
Enzymes are most active at optimum pH. It contain R groups
of amino acids with proper charges at optimum pH. It lose
activity in low or high pH as tertiary structure is disrupted.
3. The pH optimum varies for different enzymes: The pH at which
maximal enzyme activity is achieved is different for different enzymes,
and often reflects the [H+] at which the enzyme functions in the body.
For example, pepsin, a digestive enzyme in the stomach, is maximally
active at pH 2, whereas other enzymes, designed to work at neutral pH,
are denatured by such an acidic environment
INHIBITION OF ENZYME ACTIVITY
The prevention of an enzyme process as a result of
interaction of inhibitors with the enzyme.

INHIBITORS
Any substance that can diminish the velocity of an
enzyme catalyzed reaction is called an inhibitor.
REVERSIBLE INHIBITION
It is an inhibition of enzyme activity in which the inhibiting molecular
entity can associate and dissociate from the protein‘s binding site.
TYPES OF REVERSIBLE INHIBITION
There are four types
1. Competitive inhibition
2. Non-competitive inhibition
3. Uncompetitive inhibition
4. Mixed inhibition
1. Competitive inhibition
This type of inhibition occurs when the inhibitor binds reversibly
to the same site (active site of enzyme) that the substrate would
normally occupy and, therefore, competes with the substrate for
that site. Formation of Enzyme-Substrate complex is reduced
while a new Enzyme-Inhibitor complex is formed

Effect on Vmax: The effect of a competitive inhibitor is reversed

by increasing [S]. At a sufficiently high substrate concentration,
the reaction velocity reaches the Vmax observed in the absence
of inhibitor.
Effect of a competitive inhibitor on the reaction velocity
(vo) versus substrate ([S]) plot.
Statin Drug As Example of Competitive Inhibition
This group of antihyperlipidemic agents competitively inhibits the
first committed step in cholesterol synthesis. This reaction is
catalyzed by hydroxymethylglutaryl–CoA reductase (HMG-CoA
reductase).
Statin drugs, such as atorvastatin and pravastatin are structural
analogs of the natural substrate for this enzyme, and compete
effectively to inhibit HMG-CoA reductase. By doing so, they inhibit de
novo cholesterol synthesis, thereby lowering plasma cholesterol
levels.
Pravastatin competes with
HMG-CoA for the active site of
HMG-CoA reductase.
2. Noncompetitive inhibition
This type of inhibition is recognized by its characteristic effect on Vmax.
Noncompetitive inhibition occurs when the inhibitor and substrate bind
at different sites on the enzyme.
The noncompetitive inhibitor can bind either free enzyme or the ES
complex, thereby preventing the reaction from occurring (Figure 5.15).
Effect on Vmax: Noncompetitive inhibition cannot be overcome by
increasing the concentration of substrate. Thus, noncompetitive
inhibitors decrease the apparent Vmax of the reaction.
Effect of a noncompetitive inhibitor on the reaction
velocity (vo) versus substrate ([S]) plot.
A noncompetitive inhibitor binding to both
free enzyme and enzyme–substrate (ES)
complex.
Examples of noncompetitive inhibitors: Some inhibitors act by
forming covalent bonds with specific groups of enzymes. Examples
include insecticides, heavy metals etc.

3. MIXED INHIBITION
In this type of inhibition both E.I and E.S.I complexes are formed.
Both complexes are catalytically inactive.

4. UNCOMPETITIVE INHIBITION
In this type of inhibition, inhibitor does not compete with the
substrate for the active site of enzyme instead it binds to another site
known as allosteric site.
EXAMPLES OF UNCOMPETITIVE INHIBITION
Drugs to treat cases of poisoning by methanol or ethylene glycol act as
uncompetitive inhibitors. Tetramethylene sulfoxide and 3- butylthiolene 1-oxide
are uncompetitive inhibitors of liver alcohaldehydrogenase.
IRREVERSIBLE INHIBITION
This type of inhibition involves the covalent attachment of the inhibitor
to the enzyme. The catalytic activity of enzyme is completely lost. It can
only be restored only by synthesizing molecules.
Aspirin which targets and covalently modifies a key enzyme involved in
inflammation is an irreversible inhibitor.
SUICIDE INHIBITION :
It is an unusual type of irreversible inhibition where the enzyme
converts the inhibitor into a reactive form in its active site.
ENZYME ACTIVATION
Activation is defined as the conversion of an inactive form of an
enzyme to active form which processes the metabolic activity.
TYPES OFACTIVATION
• Activation by co-factors.
• Conversion of an enzyme precursor.
ACTIVATION BY CO FACTORS
Many enzymes are activated by co-factors.
Examples: DNA polymerase is a holoenzyme that catalyzes the
polymerization of de -oxyribonucleotide into a DNA strand. It uses Mg-
ion for catalytic activity. Horse liver dehydrogenase uses Zn- ion for it’s
activation.
Classification
Nomenclature
Each enzyme is assigned two names. The first is its short,
recommended name, convenient for everyday use. The second is the
more complete systematic name, which is used when an enzyme must
be identified without ambiguity.
Most commonly used enzyme names have the suffix “-ase” attached to
the substrate of the reaction (for example, glucosidase and urease), or
to a description of the action performed (for example, lactate
dehydrogenase and adenylyl cyclase).
[Note: Some enzymes retain their original trivial names, which give no
hint of the associated enzymic reaction, for example, trypsin and
pepsin.]
To address the ambiguity and confusion arising from these
inconsistencies in nomenclature and the continuing discovery
of new enzymes, the International Union of Biochemists
(IUB) developed a complex but unambiguous system of
enzyme nomenclature.
In the IUB system, each enzyme has a unique name and code
number that reflect the type of reaction catalyzed and the
substrates involved. Enzymes are grouped into six classes,
each with several subclasses.
Listed below are the six IUB classes of enzymes and the reactions they
catalyze.
1. Oxidoreductases catalyze oxidations and reductions.
2. Transferases catalyze transfer of groups such as methyl or glycosyl
groups from a donor molecule to an acceptor molecule.
3. Hydrolases catalyze the hydrolytic cleavage of C──C, C──O, C──N, P──O,
and certain other bonds, including acid anhydride bonds.
4. Lyases catalyze cleavage of C──C, C──O, C──N, and other bonds by
elimination, leaving double bonds, and also add groups to double bonds.
5. Isomerases catalyze geometric or structural changes within a single
molecule.
6. Ligases catalyze the joining together of two molecules, coupled to the
hydrolysis of a pyrophosphoryl group in ATP or a similar nucleoside
triphosphate.
For example, the enzyme commonly called “hexokinase”
is designated “ATP:D-hexose-6-phosphotransferase E.C.
2.7.1.1.” This identifies hexokinase as a member of class 2
(transferases), subclass 7 (transfer of a phosphoryl group),
sub-subclass 1 (alcohol is the phosphoryl acceptor).
Finally, the term “hexose-6” indicates that the alcohol
phosphorylated is that of carbon six of a hexose.
Vitamins
Vitamins
A vitamin is defined as “an organic compound that is
required in the diet in small amounts for the
maintenance of normal metabolic integrity”.
OR
“A group of organic nutrients required in small
quantities for a variety of biochemical functions and
which, generally, cannot be synthesized by the body
and must therefore be supplied in the diet”.
Biomedical Importance
On the basis of solubility vitamins are classified into lipid soluble
and water soluble vitamins.
The lipid-soluble vitamins are apolar hydrophobic compounds
that can only be absorbed efficiently when there is normal fat
absorption. They are transported in the blood, like any other
apolar lipid, in lipoproteins or attached to specific binding
proteins.
They have diverse functions, for example vitamin A, vision;
vitamin D, calcium and phosphate metabolism; vitamin E,
antioxidant; vitamin K, blood clotting.
Deficiency of lipid-soluble vitamins
Deficiency of lipid-soluble vitamins occurs due to the following reasons;
1. dietary inadequacy,
2. steatorrhea (affect digestion and absorption)
3. disorders of the biliary system (affect digestion and absorption)
Deficiency of;
Vitamin A: Night blindness and xerophthalmia
Vitamin D: Rickets in young children and osteomalacia in adults
Vitamin E: Neurologic disorders and anemia of the newborn
Vitamin K: Hemorrhage of the newborn.
Water-soluble vitamins
Water-soluble vitamins = Vitamin-B complex and vitamin C and
function as enzyme cofactors. Folic acid also called as B9 vitamin, it
helps the body make healthy red blood cells.
Deficiency of a single vitamin of the B complex is rare, since poor diets
are most often associated with multiple deficiency states.
beriberi (thiamin);
cheilosis, glossitis, seborrhea (riboflavin); pellagra (niacin);
peripheral neuritis (pyridoxine); megaloblastic anemia, methylmalonic
aciduria, and pernicious anemia (vitamin B12); and megaloblastic
anemia (folic acid). Vitamin C deficiency leads to scurvy.
THE VITAMINS ARE A DISPARATE GROUP OF COMPOUNDS WITH A
VARIETY OF METABOLIC FUNCTIONS

A vitamin is defined as an organic compound that is required in the

diet in small amounts for the maintenance of normal metabolic
integrity. Deficiency causes a specific disease, which is cured or
prevented only by restoring the vitamin to the diet.
However, vitamin D, which can be made in the skin after exposure
to sunlight, and niacin, which can be formed from the essential
amino acid tryptophan, do not strictly conform to this definition.
LIPID-SOLUBLE VITAMINS
Vitamin A: Also called Retinol. It has several isomers but the most
important are 13-cis retinol (fish liver oils) and 11-cis retinol which
occurs in the retina.
Quite heat stable but destroyed at high temperature in the presence of
oxygen.
Occurrence: Vitamin A as such in animals only. Richest animal sources
includes; fish liver oils, egg yolk, butter, cheese, whole milk and in the
liver of other animals.
Plant sources: in plants it occurs as provitamin. i.e., carotenes, a yellow
pigment found in carrots, sweet potatoes, peaches and spinach.
Carotenes itself have no vitamin A activity, but these are
converted in to vitamin A in the liver.
Retinoids & Carotenoids: The retinoids are a class of chemical
compounds that are vitamers of vitamin A or are chemically
related to it. “Vitamers are chemically similar substances that
have a qualitatively similar vitamin activity”.
Retinoids comprise retinol, retinaldehyde, and retinoic acid
(preformed vitamin A, found only in foods of animal origin);
whereas, carotenoids, found in plants, comprise carotenes and
related compounds, known as provitamin A, as they can be
cleaved to yield retinaldehyde and thence retinol and retinoic
acid.
The α-, β-, and γ-carotenes are quantitatively the most
important provitamin A carotenoids. Of which β-carotene is
the most important precursor because one molecule of β-
carotene should yield two of retinol, this is not so in practice;
6 μg of β-carotene is equivalent to 1 μg of preformed retinol
because carotenes are poorly absorbed and their conversion
into retinol is not 100%. The total amount of vitamin A in
foods is therefore expressed as micrograms of retinol
equivalents.
Beta-carotene and other provitamin A carotenoids are cleaved
in the intestinal mucosa by carotene dioxygenase, yielding
retinaldehyde, which is reduced to retinol.
 Vitamin A Has a Function in Vision

In deficiency, both the time

taken to adapt to darkness
and the ability to see in poor
light are impaired.
Storage and Transport of Vitamin A
Main storage organ is liver but kidney and lungs store it up to a lesser extent.
In the blood plasma it is carried by a protein called retinol binding protein. So
in protein deficiency despite of sufficient Vitamin A in the body the patient
will be unable to see in the dark (night blindness).
Vitamin A1: Retinol
Vitamin A2: Possess 40% of Vitamin A1 activity
Retinoic Acid: It is the oxidized derivative of retinol. It possess all fuctions of
retinol except visual function. All trans retinoic acid acid is the active form of
vitamin A except retina. It 10-100 times more active vs retinol.
Retinoic acid has got functions in influencing gene expressions.
Topical retinoic acid is employed for treating acnes
Vitamin A Deficiency Is a Major Public Health
Problem Worldwide
Vitamin A deficiency is the most important preventable cause of blindness.
The earliest sign of deficiency is a loss of sensitivity to green light, followed
by impairment of adaptation to dim light, followed by night blindness.
More prolonged deficiency leads to xerophthalmia: keratinization of the
cornea and skin and blindness.
Vitamin A also has an important role in differentiation of immune system
cells, and mild deficiency leads to increased susceptibility to infectious
diseases.
Furthermore, the synthesis of retinol-binding protein in response to
infection is reduced, decreasing the circulating vitamin and therefore there
is further impairment of immune responses.
Vitamin A Is Toxic in Excess
Excessive intakes of vitamin A lead to accumulation beyond the capacity of
binding proteins, so that unbound vitamin A causes tissue damage.
Symptoms of toxicity affect the
CNS (headache, nausea, ataxia, and anorexia, all associated with increased
cerebrospinal fluid pressure),
the liver (hepatomegaly with histologic changes and hyperlipidemia),
calcium homeostasis (thickening of the long bones, hypercalcemia and
calcification of soft tissues), and
the skin (excessive dryness, itchy skin, peeling of the skin, desquamation,
and alopecia, cracking of the lips).
Vitamin D
Vitamin D (also referred to as “calciferol”) is a fat-soluble vitamin
that is naturally present in a few foods, added to others, and
available as a dietary supplement. It is also produced
endogenously when ultraviolet (UV) rays from sunlight strike the
skin and trigger vitamin D synthesis.
Vitamin D2 is referred as ergocalciferol and is of plant origion
because it was first obtained by the irradiation of ergosterol. While
Vitamin D3 is called cholecalciferol and is of animal origion and can
be produced in the human skin, when ultraviolet (UV) rays from
sunlight strike the skin it converts provitamin-D3 (7-
dehydrocholestrol) into cholecalciferol.
Synthesis of Vitamin D in the Skin
VITAMIN D IS REALLY A HORMONE
Vitamin D is not strictly a vitamin since it can be synthesized in the skin,
and under most conditions that is its major source. Only when sunlight
is inadequate, then a dietary source is required.
The main function of vitamin-D is in the regulation of calcium
absorption and homeostasis (homeostasis is the state of steady
internal, physical, and chemical conditions maintained by living
systems).
Deficiency—leading to rickets in children and osteomalacia in adults—
continues to be a problem in those areas, where sunlight exposure is
poor.
Brief Overview
Vitamin D obtained from sun exposure, foods, and supplements is
biologically inert and must undergo two hydroxylations in the body for
activation.
The first hydroxylation, which occurs in the liver, converts vitamin D to
25-hydroxyvitamin D [25(OH)D], also known as “calcidiol.”
The second hydroxylation occurs primarily in the kidney and forms the
physiologically active 1,25-dihydroxyvitamin D [1,25(OH)2D], also
known as “calcitriol”
Vitamin D promotes calcium absorption in the gut and
maintains adequate serum calcium and phosphate
concentrations to enable normal bone mineralization and to
prevent hypocalcemic tetany (involuntary contraction of
muscles, leading to cramps and spasms). It is also needed for
bone growth and bone remodeling by osteoblasts and
osteoclasts.
Without sufficient vitamin D, bones can become thin, brittle, or
misshapen. Vitamin D sufficiency prevents rickets in children
and osteomalacia in adults. Together with calcium, vitamin D
also helps protect older adults from osteoporosis.
In foods and dietary supplements, vitamin D has two main
forms, D2 (ergocalciferol) and D3 (cholecalciferol), that
differ chemically only in their side-chain structures. Both forms
are well absorbed in the small intestine.
Serum concentration of 25(OH)D is currently the main
indicator of vitamin D status. It reflects vitamin D produced
endogenously and that obtained from foods and supplements.
In serum, 25(OH)D has a fairly long circulating half-life of 15
days. Serum concentrations of 25(OH)D are reported in both
nanomoles per liter (nmol/L) and nanograms per milliliter
(ng/mL). One nmol/L is equal to 0.4 ng/mL, and 1 ng/mL is
equal to 2.5 nmol/L.
In contrast to 25(OH)D, circulating 1,25(OH)2D is generally
not a good indicator of vitamin D status because it has a short
half-life measured in hours, and serum levels are tightly
regulated by parathyroid hormone, calcium, and phosphate.
Levels of 1,25(OH)2D do not typically decrease until vitamin D
deficiency is severe.
Health Benefits of Vitamin D
1. Healthy bones
Vitamin D plays a significant in the regulation of calcium and maintenance of
phosphorus levels in the blood. These factors are vital for maintaining healthy
bones.
Vitamin D to allow the intestines to stimulate and absorb calcium and reclaim
calcium that the kidneys would otherwise excrete.
Vitamin D deficiency in children can cause rickets, which leads to a severely
bowlegged appearance due to the softening of the bones.
Similarly, in adults, vitamin D deficiency manifests as osteomalacia, or softening of
the bones. Osteomalacia results in poor bone density and muscular weakness.
A vitamin D deficiency can also present as osteoporosis, for which over 53 million
people in the United States either seek treatment or face an increased risk.
Bone is constantly being remodeled. However, as people age—and
particularly in women during menopause—bone breakdown rates
overtake rates of bone building. Over time, bone density can decline,
and osteoporosis can eventually develop.
Conclusion
All adults should consume recommended amounts of vitamin D and
calcium from foods and supplements if needed. Older women and men
should consult their healthcare providers about their needs for both
nutrients as part of an overall plan to maintain bone health and to
prevent or treat osteoporosis.
2. Reduced risk of flu
A research study conducted in 2018, suggested that some
studies had found that vitamin D had a protective effect
against the influenza virus.
However, the authors also looked at other studies where
vitamin D did not have this effect on flu and flu risk.
Further research is, therefore, necessary to confirm the
protective effect of vitamin D on the flu.
3. Healthy Infants
Vitamin D deficiency has links to high blood pressure in children. One
2018 study found a possible connection between low vitamin D levels
and stiffness in the arterial walls of children.
The American Academy of Allergy Asthma and Immunology (AAAAI)
suggest that evidence points to a connection between low vitamin D
exposure and an increased risk of allergic sensitization.
An example of this is an Australian study of egg intake. Eggs are a
common early source of vitamin D. The children who started eating
eggs after 6 months were more likely to develop food allergies than
children who started between 4–6 months of age.
Furthermore, vitamin D may enhance the anti-inflammatory effects of
glucocorticoids. This benefit makes it potentially useful as a supportive
therapy for people with steroid resistant asthma.
4. Healthy pregnancy

A 2019 review, suggests that pregnant women who are deficient in

vitamin D may have a greater risk of developing pre-eclampsia and
giving birth preterm.

Doctors also associate poor vitamin D status with gestational diabetes

and bacterial vaginosis in pregnant women.

It is also important to note that in a 2013 study, researchers associated

high vitamin D levels during pregnancy with an increased risk of food
allergy in the child during the first 2 years of life.
5.Cancer
Laboratory and animal studies suggest that vitamin D might inhibit carcinogenesis
and slow tumor progression by, for example, promoting cell differentiation and
inhibiting metastasis.
Vitamin D might also have anti-inflammatory, immunomodulatory, proapoptotic,
and antiangiogenic effects. Observational studies and clinical trials provide mixed
evidence on whether vitamin D intakes or serum levels affect cancer incidence,
progression, or mortality risk.

The U.S. Preventive Services Task Force (USPSTF) stated that, due to insufficient
evidence, it was unable to assess the balance of benefits and harms of
supplemental vitamin D to prevent cancer. Taken together, studies to date do not
indicate that vitamin D with or without calcium supplementation reduces the
incidence of cancer, but adequate or higher 25(OH)D levels might reduce cancer
mortality rates.
6. Cardiovascular disease

Vitamin D helps regulate the renin-angiotensin-aldosterone system (and thereby

blood pressure), vascular cell growth, and inflammatory and fibrotic pathways.
Vitamin D deficiency is associated with vascular dysfunction, arterial stiffening,
left ventricular hypertrophy, and hyperlipidemia. For these reasons, vitamin D has
been linked to heart health and risk of CVD.

The U.S. Preventive Services Task Force (USPSTF) stated that, due to insufficient
evidence, it was unable to assess the balance of benefits and harms of
supplemental vitamin D to prevent cancer. Taken together, studies to date do not
indicate that vitamin D with or without calcium supplementation reduces the
incidence of cancer, but adequate or higher 25(OH)D levels might reduce cancer
mortality rates.
Sun exposure & Vitamin-D
Most people in the world meet at least some of their vitamin D needs
through exposure to sunlight. Type B UV (UVB) radiation with a wavelength
of approximately 290–320 nanometers penetrates uncovered skin and
converts cutaneous 7-dehydrocholesterol to previtamin D3, which in turn
becomes vitamin D3.
Season, time of day, length of day, cloud cover, smog, skin melanin content,
and sunscreen are among the factors that affect UV radiation exposure and
vitamin D synthesis.
Older people and people with dark skin are less able to produce vitamin D
from sunlight. UVB radiation does not penetrate glass, so exposure to
sunshine indoors through a window does not produce vitamin D
How Much Sun exposure is needed to maintain adequate vitamin D levels
The factors that affect UV radiation exposure, individual responsiveness
(white/blacks), and uncertainties about the amount of sun exposure
make it difficult to provide guidelines on how much sun exposure is
required for sufficient vitamin D synthesis. But
Some expert bodies and vitamin D researchers suggest, for example,
that approximately 5–30 minutes of sun exposure, particularly between
10 a.m. and 4 p.m., either daily or at least twice a week to the face,
arms, hands, and legs without sunscreen usually leads to sufficient
vitamin D synthesis.
Moderate use of commercial tanning beds that emit 2% to 6% UVB
radiation is also effective.
Is sunlight exposure worth the skin cancer risk to
make sure people get enough vitamin D?
It does seem like 10–15 minutes of sun exposure a few times a week is
harmless, but that exposure can have consequences over your lifetime.
Despite the importance of the sun for vitamin D synthesis, limiting skin
exposure to sunlight and UV radiation from tanning beds is prudent. UV
radiation is a carcinogen, and UV exposure is the most preventable cause of
skin cancer.
Experts recommend taking photoprotective measures to reduce the risk of
skin cancer, including using sunscreen with a sun protection factor (SPF) of
15 or higher, whenever people are exposed to the sun. Sunscreens with an
SPF of 8 or more appear to block vitamin D-producing UV rays. As little as 60
seconds of UVA exposure to the sun can increase your risk for melanoma.
Recommended Dietary Allowances (RDAs)
for Vitamin D
Recommended Dietary
Allowance (RDA):
Average daily level of intake
sufficient to meet the nutrient
requirements of nearly all
(97%–98%) healthy individuals;
often used to plan nutritionally
adequate diets for individuals.
1 Micro gram (mcg) of Vitamin
D is equal to 40 IU.
Vitamin D content of selected foods
Deficiency
Although the body can create vitamin D, a deficiency can occur for many reasons.
Causes
Skin type: Darker skin, for example, and sunscreen, reduce the body’s ability to
absorb the ultraviolet radiation B (UVB) rays from the sun. Absorbing sunlight is
essential for the skin to produce vitamin D.
Sunscreen: A sunscreen with a sun protection factor (SPF) of 30 can reduce the
body’s ability to synthesize the vitamin by 95% or more. Covering the skin with
clothing can inhibit vitamin D production also.
Geographical location: People who live in northern latitudes or areas of high
pollution, work night shifts, or are homebound should aim to consume vitamin D
from food sources whenever possible.
Breastfeeding: Infants who exclusively breastfeed need a vitamin D supplement,
especially if they have dark skin or have minimal sun exposure. The American
Academy of Pediatrics recommend that all breastfed infants receive 400
international units (IU) per day of oral vitamin D.
Deficiency Symptoms
Symptoms of vitamin D deficiency may include:
1. regular sickness or infection
2. fatigue
3. bone and back pain
4. low mood
5. impaired wound healing
6. hair loss
7. muscle pain
If Vitamin D deficiency continues for long periods, it may result in
complications, such as:
1. cardiovascular conditions
2. autoimmune problems
3. neurological diseases
4. infections
5. pregnancy complications
6. certain cancers, especially breast, prostate, and colon.
Risks
The upper limit that healthcare professionals recommend for vitamin D is 4,000 IU per
day for an adult. However, the National Institutes of Health (NIH) say that vitamin D
toxicity is unlikely at intakes under 10,000 IU per day. Excessive consumption of vitamin
D can lead to over calcification of bones and the hardening of blood vessels, kidney,
lung, and heart tissues. The most common symptoms of excessive vitamin D include
headache and nausea. However, too much vitamin D can also lead to the following:
loss of appetite
dry mouth
a metallic taste
vomiting
constipation
diarrhea
Vitamin-E
Vitamin E is found naturally in some foods, added to others, and
available as a dietary supplement. “Vitamin E” is the collective name
for a group of fat-soluble compounds with distinctive antioxdant
activities”.
Naturally occurring vitamin E exists in eight chemical forms (alpha-,
beta-, gamma-, and delta-tocopherol and alpha-, beta-, gamma-, and
delta-tocotrienol) that have varying levels of biological activity.
Alpha- (or α-) tocopherol is the only form that is recognized to meet
human requirements.
Serum concentrations of vitamin E (alpha-tocopherol)
depend on the liver, which takes up the nutrient after
the various forms are absorbed from the small intestine.
The liver preferentially resecretes only alpha-tocopherol
via the hepatic alpha-tocopherol transfer protein;
whereas the liver metabolizes and excretes the other
vitamin E forms.
As a result, blood and cellular concentrations of other
forms of vitamin E are lower than those of alpha-
tocopherol and have been the subjects of less research.
Antioxidant Activity of Vitamin E
Vitamin E protect cells from the damaging effects of free radicals,
which are molecules that contain an unshared electron. Free radicals
damage cells and might contribute to the development of
cardiovascular disease and cancer.
Unshared electrons are highly energetic and react rapidly with oxygen
to form reactive oxygen species (ROS). The body forms ROS
endogenously when it converts food to energy, and antioxidants might
protect cells from the damaging effects of ROS.
The body is also exposed to free radicals from environmental
exposures, such as cigarette smoke, air pollution, and ultraviolet
radiation from the sun.
Vitamin E is a fat-soluble antioxidant that stops the
production of ROS formed when fat undergoes oxidation.

Therefore, scientist are of the conclusion that whether, by

limiting free-radical production and possibly through other
mechanisms, vitamin E might help prevent or delay the
chronic diseases associated with free radicals.
Other Roles of Vitamin E
In addition to its activities as an antioxidant, vitamin E is involved in boosting
immune function by cell signaling, regulation of gene expression, and other
metabolic processes.
Alpha-tocopherol inhibits the activity of protein kinase C, an enzyme
involved in cell proliferation and differentiation in smooth muscle cells,
platelets, and monocytes.
Vitamin-E– replete endothelial cells lining the interior surface of blood
vessels are better able to resist blood-cell components adhering to this
surface.
Vitamin E also increases the expression of two enzymes that suppress
arachidonic acid metabolism, thereby increasing the release of prostacyclin
from the endothelium, which, in turn, dilates blood vessels and inhibits
platelet aggregation.
Roles in Coronary heart disease
Vitamin E could help prevent or delay coronary heart disease (CHD) comes
from several sources. In vitro studies have found that Vitamin E inhibits
oxidation of low-density lipoprotein (LDL) cholesterol, thought to be a crucial
initiating step for atherosclerosis. It also prevent the formation of blood clots
that could lead to a heart attack or venous thromboembolism.

One study of approximately 90,000 nurses found that the incidence of heart
disease was 30% to 40% lower in those with the highest intakes of vitamin
E.
Among a group of 5,133 Finnish men and women followed for 14 years,
higher vitamin E intakes from food were associated with decreased mortality
(Deaths) from CHD.
Roles in Cancer
Vitamin E protect cell constituents from the damaging effects of free
radicals that, if unchecked, might contribute to cancer development.
Vitamin E might also block the formation of carcinogenic nitrosamines
formed in the stomach from nitrites in foods and protect against cancer
by enhancing immune function.
Roles in Eye Health
Age-related macular degeneration (AMD) and cataracts are among the
most common causes of significant vision loss in older people. Their
etiologies are usually unknown, but the cumulative effects of oxidative
stress have been postulated to play a role.
Therefore, nutrients with antioxidant functions, such as vitamin E,
could be used to prevent or treat these conditions.
Roles in Congnitive decline
The brain has a high oxygen consumption rate and abundant
polyunsaturated fatty acids in the neuronal cell membranes.
Researchers hypothesize that if cumulative free-radical damage to neurons
over time contributes to cognitive decline and neurodegenerative diseases,
such as Alzheimer’s disease, then ingestion of sufficient or supplemental
antioxidants (such as vitamin E) might provide some protection.
This hypothesis was supported by the results of a clinical trial in 341 patients
with Alzheimer’s disease of moderate severity who were randomly assigned
to receive a placebo, vitamin E and selegiline.
Over 2 years, treatment with vitamin E and selegiline, separately or together,
significantly delayed functional deterioration and the need for
institutionalization compared to placebo.
Recommended Dietary Allowances (RDAs)
International Units and Milligrams

Vitamin E is listed on the new Nutrition Facts and Supplement Facts

labels in mg.
The U.S. Food and Drug Administration (FDA) required
manufacturers to use these new labels starting in January 2020,
but companies with annual sales of less than $10 million may
continue to use the old labels that list vitamin E in international
units (IUs) until January 2021.
Conversion rules for alpha-tocopherol are as follows:
 To convert from mg to IU:
1 mg = 1.49 IU of the natural form or 2.22 IU of the synthetic form.

 To convert from IU to mg:

1 IU of the natural form = 0.67 mg of alpha-tocopherol.
1 IU of the synthetic form = 0.45 mg of alpha-tocopherol.

For example, 15 mg of natural alpha-tocopherol would equal 22.4 IU

(15 mg x 1.49 IU/mg = 22.4 IU).
The corresponding value for synthetic alpha-tocopherol would be 33.3
IU (15 mg x 2.22 IU/mg).
Tolerable Upper Intake Levels (ULs) for Vitamin

Research has not found any adverse effects from consuming

vitamin E in food. However, high doses of alpha-tocopherol
supplements can cause hemorrhage (Hemorrhagic stroke) and
interrupt blood coagulation in animals, and in vitro data suggest
that high doses inhibit platelet aggregation.
 Sources of Vitamin E

Nuts, seeds, and vegetable

oils are among the best
sources of alpha-tocopherol,
and significant amounts are
available in green leafy
vegetables and fortified cereals
Vitamin E Deficiency
Deficiency symptoms include
1. peripheral neuropathy
2. ataxia
3. skeletal myopathy
4. retinopathy
5. impairment of the immune response
Water Soluble Vitamins
Vitamin B Complex
There are many different types of vitamin B.
1. Thiamin (vitamin B1)
2. Riboflavin (vitamin B2)
3. Niacin (vitamin B3)
4. Pantothenic acid
5. Vitamin B6
6. Biotin (vitamin B7)
7. Folate and folic acid
8. Vitamin B12