BIOMOLECULES

ISC Chemistry
 BIOMOLECULES

▪ Biochemistry is the branch of chemistry concerned with the chemical reactions occurring in living organism.
▪ These chemical reactions in living organism involve chemical compounds called biomolecules.
▪ They are the building blocks of life and are composed of mainly carbon, hydrogen, oxygen, nitrogen,
sulphur and phosphorus. 2
 CARBOHYDRATES
▪ Carbohydrates are mainly produced by plants and form a large group of naturally occurring organic
compounds.
▪ They are usually defined as optically active polyhydroxy aldehydes and ketones or substances that
hydrolyze to yield polyhydroxy aldehydes and ketones.

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CLASSIFICATION (BASED ON HYDROLYSIS)
▪ Monosaccharides: The simplest carbohydrates, those cannot be hydrolysed into simpler carbohydrates are called monosaccharides. For example, glucose, fructose, ribose etc.
▪ Oligosaccharides: Carbohydrates, that hydrolyse to yield 2-10 molecules of monosaccharide. They are further classified as disaccharides, trisaccharides, tetrasaccharides etc.,
depending upon the number of monosaccharides produced upon hydrolysis. For example, sucrose, maltose etc.
▪ Polysaccharides: Carbohydrates, that yield a large number of molecules of monosaccharides (> 10) are called polysaccharides. They are also called non-reducing sugars. For
example, starch, cellulose.

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 CLASSIFICATION
(BASED ON REDUCING BEHAVIOUR)

Reducing Sugars:
▪That reduce Fehlings and Tollens are called reducing sugar.
▪All monosaccharides come under this category.
▪ They have either α-hydroxy aldehyde (glucose, mannose) or α
hydroxy ketone (fructose)
Non-Reducing Sugars:
▪ Those which do not reduce Fehlings or Tollens (Sucrose)

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GLUCOSE: PREPARATION
▪From Cane Sugar (Sucrose)

▪ From Starch

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GLUCOSE: PHYSICAL PROPERTIES
▪White crystalline solid soluble in water.
▪ Its M.P. is 419 K.

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GLUCOSE: STRUCTURAL ELUCIDATION

▪On prolonged heating with HI, glucose gives n-hexane indicating

the presence of six carbon atoms in a straight chain.

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GLUCOSE: STRUCTURAL ELUCIDATION

▪This reaction shows the presence of one carbonyl group to form

glucoxime.

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GLUCOSE: STRUCTURAL
ELUCIDATION
▪Shows the presence of a aldehydic group and a primary alcohol

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GLUCOSE: STRUCTURAL ELUCIDATION

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GLUCOSE: STRUCTURAL ELUCIDATION
▪Confirms the presence of 5 OH groups.

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 GLUCOSE: STRUCTURAL ELUCIDATION
▪On the basis of above reactions, its configuration was given as:

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GLUCOSE: OBJECTIONS AGAINS OPEN
STRUCTURE
▪even though contains -CHO group but does not react with NaHSO 3,
ammonia and Schiff's reagent.
▪The pentaacetate of glucose does not react with hydroxyl amine
indicating the absence of free-CHO group.
▪ Glucose exists in two stereoisomeric forms, α-D-glucose and β-D-
glucose with different melting points and their methods of preparation.
▪It does not give 2, 4-DNP derivative.

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GLUCOSE: CYCLIC STRUCTURE
▪ The above objections have been explained by the ring (cyclic) structure of glucose. In
the cyclic structure of glucose.
▪ -OH group at C5 and -CHO group at C combine to give a 6-membered ring (pyranose
structure). These are called Fischer Projection Formulae.

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 GLUCOSE: CYCLIC STRUCTURE
▪The above cyclic structures can also be represented by hexagonal structure (Haworth
Projection formulae).

▪The above optical isomers are also called as Anomers as differ only in the configuration of C-
1 position (anomeric carbon).
▪Anomeric carbon is also called as glycosidic carbon.
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GLUCOSE: CYCLIC STRUCTURE
▪In aqueous solution, glucose rapidly interconverts between straight and
cyclic forms as shown below

▪The spontaneous change in specific rotation of an optically active compound

with time to an equilibrium value is called mutarotation.

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D & L FORMS OF MONOSACCHARIDES
▪'D' and 'L' have no relation with the optical activity of the
compound.
▪ D – (+) Glyceraldehyde is taken as a reference

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FRUCTOSE

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FRUCTOSE - CYCLIC STRUCTURE

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FRUCTOSE- FISCHER
PROJECTION FORMULA

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FRUCTOSE: FURANOSE FORM
It can also exist in
five membered ring
form (furanose
form) mainly when
it is present in a
disaccharide.

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DISACCHARIDES
It is made up of two monosaccharide units joined together by glycosidic linkage
SUCROSE: (CANE SUGAR, C12H22O11)

▪It is obtained commercially from cane sugar or sugar beets.

▪ On hydrolysis it gives equimolar mixture of D-(+)-glucose and D-(-)-
fructose.
▪ It is a non-reducing sugar.
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INVERT SUGAR

▪ Dextrorotatory sucrose upon hydrolysis yields dextrorotatory glucose and laevorotatory

fructose.
▪ The dextrorotation of glucose (+ 52.5°) is less than the laevorotation of fructose (-92.4°)
▪ so the mixture is laevorotatory.
▪ Upon hydrolysis, the sign of rotation changes from dextro (+) to laevo (-).
▪ Hence, the product is known as invert sugar.
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MALTOSE (MALT SUGAR, C12H22011)
▪It is composed of two a-D-glucose units in which C 1 of one glucose
unit is linked to C4 of another glucose unit.
▪It is a reducing sugar as the free aldehydic group can be produced
at C1 of the second glucose unit in solution.

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LACTOSE (MILK SUGAR, CI2H22011)

▪It is composed of B-D-galactose and B-D-glucose.

▪ It is a reducing sugar.

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 POLYSACCHARIDES
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Polysaccharides are composed of large number of monosaccharide units joined
together by glycosidic linkages.
 STARCH [AMYLOSE, (C6H10O5)N
▪It occurs as microscopic granules in the roots, tubers and seeds of plants.
▪ It is dietary source for human beings.
▪ Starch consists of Amylose ( water soluble) and Amylopectin (water
insoluble)

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 STARCH [AMYLOSE, (C6H10O5)N
▪It is a polymer of α-glucose and consists of amylose and amylopectin.
Amylose is water soluble component and makes 15-20% of starch. It consists
of 200-1000 a-D-(+) glucose units held by C1-C4 glycosidic linkage. It is a
long unbranched chain.

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 STARCH [AMYLOPECTIN, (C6H10O5)N
▪ Water insoluble amylopectin has a structure similar to that of amylose with the
exception that in amylopectin the chains are branched. It constitutes about 80-
85% of starch.

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 CELLULOSE
▪It is a straight chain polysaccharide exclusively occurs in plants.
▪ It is composed only of B-D-glucose units which are joined by
glycosidic linkage between C1 of one glucose unit and C4 of the next
glucose unit.

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GLYCOGEN
▪Itis an energy storage molecule and is also called animal starch.
▪ It occurs in liver, muscles and brain and is broken down into
glucose.
▪ It is also found in yeast and fungi.

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IMPORTANCE OF CARBOHYDRATES
▪They act as store house of chemical energy for the functioning of
living organisms.
▪ They are essential components of nucleic acids.
▪ They form structural materials for cells and are essential
component of ATP.

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PROTEINS
 PROTEINS
▪Chemically proteins are the polymers of amino acids with molar mass
ranging up to more than 50 million.

▪ About 15% of the human body weight is protein.

▪ Amino acids contain amino (-NH2) and carboxyl (-COOH) function groups.
▪Only α-amino acids are obtained on hydrolysis of proteins.

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CLASSIFICATION OF AMINO ACIDS
ACIDIC BASIC NEUTRAL
More carboxyiic More amino groups Equal number of
acids than amino than carboxylic acids amine and carboxylic
group acids

ESSENTIAL NON-ESSENTIAL
AMINO ACIDS AMINO ACIDS
• Not synthesised in the body • Synthesised in the body
but, they are essential to our diets

▪Out of 20, 10 are essential amino acids and 10 are non-essential amino acids
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 Zwitter ion:

▪Net positive and negative charges are equal, molecule as a whole is neutral.
▪ The pH at which it forms is isoelectric point.
▪ This structure is also known as internal salt.
▪ Here, amino acids show amphoteric behaviour.
▪ On passing electricity, the dipolar ion does not migrate to any electrodes
▪ At isoelectric point, solubility reduces (used in separation)
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 PEPTIDES AND PROTEINS

▪Amino acids condense (eliminate water) forming a peptide.

▪Two amino acids form a dipeptide.
▪ > 10 amino acids form a polypeptides
▪ > 100 amino acids form a protein (mol. Mass > 10000 u)

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STRUCTURE OF PROTEINS
▪Primary structure
▪ Secondary structure
▪ Tertiary structure

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DENATURATION OF PROTEINS
▪When this native protein is subjected to physical change like
temperature, pH etc, the hydrogen bonds are disturbed.
▪ So that globules unfold and helix gets uncoiled. Thus, protein
loses its biological activity. This is called denaturation of protein.
▪ During this, 2° and 3° structures are destroyed but 1° structure
remains intact. For example,
▪ Coagulation of egg while on boiling, curdling of milk.

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ENZYMES
▪Enzymes are biological catalysts and catalyze the biochemical reactions.
Almost all enzymes are globular proteins
▪ Enzymes show specificity for both, the reaction and the substrate.
▪ They act as catalysts by lowering the activation energy. They are needed
only in small quantity.
▪ Depending upon enzyme, the degree of specificity shown for the
substrates can vary widely.

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 HORMONES
▪Hormones function as chemical messengers in the body. They are produced in
the endocrine glands and travel to the organs and tissues in the blood stream.

▪ Chemically they may be steroids, (e.g., estrogen and androgen), polypeptides

(eg insulin and endorphins) or amino acid derivatives (e.g, epinephrine and
norepinephrine).
▪ Hormones affect growth and development , metabolism, sexual functions and
reproduction. They also affect moods. Insulin and glucagon regulate the level
of glucose in the blood.
▪ Steroid hormones regulate tissue growth and reproductive processes and are
secreted by gonads and adrenal cortex.

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 VITAMINS
▪These organic compounds are required in small amounts in the diets of
animals in order to ensure healthy growth and reproduction.
▪ Most of them cannot be synthesized in our body but plants can
synthesize almost all of them.
▪ Classification.
▪ Fat soluble vitamins : Vitamins A, D, E and K are fat soluble and water
insoluble. They are stored in adipose tissue and liver.
▪ Water soluble vitamins : Vitamins of B group and vitamin C are water
soluble. They cannot be stored in the body (except vitamin B12) and
hence, their in take should be regular.

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NUCLEIC ACIDS
▪The nucleus of the cell transmits the inherent characters of
an individual from one generation to the next.
▪ This transmission of characters is called heredity.
▪ The nucleus consists of chromosomes which are made up
of proteins and nucleic acids.

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NUCLEIC ACIDS
▪Nucleic acids are of two types:

▪ Deoxyribonucleic Acid (DNA)

▪ Ribonucleic Acid (RNA).

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NUCLEOTIDES
▪The repeating unit (monomeric unit)
of nucleic acids are called
nucleotides.
▪ Therefore, they are regarded as
polynucleotides. A nucleotide is
consisted of :
▪ 1. A nitrogenous base (nitrogen
containing heterocyclic base).
▪ 2. A pentose sugar.
▪ 3. A phosphate group
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A NITROGENOUS BASE
▪ There are two types of nitrogenous base known as purines and pyrimidines.
▪ Purines : Two purines found in nucleic acids are
▪ adenine (A) and guanine (G).
▪ Pyrimidines : Three pyrimidines in nucleic acids are
▪ uracil (U), thymine (T) and cytosine (C).
▪ DNA contains A, G, T and C but RNA contains A, G, U and C.

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A PENTOSE SUGAR :
▪ There are two types of sugars present in the nucleic acids RNA contains B-D-ribose but in
DNA, there is B-D-2-deoxyribose.

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A PHOSPHATE GROUP
▪ They are responsible for the linkage in nucleic acid polymers.
▪ The phosphate group is bonded to a hydroxyl group of sugars.

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NUCLEOSIDES AND
NUCLEOTIDES
▪ A nucleoside consists of only two basic components i.e., a pentose sugar and a
▪ nitrogenous base. Depending upon the type of the sugar present, nucleosides
▪ are of two types: () Ribonucleosides and (ii) De0xyribonucleosides.
▪ Anucleotide contains all the basic components ofnucleic acid i.e, aphosphoric
▪ acid group, a pentose sugar and a nitrogenous base.
▪ When a large number of nucleotides are connected, we get polynucleotide.

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Name Solubility Food Sources Deficiency Diseases
Vitamin A Fat Green leafy vegetables, ripe yellow fruits, guava, Hyperkeratosis, night
milk, liver, nuts, tomatoes, oranges, carrots, broccoli, blindness, and keratomalacia
watermelon etc.

Vitamin B1 (Thiamine) Water Fresh fruits, potatoes, sweet potatoes, peas, corn, Beriberi
cashew nuts, wheat, milk, black beans, dates etc.

Vitamin B2 (Riboflavin) Water Banana, dates, mushrooms, grapes, mangoes, peas, Slow growth, sore eyes
pumpkin, popcorn etc.
Vitamin B3 (Niacin) Water Meat, fish, eggs, milk products, cereals, mushroom, Pellagra
guava etc.
Vitamin C Water Fresh fruits, black currant, broccoli, goat milk and Scurvy
chestnuts.
Vitamin D Fat Fish, egg, liver, beef, cod, chicken breast etc. Rickets and Osteomalacia
Vitamin E Fat Potatoes, pumpkin, guava, mango, milk, nuts, seeds Heart problems, Haemolysis
etc. and sterility
Vitamin K Fat Tomatoes, broccoli, chestnuts, cashew nuts, beef, Haemorrhage
lamb, mangoes, grapes etc.

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OUR FRESH PRODUCE
PROMISE

LOCAL FRESH DELICIOUS

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PRIMARY STRUCTURE
▪ The sequence of amino acid residues in polypeptide or protein, is called primary structure.
▪ Any change in the primary structure creates a different protein.

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SECONDARY Secondary structure refers to regular, local structure of the
protein backbone, stabilised by intramolecular and sometimes
STRUCTURE intermolecular hydrogen bonding of amide groups.

There are two common types of secondary structure (Figure 11).

The most prevalent is the alpha helix.

The alpha helix (α-helix) has a right-handed spiral

conformation, in which every backbone N-H group donates a
hydrogen bond to the backbone C=O group of the amino acid
four residues before it in the sequence.

The other common type of secondary structure is the beta

strand. A Beta strand (β-strand) is a stretch of polypeptide chain,
typically 3 to 10 amino acids long, with its backbone in an
almost fully extended conformation. Two or more parallel or
anti-parallel adjacent polypeptide chains of beta strand
stabilised by hydrogen bonds form a beta sheet. For example,
the proteins in silk have a beta sheet structure. Those local
structures are stabilised by hydrogen bonds and connected by
tight turns and loose, flexible loops.

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TERTIARY STRUCTURE
▪ This structure represents overall folding of the polypeptide chains ie, further folding of the secondary structure.
▪ Fibrous and globular structures arise due to tertiary structure.
▪ Fibrous Proteins
▪ When a large number of amino acids (more than ten) are combined, the products are called polypeptides. A polypeptide
▪ with more than hundred amino acid residues having molecular mass higher than 10000 u is called a protein.
▪ Alanine
▪ Structure of Proteins
▪ These types of proteins consist of linear thread like molecules which
▪ tend to lie side by side to form fibres. The molecules are held together
▪ at many points by hydrogen bonds or disulphide bonds. They are
▪ usually insoluble in water. For example, keratin in skin, hair, nails and
▪ wool; collagen in tendons; fibroin in silk; myosin in muscles etc.
▪ 2. Globular Proteins
▪ In thistype of proteins, the molecules are folded together into compact
▪ units forming spheroidal shapes. They are held together by hydrogen
▪ bonds and are soluble in water or aqueous solutions of acids, bases or
▪ salts. For example, albumin, insulin. As compared to fibrous proteins,
▪ they are very sensitive to small changes in temperature and pH.

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HARVESTING SEASONS
9
Jul; 8
8
Feb; 7 Nov; 7
7
Oct; 6
6
Jan; 5 May; 5 Sep; 5
5
Aug; 4 Dec; 4
4
Apr; 3
3
Mar; 2
2
Jun; 1
1

0
Jan Feb Mar Apr May Jun Jul Aug Sep Oct Nov Dec

Row

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OUR PROCESS

Plant

Grow

Pick

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