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UNIT-1

What should I eat?


Identify the cell structure.
What molecules make up or are used by the different cell structure
Nucleus
Cytoplasm
Endoplasmic Reticulum
Mitochondria

Cell Membrane

Ribosome
Chemical Elements
•Most of the molecules in living organisms fall into three
categories: carbohydrates, proteins and lipids
•These all contain carbon and so are described as organic
molecules
What are the most frequently occurring chemical elements in
living things?

• Carbon

• Hydrogen

• Oxygen

• Nitrogen
CARBOHYDRATES
 Largestgroupof organiccompounds.

 Compounds made upof carbon, hydrogen, and oxygen atoms usually in a ratioof 1:2:1.

 General Formula : Cm(H2O)n .

 Carbohydratesare sugars thatgenerallyend in –ose.

 Carbohydrates, in general, are used forstructure and energy.

 Carbohydrate monomers are joined through condensation reactions.

 Carbohydrate monomers aresplit through hydrolysis reactions.

 Single sugarmoleculesarecalled monosaccharides.

 The large macromolecules formed from monosaccharides are known as polysaccharides.


Glucose
Starch

Glucose
5
Other carbohydrates
2 molecules of glucose can sucrose is formed when
join together to form a a molecule of glucose and
molecule of maltose a molecule of fructose combine

Starch and cellulose are


formed from hundreds of
glucose molecules joined
maltose to form a long chain

part of a starch
molecule
EXAMPLES OF CARBOHYDRATES
Name Type Monomer Unit Example Function
Glucose Monosaccharide - Chemical fuel
Ribose Monosaccharide - Component of RNA
Galactose Monosaccharide - Chemical fuel
natural simple sugar found in fruits,
honey, and vegetables
Fructose Monosaccharide - Like glucose, fructose is a source
of energy for the cells
Lactose Disaccharide Glucose + Galactose Solute in milk
Sucrose Disaccharide Glucose + Fructose Table sugar, transports sugars in plants
Found in germinating seeds as starch is
Maltose Disaccharide Glucose + Glucose
broken down
Starch Polysaccharide Glucose (n) Stores energy in plants
Cellulose Polysaccharide Glucose (n) Forms cell walls in plants
Glycogen Polysaccharide Glucose (n) Stores glucose in liver and muscles
LIPIDS
• Lipids are used as energy storage molecules in plants and
animals.

• Lipids are generally water insoluble.


• Lipids provide the structural components of membranes.
• Fatty-acids are simplest form of lipids.
• Most fats (lipids) in the body are made up of triglycerides
• Their basic unit is 1 glycerol molecule chemically bonded
to 3 fatty acid chains

• The fatty acids vary in size and structure


• Lipids are divided into fats (solids at room temperature)
and oils (liquids at room temperature)

• A fatty acid has a carboxyl group attached to an R group.


• The R group could be a methyl (–CH3), or ethyl (–C2H5) or
higher number of –CH2 groups (1 carbon to 19 carbons).
 Fatty acids could be saturated or unsaturated.

 They can be then monoglycerides, diglycerides


and triglycerides.

 These are also called fats and oils based on


melting point. Oils have lower melting point
and hence remain as oil in winters.

 Animals store energy as fat whereas plants


store oils (olive oil).

 Some lipids have phosphorous and a


phosphorylated organic compound in them.
These are phospholipids.

 They are found in cell membrane. Lecithin is


one example.
AMINO ACIDS & PROTEINS
• Proteins are an important class of biological macromolecules which are the polymers of amino acids.

•There are about 20 different amino acids

They all contain the same basic structure but the ‘R’ group is different for each one

•When amino acids are joined together a protein is formed

•The amino acids can be arranged in any order, resulting in hundreds of thousands of different proteins

•Even a small difference in the order of the amino acids results in a different protein being formed

• A peptide is a composed consisting of two or more amino acids.


• Peptide chains of more than 12 and less than about 20 amino acid residues are usually referred to as
oligopeptides.
• Many amino acids joined together in chain is know as Polypeptide.
Amino Acids

Carboxyl group

General structure Alanine Serine


PROTEINS

Amino
Acids

https://www.youtube.com/watch?v=HSCUAjZQhXI
PROTEINS (FUNCTIONS)

 Enzymes (catalyze chemical reactions)


 Antibodies (fight infection)
 Structural functions
 Movement
 Repair / maintenance
 Energy
 Some hormones
 Transportation and storage of
molecules
HUMAN DIGESTIVE SYSTEM
THE HUMAN DIGESTIVE SYSTEM
The Stages of Food Breakdown

•Food taken into the body goes through 5 different


stages during its passage through the alimentary
canal (the gut):

• Ingestion – the taking of substances, e.g. food


and drink, into the body through the mouth
• Mechanical digestion – the breakdown of
food into smaller pieces without chemical
change to the food molecules
• Chemical digestion – the breakdown of large,
insoluble molecules into small, soluble
molecules
• Absorption – the movement of small food
molecules and ions through the wall of the
intestine into the blood
• Assimilation – the movement of digested food
molecules into the cells of the body where
they are used, becoming part of the cells
• Egestion – the passing out of food that has not
been digested or absorbed, as faeces, through
the anus.
How Do Enzymes Work?
Enzyme Specificity
•Enzymes are specific to one particular substrate(s) as the active site of the enzyme, where the substrate attaches, is a complementary shape
to the substrate
•This is because the enzyme is a protein and has a specific 3-D shape
•This is known as the lock and key hypothesis
•When the substrate moves into the enzyme’s active site they become known as the enzyme-substrate complex
•After the reaction has occurred, the products leave the enzyme’s active site as they no longer fit it and it is free to take up another substrate
Substrate: A substrate is a molecule acted upon by an enzyme. It is
the reactant present at the beginning of the reaction.

Active Site: The substrate molecules interact or bond with the enzyme
molecules at some specific regions or sites on the enzyme. Such sites of
attachment are variously called as ‘active sites’ or ‘catalytic sites’ or ‘substrate
sites’.

Product: The final substance formed after the reaction.


I

II
EXAMPLES OF ENZYMES:

1. Amylase

2. Protease

3. Starch phosphorylase

4. Carbohydrase

5. Lipase

6. Maltase

7. Sucrase
EXAMPLES OF ENZYMES:

1. Amylase: Breakdown of Starch

2. Protease: Breakdown/digestion of proteins into amino acids.

3. Starch phosphorylase: Synthesis starch from glucose molecules in


plants.

4. Carbohydrase: Breakdown/digestion of carbohydrate

5. Lipase: Breakdown/digestion of fats/lipids

6. Maltase: Breakdown/digestion of maltose

7. Sucrase: Breakdown/digestion of sucrose


ENZYME ACTIVITY
FACTORS AFFECTING ENZYME ACTIVITY
TEMPERATURE & ENZYME ACTIVITY

At low temperatures, an increase


in temperature increases the rate of an enzyme-
catalyzed reaction.

At higher temperatures, the protein is denatured,


and the rate of the reaction dramatically
decreases.

An enzyme has an optimum temperature range in


which it exhibits maximum activity.

In human body the optimum temperature is 40


degree Celsius after which the enzymes starts to
denature.
PH & ENZYME ACTIVITY
An enzyme has an optimum pH range in which it exhibits maximum activity. The optimum pH
is specific for individual enzymes.
Enzyme Investigations

•Amylase is an enzyme that digests starch (a polysaccharide of glucose) into maltose (a disaccharide of glucose).
•Starch can be tested for easily using iodine solution.
Investigating the Effect of Temperature on Amylase
•Starch solution is heated to a set temperature
•Iodine is added to wells of a spotting tile
•Amylase is added to the starch solution and mixed well
•Every minute, droplets of solution are added to a new well of iodine solution
•This is continued until the iodine stops turning blue-black (this means there is no more starch left in the solution as the amylase has
broken it all down)
•Time taken for the reaction to be completed is recorded
•Experiment is repeated at different temperatures
•The quicker the reaction is completed, the faster the enzyme is working
Investigating the Effect of pH on Amylase Activity

•Place single drops of iodine solution in rows on the tile

•Label a test tube with the pH to be tested

•Use the syringe to place 2cm3 of amylase in the test tube

•Add 1cm3 of buffer solution to the test tube using a syringe

•Use another test tube to add 2cm3 of starch solution to the amylase and buffer solution,

start the stopwatch whilst mixing using a pipette

•After 10 seconds, use a pipette to place one drop of mixture on the first drop of iodine,

which should turn blue-black

•Wait another 10 seconds and place another drop of mixture on the second drop of iodine

•Repeat every 10 seconds until iodine solution remains orange-brown

•Repeat experiment at different pH values – the less time the iodine solution takes to remain

orange-brown, the quicker all the starch has been digested and so the better the enzyme

works at that pH

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