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Multicellular organisms have many levels of organisation
Cells are the basic building blocks of all living organisms Your notes
Unicellular organisms are made from one cell, whereas multicellular organisms are made up of
collections of cells
In complex multicellular organisms, cells are specialised to carry out particular functions. These
specialised cells form tissues, which form organs in organ systems
In humans, the digestive system (provides the body with nutrients) and the respiratory system
(provides the body with oxygen and removes carbon dioxide) are examples of organ systems that
provide dissolved materials that need to be moved quickly around the body in the blood by the
circulatory system
Organisation table
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Your notes
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Your notes
The Importance of Bacteria in Digestion
The large intestine is home to hundreds of species of bacteria
These bacteria form a microbial ecosystem (the microbiota, or gut flora) that play an essential role in
human digestion of food by:
Breaking down substances we can’t digest (like cellulose)
Supplying essential nutrients
Synthesising vitamin K
Providing competition with any harmful bacteria to restrict their growth
Taking antibiotics can disrupt the gut microbiota which can cause short-term problems with digestion
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Enzymes & Metabolism
Your notes
Enzymes & metabolism
Digestive enzymes work outside of cells; they digest large, insoluble food molecules into smaller,
soluble molecules which can be absorbed into the bloodstream
Metabolism is the sum of all the reactions happening in a cell or organism, in which molecules are
synthesised (made) or broken down
Enzymes are biological catalysts made from protein
Enzymes speed up chemical reactions in cells, allowing reactions to occur at much faster speeds
than they would without enzymes at relatively low temperatures (such as human body
temperature)
Substrates temporarily bind to the active site of an enzyme, which leads to a chemical reaction and the
formation of a product(s) which are released
Enzymes remain unchanged at the end of a reaction, and they work very quickly
Some enzymes can process 100s or 1000s of substrates per second
Enzyme specificity diagram
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Enzymes are biological catalysts that work in cells, so they randomly move about wherever they are in
the cell. They don’t ‘choose’ to collide with a substrate – collisions occur because all molecules are in
motion in a liquid Your notes
How do enzymes work?
Enzymes catalyse specific chemical reactions in living organisms – usually one enzyme catalyses one
particular reaction:
Enzyme specificity of catalase to hydrogen peroxide diagram
The enzyme catalase can bind to its substrate hydrogen peroxide as they are complementary in shape,
whereas DNA polymerase is not
The specificity of an enzyme is a result of the complementary nature between the shape of the active
site on the enzyme and its substrate(s)
Enzymes have specific three-dimensional shapes because they are formed from protein molecules
Proteins are formed from chains of amino acids held together by bonds
The order of amino acids determines the shape of an enzyme
If the order is altered, the resulting three-dimensional shape changes
The lock & key model
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The ‘lock and key theory’ is one simplified model that is used to explain enzyme action
The enzyme is like a lock, with the substrate(s) the keys that can fit into the active site of the enzyme Your notes
with the two being a perfect fit
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Your notes
Diagram showing the lock and key model
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1. Enzymes and substrates move about randomly in solution
2. When an enzyme and its complementary substrate randomly collide – with the substrate fitting into the Your notes
active site of the enzyme – an enzyme-substrate complex forms, and the reaction occurs
3. A product (or products) forms from the substrate(s) which are then released from the active site. The
enzyme is unchanged and will go on to catalyse further reactions
The effect of temperature and pH on enzyme activity
The effect of temperature
The specific shape of an enzyme is determined by the amino acids that make the enzyme
The three-dimensional shape of an enzyme is especially important around the active site area; this
ensures that the enzyme’s substrate will fit into the active site enabling the reaction to proceed
Enzymes work fastest at their ‘optimum temperature’ – in the human body, the optimum temperature
is around 37°C
Heating to high temperatures (beyond the optimum) will start to break the bonds that hold the enzyme
together – the enzyme will start to distort and lose its shape – this reduces the effectiveness of
substrate binding to the active site reducing the activity of the enzyme
Eventually, the shape of the active site is lost completely and the enzyme is described as being
‘denatured’
Substrates cannot fit into denatured enzymes as the specific shape of their active site has been
lost
Enzyme denaturation diagram
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Your notes
Denaturation is largely irreversible – once enzymes are denatured they cannot regain their proper shape
and activity will stop
Increasing temperature from 0°C to the optimum increases the activity of enzymes as the more energy
the molecules have the faster they move and the number of collisions with the substrate molecules
increases, leading to a faster rate of reaction
This means that low temperatures do not denature enzymes, but at lower temperatures with less
kinetic energy both enzymes and their substrates collide at a lower rate
The effect of temperature on enzyme activity diagram
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Your notes
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This graph shows the effect of temperature on the rate of activity of an enzyme
The effect of pH Your notes
The optimum pH for most enzymes is 7 but some that are produced in acidic conditions, such as the
stomach, have a lower optimum pH (pH 2) and some that are produced in alkaline conditions, such as
the duodenum, have a higher optimum pH (pH 8 or 9)
If the pH is too high or too low, the bonds that hold the amino acid chain together to make up the
protein can be destroyed
This will change the shape of the active site, so the substrate can no longer fit into it, reducing the rate
of activity
Moving too far away from the optimum pH will cause the enzyme to denature and activity will stop
If pH is increased or decreased away from the optimum, then the shape of the enzyme is altered
The effect of pH on enzyme activity diagram
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Your notes
This graph shows the effect of pH on the rate of activity of an enzyme from the duodenum
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Required Practical: Enzymes
Your notes
Enzyme required practical
Aim: To investigate the effect of pH on the rate of reaction of amylase
You will:
Use the enzyme amylase to breakdown starch at a range of pH values, using iodine solution as an
indicator for the reaction occurring
Use a continuous sampling technique to monitor the progress of the reaction
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
Iodine can be used qualitatively to indicate the presence or absence of starch from a sample
Method
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Place single drops of iodine solution in rows on the tile
Label a test tube with the pH to be tested Your notes
Use the syringe to place 2cm3 of amylase in the test tube
Add 1cm3 of pH 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 the mixture on the first drop of iodine, which
should turn blue-black
Wait another 10 seconds and place another drop of the 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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Your notes
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Investigating the effect of pH on enzyme activity Your notes
Adjustments to the method
The above method can be adapted to control temperature by using a water bath at 35°C
All solutions that need to be used (starch, amylase, pH buffers) should be placed in a water bath and
allowed to reach the temperature (using a thermometer to check) before being used
A colorimeter can be used to measure the progress of the reaction more accurately; with a solution
containing starch being darker and glucose light (as a result of the colour-change of iodine) – this will
affect the absorbance or transmission of light in a colorimeter
Examiner Tips and Tricks
Describing and explaining experimental results for enzyme experiments is a common type of exam
question so make sure you understand what is happening and, for a 7, 8 or 9, can relate this to
changes in the active site of the enzyme when it has denatured.
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Enzymes & Digestion
Your notes
Chemical Digestion
The purpose of digestion is to break down large, insoluble molecules into smaller, soluble molecules
that can be absorbed into the bloodstream
Large insoluble molecules, such as starch and proteins, are made from chains of smaller molecules
which are held together by chemical bonds. These bonds need to be broken
Enzymes are biological catalysts – they speed up chemical reactions without themselves being used
up or changed in the reaction
There are three main types of digestive enzymes – carbohydrases, proteases and lipases
Carbohydrases
Carbohydrases break down carbohydrates to simple sugars. Amylase is a carbohydrase which breaks
down starch into maltose, which is then broken down into glucose by the enzyme maltase
Amylase is made in the salivary glands, the pancreas and the small intestine
Diagram showing the digestion of starch
Proteases
Proteases are a group of enzymes that break down proteins into amino acids in the stomach and small
intestine
Protein digestion takes place in the stomach and small intestine, with proteases made in the stomach
(pepsin), pancreas and small intestine
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Your notes
Diagram showing the digestion of proteins
Lipases
Lipases break down lipids (fats) to glycerol and fatty acids.
Lipase enzymes are produced in the pancreas and secreted into the duodenum
Diagram showing the digestion of lipids
Examiner Tips and Tricks
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The pancreas is an accessory organ in the digestive system. Food does not pass directly through it,
but it has a key role in producing digestive enzymes as well as the hormones that regulate blood
sugar (insulin and glucagon). Your notes
The Role of Bile
Cells in the liver produce bile which is then stored in the gallbladder
Bile production and secretion
Bile has two main roles:
It is alkaline to neutralise hydrochloric acid from the stomach. The enzymes in the small intestine
have a higher (more alkaline) optimum pH than those in the stomach
It breaks down large drops of fat into smaller ones, increasing surface area. This is known as
emulsification.
The alkaline conditions and larger surface area allows lipase to chemically break down fat (lipids) into
glycerol and fatty acids faster (the rate of fat breakdown by lipase is increased)
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Examiner Tips and Tricks
Your notes
Emulsification is the equivalent of tearing a large piece of paper into smaller pieces of paper.
Products of Digestion
The products of digestion are used to build new carbohydrates, lipids and proteins required by all cells
to function properly and grow
Some glucose released from carbohydrate breakdown is used in respiration to release energy to fuel
all the activities of the cell
Amino acids are used to build proteins like enzymes and antibodies
The products of lipid digestion can be used to build new cell membranes and hormones
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Required Practical: Food Tests
Your notes
Food Tests
Aim: To use qualitative reagents to test for a range of carbohydrates, lipids and proteins. To include:
Benedict’s test for sugars, Iodine test for starch, the emulsion test for lipids and the Biuret reagent for
protein
You will:
Use qualitative reagents to test for the presence of key biological molecules in a range of foods
Safely use appropriate heating devices and techniques including the use of a Bunsen burden and a
water bath
A qualitative food test indicates if a substance is present or absent in a sample (although it doesn’t tell
you how much is present)
Observations are essential in this practical; you are looking for colour changes in particular which can
indicate if a substance is present or absent:
Food test colour changes table
Use this image
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Preparing a sample
Before you can carry out any of the food tests described below, you may need to prepare a food Your notes
sample first (especially for solid foods to be tested)
To do this:
Break up the food using a pestle and mortar
Transfer to a test tube and add distilled water
Mix the food with the water by stirring with a glass rod
Filter the mixture using a funnel and filter paper, collecting the solution
Proceed with the food tests
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Your notes
Use this image
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Your notes
Use this image
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Your notes
Use this image
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Your notes
Use this image
It is important that you carry out the tests methodically, recording your observations carefully
Important hazards
Whilst carrying out this practical you should try to identify the main hazards and be thinking of ways to
reduce harm:
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Biuret solution contains copper (II) sulfate which is dangerous particularly if it gets in the eyes, so
always wear goggles
Your notes
Iodine is also an irritant to eyes (wear goggles)
Sodium hydroxide in biuret solution is corrosive, if any chemicals get onto your skin wash hands
immediately
Ethanol is highly flammable; keep it away from the Bunsen burner used in the Benedict’s test (you
should turn the Bunsen off completely)
And of course, the Bunsen itself is a hazard!
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Use this image
Be prepared to explain what molecules are or are not present in a food sample – make sure you know Your notes
the positive and negative results for each test
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