Chapter 5: Enzymes
Outline
• 5.1 Biological catalysts
  – Naming Enzymes
  – The lock and key mechanism
  – The active site
• 5.2 Properties of enzymes
  – Temperature and enzyme activity
  – pH and enzyme activity
          Biological Catalysts
• Chemical reactions take place all the time
  within living organisms.
• Do you remember what these chemical
  reactions are called?
           Biological Catalysts
• “Metabolic reactions”
  – These reactions take so much time to happen
  – If they were allowed to occur without some help,
    then an organisms body will not be able to sustain
    life!
                Biological Catalysts
• In order to speed up any reaction, substances known as
  catalysts are used:
   – “they are substances that increase the rate of a chemical reaction and
     are not changed by the reaction”
• Our bodies have biological catalysts. These are called
  enzymes:
   – “they are proteins that function as biological catalysts”
       • Protein  1 mark
       • Biological  1 mark                            Differentiate between
       • Catalyze/speed up reactions  1 mark           “catalyst” and “enzyme”.
                                                        An enzyme is a type of
                                                        biological catalyst.
                   Biological Catalysts
Enzymes function by
decreasing the activation
energy of a reaction.
This is the amount of
energy needed for the
reaction to occur.
This means that with an
enzyme reactions can take
place at lower
temperatures.
          Biological Catalysts
• Example: the digestion of food requires many
  enzymes
            Biological Catalysts
• Example: amylase in seeds:
  – Water is soaked up by the seeds
  – This activates the amylase present
  – Amylase breaks downs starch stored in the seeds
    and converts it to maltose which is then used for:
     • Energy
     • To provide glucose for building cellulose cell walls
          Biological Catalysts
• Example: the enzyme catalase
  – Many animal and plant cells produce a dangerous
    substance known as hydrogen peroxide
  – Cells must get rid of this substance quickly!
  – Catalase converts it to water and oxygen:
          Biological Catalysts
• Did you notice that in all the previous
  reactions, the enzyme works to break down
  substances?
• Can enzymes help build large molecules from
  smaller ones?
                   Outline
• 5.1 Biological catalysts
  – Naming Enzymes
  – The lock and key mechanism
  – The active site
• 5.2 Properties of enzymes
  – Temperature and enzyme activity
  – pH and enzyme activity
           Naming Enzymes
• Enzymes are named according to the reaction
  that they catalyse.
• Example: enzymes that break down
  – CHOs  carbohydrases                  Old naming
  – proteins  proteases
  – lipids  lipases
  – maltose  maltase
  – sucrose  sucrase
                   Outline
• 5.1 Biological catalysts
  – Naming Enzymes
  – The lock and key mechanism
  – The active site
• 5.2 Properties of enzymes
  – Temperature and enzyme activity
  – pH and enzyme activity
    The Lock and Key Mechanism
• The substance which the enzyme works on can fit into the
  enzyme perfectly.
• Their shapes are described as “complementary” to one another.
   The Lock and Key Mechanism
• In the lock and key mechanism there is:
  – An enzyme: the biological catalyst
  – The substrate: the substance which the enzyme
    works on
  – The product: the end result of the reaction
  The Lock and Key Mechanism
• Example:
  – The enzyme: amylase
  – The substrate: starch
  – The product: maltose
                   Outline
• 5.1 Biological catalysts
  – Naming Enzymes
  – The lock and key mechanism
  – The active site
• 5.2 Properties of enzymes
  – Temperature and enzyme activity
  – pH and enzyme activity
                The Active Site
• Enzymes have dents (like a small pocket) called the
  active site.
• The shape of the active site is complementary to the
  shape of part of the substrate.
• The substrate will fit into the enzyme and form an
  enzyme-substrate complex.
• Every active site/enzyme is specific to only one
  substrate.
                      Paper 4 Question:
                      Why is the shape of the enzyme important?
You must be able to identify and label the following:
Enzyme – active site – substrate – enzyme-substrate complex - products
              The Active Site
• What is so special about the active site?
• The shape of the active site can only allow a
  specific shape to fit into it.
• Each enzyme has an active site.
• What can you conclude from this information?
             The Active Site
• Each enzyme can only act on a particular kind
  of substrate.
• “Enzymes are very specific”.
                   Outline
• 5.1 Biological catalysts
  – Naming Enzymes
  – The lock and key mechanism
  – The active site
• 5.2 Properties of enzymes
  – Temperature and enzyme activity
  – pH and enzyme activity
        Properties of Enzymes
1. All enzymes are proteins.
   Yes, enzymes can digest proteins even though
   they are proteins themselves!
2. Enzymes are made inactive by high
   temperatures.
   Protein molecules are damaged by heat.
            Properties of Enzymes
 3. Enzymes work best at particular temperatures
   E.g. enzymes in human bodies work best at
   37˚C.
                                     IMPORTANT
“minimum”                            Notice that the rate of
“optimum”                            reaction steeply
“maximum”                            decreases, not
                                     gradually!
                                     (Frequent P2 question)
         Properties of Enzymes
4. Enzymes work best at particular pH
  E.g. the enzymes in our stomachs work best at
  the very low pH found in that organ
Most enzymes have an
optimum pH of around
7 (neutral)
        Properties of Enzymes
5. Enzymes are catalysts  they are not changed
  in the chemical reactions which they control!
  This means they can be used over and over
  again  only a small amount of enzyme can
  change a lot of substrate into product.
        Properties of Enzymes
6. Enzymes are specific
  Each kind of enzyme will only catalyse one
  kind of chemical reaction
                   Outline
• 5.1 Biological catalysts
  – Naming Enzymes
  – The lock and key mechanism
  – The active site
• 5.2 Properties of enzymes
  – Temperature and enzyme activity
  – pH and enzyme activity
 Temperature and Enzyme Activity
• When the temperature is higher:
  1. Molecules have more kinetic energy.
  2. Molecules move faster.
  3. Collisions between active site and substrate are more frequent.
  4. There is a larger number of successful collisions:
       • They bump into each other more often
       • They bump into each other with more energy
• The reaction is more likely to take place  the
  rate of the reaction increases.
• “The frequency of effective collisions increases”.
A:                                     B
Molecules are gaining kinetic
energy so chances of successful
collisions increases between the
enzyme and substrate.
                                   A
B:                                         C
Optimum temperature at which
the enzyme works the
fastest/most efficient.
C:
Enzyme is denatured; active site
no longer fits the substrate.
 Temperature and Enzyme Activity
• However, at a certain point, the very high temperature
  will start to damage the protein/enzyme and it starts to
  lose its shape.
• In a human body, this begins at 40˚C or more.
• So increasing the temperature can either increase or
  decrease the rate of a reaction!
• What happens to the shape of the active site if it
  changes?
 Temperature and Enzyme Activity
• The active site no longer fits perfectly with its
  substrate, and the enzyme can no longer
  catalyse the reaction.
• The enzyme is said to be denatured.
• Remember: we cannot say that enzymes are
  killed by high temperature! Enzymes are
  chemicals NOT living organisms!
 Temperature and Enzyme Activity
• Every enzyme has a temperature that it can
  work the fastest at  optimum temperature
                 Question
• What is the optimum temperature for the
  enzyme in the figure below?
                   Outline
• 5.1 Biological catalysts
  – Naming Enzymes
  – The lock and key mechanism
  – The active site
• 5.2 Properties of enzymes
  – Temperature and enzyme activity
  – pH and enzyme activity
         pH and Enzyme Activity
• The pH of a solution affects the shape of an enzyme:
   – Enzymes are proteins
   – Proteins curl and fold into 3D shapes which affects their
     function
• Most enzymes are in their correct shape at neutral pH
  (~7).
• Each enzyme has an optimum pH at which the shape of
  the active site is complementary to that of the substrate.
       pH and Enzyme Activity
• If the pH becomes too acidic/alkaline, the
  enzymes denature. What happens if the enzyme
  denatures?
  – Active site shape changes.
• Keep in mind:
  – Some enzymes have optimum pH that are
    acidic/alkaline
  – Can you think of examples?
pH and Enzyme Activity
     Factors Affecting Enzyme Activity/Reaction Rate
1.   Temperature.
2.   pH.
3.   Concentration/volume of enzyme added.
4.   Concentration/volume of substrate added.
5.   Surface area of substrate.
6.   Amount of product.
7.   Type of enzyme.
8.   Type of substrate.
P2/March/2019
P1/O/N/2015
                              Question
Describe how enzymes function.
1. They are proteins which are unchanged by the reaction.
2. They catalyze reactions by decreasing the energy needed.
3. They are specific for a certain substrate (lock and key mention).
4. The shape of the active site is complementary to the shape of the
    substrate.
5. This allows them to bind together and form an enzyme-substrate
    complex.
6. After the substrate is converted into a product, the product is released
    from the active site and the enzyme is able to catalyze another reaction.
7. Each enzyme has an optimum pH and temperature at which it functions
    the quickest and most efficiently:
   •     Incorrect pH = active site shape changes
   •     Temp. too high = denatured enzyme
   •     Temp. too low = low kinetic energy  slow reaction
P4/O/N/2016