Culinary consultants

Concept Developers
Food Designers

Nutrients in Food
The Major Food
Groups
The Six Major Nutrients in
Food,
 Carbohydrates,
 Lipids (fats/oils)
 Proteins
 Mineral salts (eg. Ca, Fe and K compounds)
 Vitamins (eg. Vitamin C & D)
 Water
Carbohydrates

 Function
 Energy source
 Dietary Fibre
 Typical Sources
 Potatoes Honey
 Bread Celery
Lipids (Fats & Oils)

 Function
 Energy source
 Typical Sources
 Margarine
 Butter
 Oils
Proteins

 Function
 Growth & repair of tissues
 Control of reactions
 Energy source
 Typical Sources
 Meat Fish
 Broad beans Lentils
Mineral Salts

 Function
 Various specialised roles
 Typical Sources
 Meat
 Vegetables
 Dairy products
Vitamins

 Function
 Various specialised roles
 Typical Sources
 Milk
 Meat
 Vegetables
 Fruit
Water

 Function
 Solvent
 Transport agent
 Hydrolysis reactions
 Typical Sources
 Drinks
 Fruit
 Vegetables
Human Digestive System

 Mouth
 Food is chewed into small pieces
 Food begins to react
 Reaction catalysed by enzymes in saliva
 Stomach
 Food is further broken down in combined action of
hydrochloric acid and enzymes present in gastric juice
Human Digestive System

 Small Intestine
 Mixture of enzymes act on the food
 Enzymes come from pancreas & wall of duodenum
 Simple substances produced are absorbed into blood
stream and transported to various parts of the body
Human Digestive System

 Large Intestine
 Water is absorbed from remaining undigested food
 Undigested food contains large proportion of dietary fibre
 Bacteria in colon ferment some of the fibre producing
useful small molecules
 These are absorbed into bloodstream
 Remaining undigested matter is excreted
 Chemical Processes Occuring to
Digested Food
Immediate use as an
Digestion (Hydrolysis energy source
using enzymes
Absorption
Polysaccharides
(starch) Monosaccharides
Fatty acids
Fats Amino Acids (Condensation using
Proteins
enzymes)

Food containing large Small molecules

Glycogen
molecules Fats
Proteins

Large molecules for storage or

other purposes
Carbohydrates :
Composition and
Occurrence 
 Carbohydrates make up more than 50% of organic
matter found on earth and are the major component of
plants.
 They contain the elements carbon, hydrogen and
oxygen and usually have the formula Cx(H2O)Y (where x
and y are whole numbers).
 
Carbohydrates

 They range in size from small molecules to very large

polymers and can be classified as:
 i) monosaccharides (e.g. glucose)
 
ii) disaccharides (e.g. sucrose)
 
iii) polysaccharides (e.g. cellulose)
Carbohydrates

 Typical food sources include bread, cereals, honey,

potatoes, grains, flours, Pastries etc.
 Detailed knowledge of carbohydrate structures (e.g.
valence structures) is not required in this area of study.
 
Monosaccharides

 These are the simplest carbohydrates

 (mono = one)
 are sweet, white solids which are very soluble in water.
Monosaccharides

 Glucose,fructose and galactose all have the same

molecular formula (C6H12O6)
 but their structures, all of which are cyclic, are slightly
different;
 they are examples of structural isomers.
 A pictorial structure diagram of glucose and galactose
may be drawn as (a hexose) and that of fructose
drawn as (a pentose).
Monosaccharides

 All three isomers contain a number of hydroxy (‑OH)

groups in their cyclic
structures
 hydrogen bonding exists between monosaccharide
molecules and solvent water molecules
 this enhances their solubility.
Glucose

 the most abundant monosaccharide, is found in all living

things, including animal tissue, plant sap and fruit
Juices.
 It is a key energy source and also a monomer (building
block) for other more complex carbohydrates.
 
Fructose

 The sweetest natural sugar known, is present in honey

and many fruit Juices.
 It is a key energy source and monomer of more complex
carbohydrates.
Galactose

 while not found as a free monosaccharide, is a common

monomer of more complex carbohydrates.
 
Structure of Glucose
CH2OH

HO H H

H OH
OH H

H OH
Structure of Galactose
CH2OH

H H
H

HO OH
OH H

H OH
Structure of Fructose

HOCH2 H

HO CH2OH
H HO

HO H
Disaccharides

 These consist of 2 (di=two) monosaccharide molecules

which have reacted and have been chemically linked
together
 
2 C6H12O6(aq)  C12H22011(aq) + H2O(1)
 
Disaccharides

 This is an example of Condensation Reaction

 Where molecules react and chemically bond together
with the elimination of a small molecule (H2O in this
case)
 Condensation also because water is produced
Disaccharides

 The reverse reaction is:

 C12H22O11 (aq) + H 2O(1)  2C 6H 12O 6 (aq)
 
 This reaction occurs in the body with acids or enzymes
and is called a hydrolysis
reaction (i.e. reaction with water).
 
Disaccharides

 The most important disaccharides in terms of diet are

 Sucrose
 Maltose
 Lactose.
Sucrose

 Formed from glucose and fructose monomer units

 Commonly extracted from sugar cane and is known as
cane or table sugar.
 
Sucrose

 A pictorial structure diagram of a sucrose molecule may

be drawn as:
 G = Glucose F = Fructose
 

G F
Maltose,

 Formed from the two glucose monomer units,

 Is known as malt sugar and
 Is present in germinating grain.
 The pictorial structure diagram of a maltose molecule
may be drawn as:
 
 

G G
Lactose,

 formed from glucose and galactose monomer units,

 the main carbohydrate found in milk and is known as
milk sugar.
 pictorial structure diagram of a lactose molecule may
be drawn as:
 G = Glucose Ga = Galactose
 

G Ga
Polysaccharides

 When monosaccharides react together, there is a

reaction between some of the hydroxy (‑OH) functional
groups.
 When two neighbouring ‑OH groups interact, a water
molecule is eliminated and a new covalent bond is
formed.
Polysaccharides

 This type of reaction where functional groups react

together and a small molecule is eliminated is a
"condensation" reaction.
Polysaccharides

 The new covalent bond (a strong bond) holds the

previously separate monomers together to form a larger
molecule ‑this now linkage is termed an "ether linkage."
Polysaccharides

 This can be illustrated in the following diagram.

 

CH2OH CH2OH
O O
H H H H H
H
H H H H OH
OH O

OH OH OH
OH
Polysaccharides

 This can be illustrated in the following diagram.

 

CH2OH CH2OH
O O
H H H H H
H
H H H H OH
OH O

OH OH OH
OH
Ether link
Polysaccharides

 These are polymers formed from simple sugars by

condensation polymerisation reactions and which have a
backbone consisting of C and H atoms:
 e.g. n C6H1206 (C 6H1005)n + n H2O  
monosaccharide polysaccharide
 
(n = a very large whole number)
 
Polysaccharides

 They are very large molecules with high molar masses

and, in general, have no taste nor are they soluble in
water.
 Three important examples are
 starch,
 cellulose
 glycogen.
Polysaccharides

 A general pictorial structure diagram of a section of

polysaccharide may be
drawn as:
 
Starch

 has a major role in storage of carbohydrates (glucose) in

plants
 It provides energy requirements at night when there is
no photosynthesis.  
 is obtained in foods such as cereal grains, potatoes and
rice.
 
Cellulose

 is the major structural material in plants and, thus, has

a significant abundance in the biosphere.
 It is present in such common foods as cereals, fruits and
vegetables
 plays a significant role in dietary needs as dietary
fibre/roughage.
 
Glycogen

 a soluble polysaccharide which has a

major role of
 glucose storage in animals as energy is
required,
 glycogen undergoes a hydrolysis
reaction producing glucose and
providing energy.
 This is effectively the reverse of the
condensation polymerisation e.g.
 ( C6H10O5 )n + n H2O .n C6H12O6
Digestion of Polysaccharides

 Starch and glycogen can be broken down with enzymes

in hydrolysis reactions to form maltose (a disaccharide)
and ultimately glucose (a monosaccharide) which is
absorbed in the body.
 A general diagram can be drawn as follows:
 
Digestion of Polysaccharides
Starch or Glycogen

Enzyme catalysed hydrolysis during

digestion

Maltose

Enzyme catalysed hydrolysis during

digestion

Glucose
Digestion of Polysaccharides

 Most cellulose is not broken down by our digestive

systems but, as mentioned above, is utilised as dietary
fibre/roughage which of great benefit to the proper
functioning of our bodies.
 
Lipids (Fats and Oils)
 
Composition and Occurrence

 Lipids mainly contain the elements carbon and hydrogen

with small amounts of oxygen and sometimes other
elements.
 • Most are essentially non‑polar so they tend to
dissolve in non‑polar solvents but not in polar solvents
such as water.
• Fats and oils are the most common lipids with fats
being solid at normal temperatures whereas oils are
liquids.
Lipids (Fats and Oils)

 Typical food sources include oils, butter, margarine,

some meats, nuts etc.
 Their major role is as an energy source and to provide
insulation ‑ fats/oils provide more than twice as much
energy, per gram, as carbohydrates or proteins.
 
Formation of Lipids

 Most fats/oils are produced by a condensation reaction

between a glycerol molecule and 3 fatty acid
molecules;
 in this reaction, water is released and the product of
the reaction is referred to as a triglyceride.
 An example is shown below:
 Formation of Lipids
H

H C OH

H C OH

H C OH

glycerol
 Formation of Lipids
H O

H C OH OH C R
O

H C OH
+ OH C
O
R

H C OH
OH C R
H

glycerol 3 fatty acid

molecules
 Formation of Lipids
H O H O

H C OH OH C R H C OH OH C R
O O

H C OH
+ OH C
O
R
H C OH
OH C
O
R

H C OH H C OH
OH C R OH C R
H H

glycerol 3 fatty acid

molecules
 Formation of Lipids
H O H O

H C OH OH C R H C O C R
O O

H C OH
+ OH C
O
R
H C O
C
O
R

H C OH H C O
OH C R C R
H H + 3 H2O
glycerol 3 fatty acid
molecules
 Formation of Lipids
O
H O H
C R
H C OH OH C R H C O
O
O

H C OH
+ OH C
O
R
H C O C
O
R

H C OH H C O C R
OH C R
H H + 3 H2O
glycerol 3 fatty acid
molecules A triglyceride
Classification of Fats

 This depends on structural features of the fatty acid

from which the fat (triglyceride) is made.
 a) Saturated fats
 The fatty acid contains C‑C single bonds only.
 These fats are generally waxy, unreactive solids.  
Classification of Fats

 b) Mono‑unsaturated fats
 The fatty acid contains one C=C (double bond).
 c) Poly‑unsaturated fats
 The fatty acid contains more than one C=C double bond.
 These are often liquids and are more reactive.
 
Digestion of Fats

 This occurs mainly in the small intestine

where bile (produced in the liver and
stored in the gall bladder) converts the
fat into an emulsion.
 Enzymes catalyse the hydrolysis of fat
back to glycerol and fatty acids (once
again, the reverse of the condensation
reaction); these small molecules are
absorbed by the body.
 After absorption, these are re‑converted
by enzymes into triglycerides (in a
condensation polymerisation reaction).
Functions of Lipids

 Fats are used by the body as

 i) an energy source

 ii) a heat insulator

 iii) a shock insulator (for internal organs),

Phospholipids,

 an important group of complex lipids,

form the main constituent of cell
membranes.
 are complex lipids, which together
with proteins, make up the major
components of cell membranes.
 Like fats, phospholipids are also esters
of glycerol but they contain only two
fatty acids.
 The third carbon atom from the
original glycerol molecule is attached
to a phosphate group.
Structure of Palmitic Acid,

 A Saturated Fat
 CH3 (CH2)14 COOH
Structure of Aleic Acid

 A Mono Saturated Fat

 CH3 (CH2)7 CH ==CH (CH2)7 COOH
 Structure of Linoleic Acid

 A Polyunsaturated Fat

CH3 (CH2)4 CH ==CHCH2CH==CH (CH2)4 COOH

Proteins
Composition and Occurrence

 Proteins are of major importance, being present in

every cell and crucial to both cell structure and
functioning.
 They comprise between 15% and 20% of the human
body, contributing an average of 67% of the dry weight
of cells.
 
Proteins

 There are many hundreds of different types of proteins

which have specific purposes either as the basic
structural material for the repair and growth of tissues
or in the body's metabolism.
 They contain the elements carbon, hydrogen, nitrogen,
oxygen and often sulphur.
Functions of Proteins

 The main function of proteins is for building new tissues

and maintaining existing tissues.
 Apart from this role they play a crucial part in the
body's metabolism.
Functions of Proteins

 Cells use proteins in a range of ways ‑

 to act as biological catalysts (enzymes),
 in communication through nerves,
 in regulation of the body's metabolism with hormones,
 as haemoglobin in the transport of oxygen in the blood and
 as protective agents against disease.
Protein Monomers

 Proteins are polymers (very large molecules) that are

composed of large numbers of smaller molecules called
monomers.
 The monomers from which proteins are constructed are
called "a‑amino acids".
 
Amino Acids

 are named as such (i.e. as "a" because the

amino (‑NH 2) functional group is on the first
carbon atom that is bonded to the carboxyl
(‑COOH) functional group.
 They are also known as 2‑amino acids with
the first carbon being the carbon that is part
of the carboxyl (‑COOH) functional group and,
thus, the amino (‑NH 2) functional group is
attached (bonded) to the second carbon
atom.
 they will be referred to as a‑amino acids for
simplicity.
 
Amino Acids

  The general formula of an a‑amino acid is: 

 where Z represents an organic group.
 

H O
Z
C C
OH
NH2
Amino Acids

 a‑amino acids contain a carboxyl group (‑COOH) and an

amino group (‑NH 2) on the next carbon atom.
 Two simple a‑amino acids are:
 
 
Glycine

Z=H
H O
H
C C
OH
NH2
Alanine

Z = CH3
CH3 H O
C C
OH
NH2
Amino Acids

 Unlike animals and humans, plants can manufacture all

their required amino acids from inorganic ingredients.
Non Essential Amino Acids

Humans are able to internally manufacture only 11 of the

20 amino acids which are necessary to produce the
range of required proteins ‑
those 11 are referred to as non‑essential amino acids
because an external food source is not required for
their production.
Essential Amino Acids

The remaining 9 amino acids needed for protein synthesis

must be provided by our food intake.
They are referred to as essential amino acids because an
external food source is required to obtain them.
 
Functional Groups

The carboxyl group (‑COOH) and amino (‑NH 2) group are

examples of "functional groups".
These are a small group of atoms that attach to a longer
organic 'backbone' and which give the organic molecule
particular properties (or 'functions').
Carboxyl Group (COOH)

The carboxyl group (‑COOH) is found in a family of organic

compounds called 'carboxylic acids'; the ‑COOH group
can act as an acid.
Amino Group (NH2)

The amino group (‑NH2) is found in another family of

organic compounds called ' amines';
the ‑NH2 group can act as a base.
Amino Group (NH2)

As mentioned above, every amino acid contains two

functional groups ‑ an amino group (‑NH 2) and a
carboxyl group (‑COOH).
The amino group can act as a weak base (H+ acceptor)
whereas the carboxyl group can act as a weak acid (H+
donor).
Alanine

In a low pH solution (acidic solution), the amino group,

being a base, will react with the acid in solution, accept
a hydrogen ion and form ‑NH +
Alanine

For example, the structural formula for alanine is usually

drawn as:
 

CH3 H O
C C
OH
NH2
Alanine in Acidic Solution

In a low pH (acidic) solution, the structural formula for

alanine will be:
(NB: the amino acid exists as a cation in the low pH
Solution)
 

CH3 H O
C C
OH
+
NH3
Alanine in Basic Solution

In a high pH solution the carboxyl group, being an acid, will

react with the base in solution and donate a hydrogen
ion and form the anion ‑COO‑ (aq).

CH3 H O
C C
O--
NH2
Alanine in Intermediate pH

In a solution with intermediate pH, there is not a strong

acid or base in solution
to react with acidic carboxyl group (as in the high pH
example) or the basic amino group (as in the low pH
example).
Alanine in Intermediate pH

The structure of the a‑amino acid is such

that the amino group is close to the
carboxyl group and an
"Intra‑molecular" acid‑base reaction
(H+ transfer) occurs.
The carboxyl group (‑COOH) donates H+
to the amino group (‑NH2) producing
both ‑COO‑ and ‑NH3+ on different
parts of the same molecule.
 
Alanine in Intermediate pH

Thus, the structural formula for alanine in a solution with

intermediate pH will be: 

NB: the amino acid exists as a

"zwitter‑ion" in the intermediate pH
solution ‑ i.e. a molecule with no
net charge (neutral) but with
H within it).O
CH3 parts
specific charged

C C
O--
NH3+
Formation of Proteins 

 Proteins are formed by a reaction between amino acids

(often called peptides) ‑
 this is an example of a condensation polymerisation
reaction in which water is eliminated (the same type of
reaction in which monosaccharides form
polysaccharides).
Condensation Reaction

 An example of the condensation reaction between 3

different a‑amino acids is shown below:
 
 O O O

H N C C OH H N C C OH H N C C OH

H Z1 H Z2 H Z3
 O O O

H N C C OH H N C C OH H N C C OH

H Z1 H Z2 H Z3
 O O O

H N C C OH H N C C OH H N C C OH

H Z1 H Z2 H Z3

O O O

H N C C N C C N C C OH

H Z1 H Z2 H Z3
 O O O

H N C C OH H N C C OH H N C C OH

H Z1 H Z2 H Z3

O O O

H N C C N C C N C C OH

H Z1 H Z2 H Z3
 O O O

H N C C OH H N C C OH H N C C OH

H Z1 H Z2 H Z3

O O O

H N C C N C C N C C OH

H Z1 H Z2 H Z3

Peptide Links
 Copolymers 

 The copolymers produced by the

condensation reactions of amino acids
(peptides) are called polypeptides; if
more than 50 amino acid units are
present, the polypeptide is referred to
as a protein.
 The simplest protein is the hormone
insulin (which plays an important role
in controlling the level of blood sugar);
this protein contains 51 amino acid
units.
Formation of Proteins

 An example of a polypeptide (protein) chain showing

the peptide linkages is given below:
Polypeptide (Protein)

H O H O H O H O

C C N C C N C C N C C N

CH2 H CH2 H CH2 H CH2 H

CH3 CH2 SH CH2

OH OH
Polypeptide (Protein)

H O H O H O H O

C C N C C N C C N C C N

CH2 H CH2 H CH2 H CH2 H

CH3 CH2 SH CH2

OH OH

Peptide Links
Proteins

 Proteins differ with respect to the number, type and

sequence of their constituent amino acids.
 
Protein Structure 

 Each protein performs a particular function in the body.

 A significant aspect of chemical functions of proteins
relates to their structure which needs to be considered
on three levels in what is termed "primary structure',
'secondary structure' and tertiary structure'.
Primary Structure

 The 'primary structure' of proteins refers to

the number and sequence of amino acids in
the polypeptide chain.
 The human body is thought to contain over
one hundred thousand different proteins and
these, as mentioned above, are constructed
from only 20 different amino acids!
 This situation is often compared to the
existence of only 26 letters in the English
alphabet but the enormously large number of
words that can be formed with these 'building
blocks'.
 
Secondary Structure

 The of proteins refers to the coiling, folding or pleating

of the protein chains into particular three‑dimensional
arrangements.
 This is due to the attractive forces of the dipoles
present in the polar ‑CO and ‑NH sections of the
polypeptide backbone ‑ this involves "hydrogen
bonding'.
Tertiary Structure

 The of proteins refers to the manner in

which the coiled polypeptide chains are
folded and describes the overall
three‑dimensional shape of the protein.
 The Z‑groups in the amino‑acid units are
often bulky and prevent the protein from
adopting a particular shape.
 A number of factors may play a role in
determining the overall three‑dimensional
shape of a protein.
Tertiary Structure

 These include cross‑links (with covalent bonds) between

the chains, ion‑Ion and ion‑dipole attractions and
dipole‑dipole attractions, including hydrogen bonding.
 
Result of Structures

 As a result there is great variety in protein shapes.

 Some proteins have a flat sheet structure, others are
compact, globular shapes while others consist of long
fibrous strands.
Digestion of Proteins

 During digestion, the proteins in food

are broken down by enzymes in the
stomach and small intestine into their
constituent amino acids.
 This is a hydrolysis reaction (similar in
type to the reaction in which
polysaccharides are broken down
during digestion) and
 is the reverse of the condensation
reaction in which the original protein
was formed.
Digestion of Proteins

 The amino acids that are produced in this

hydrolysis reaction are absorbed into the
bloodstream and eventually into the cells
which use them to manufacture proteins,
depending on the part of the body
involved.
 As the body does not store proteins, a
balanced intake of protein is required
daily.
 Unused protein is broken down in the liver
and unwanted nitrogen atoms are
eventually eliminated in the urine as urea
((NH2)2CO).
Denaturation of Proteins

 The 'denaturation' of a protein refers to any change that

destroys the biological functioning of the protein.
 As mentioned above, protein structure is crucial to the
biological functioning of proteins and changes in
conditions can disrupt protein structure and, as a
consequence, alter the biological activity
Denaturation of Proteins

 Such changes in conditions would include:

 
‑ a change in pH
‑ an increased temperature
 
‑ the addition of other chemicals.
 
Denaturation of Proteins

 In the denaturation process, there is an unfolding and

possibly unwinding of the protein helical structures.
 The unfolded chains intertwine and come into close
contact; as a result, large clumps of protein molecules
tend to form ‑ this is termed 'coagulation'.
Denaturation of Proteins

 Common examples of protein

denaturation include:
 the change in egg white when the egg
is cooked
 ‑cooking meat
 ‑ the curdling of milk in the presence
of an acid: for example, the addition
of vinegar or lemon juice or the
presence of lactic acid which is due to
the action of bacteria as milk sours.
Enzymes

 Enzymes are biological catalysts because. they increase

the rate of chemical reactions
that occur in the body.
 Biological reactions often occur in a number of stages
with each of these stages being controlled by a specific
enzyme.
 
Enzymes

 Enzymes are proteins.

 Enzymes and inorganic catalysts are thought to be
similar in that they accelerate the rate of chemical
reactions by lowering the 'Activation Energy' barrier for
the reaction
 ‑ i.e. they provide a lower activation energy pathway
for the reaction
Difference of Inorganic
Catalysts and Enzymes
 Enzymes produce much .faster
reaction rates.
 Enzymes operate under much milder
conditions ‑ lower temperatures (body
temperature compared with the high
industrial temperatures) and a narrow
temperature range.
 Enzymes are very selective in their
catalytic function.
Selectivity of Enzymes

 It is not unusual to find an inorganic

catalyst being effective for a number of
reactions.
 An enzyme, on the other hand, is an
effective catalyst for a specific reaction.
 The specificity of enzymes is
demonstrated, for example, by the
digestion of starch but not cellulose in the
human body.
 Both of these are polysaccharides but the
body does not contain the necessary
enzyme to break down the cellulose
polymer.
Thank you,

Harsh Deep Mishra

harshdeepmishra@gmail.com
www.angelsandachef.com
Hand phone - +91 75688 18304
Whatsapp – +91 97997 57159