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Properties Of Enzymes Essay About Myself

Exploring the Properties and Functions of Enzymes

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Exploring the Properties and Functions of Enzymes
Introduction

In this experiment I will attempt to investigate how the change in
temperature effects the catalyse reaction and what the optimum
temperature is.

Key factors

Key factor

(variable)

Reason for controlling

How it is going to be controlled

Temperature of hydrogen peroxide H202

I am going to control this variable because if the temperature of the
hydrogen peroxide was higher or lower then the right temperature the
test wouldn’t be fair and my results could be affected because a
different temperature would result in a different froth height.

I am going to control the temperature by placing the hydrogen peroxide
into a water bath with the exact temperature for at least 3 minutes.

Temperature of yeast

I am going to control this variable because if the temperature of the
yeast was higher or lower than the right temperature the test wouldn’t
be fair and my results could be affected because a different
temperature would result in a different froth height.

I am going to control the temperature by placing the hydrogen peroxide
into a water bath with the exact temperature for at least 3 minutes.

Water temperature

I am going to control this variable because if I didn’t the hydrogen
peroxide and the yeast will be at different temperatures because I
will use the water to heat the hydrogen peroxide and yeast.

I am going to control this variable by having the water placed in a
water bath which will keep the water at a constant temperature.

Volume of hydrogen peroxide

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Properties         Enzymes         Functions         Variable         Key Factors         Placing         Hydrogen Peroxide         Results         Temperatures        





I am going to control this variable because if I didn’t my results
would differ to the results I would have if my results where accurate
and this wouldn’t be a fair test.

I am going to control this variable by using a pipette to pour the
hydrogen peroxide into the small measuring cylinder (10cm3).

Volume of yeast

I am going to control this variable because if I didn’t my results
would differ to the results I would have if my results where accurate
and this wouldn’t be a fair test.

I am going to control this variable by using a pipette to pour the
hydrogen peroxide into the small and thin measuring cylinder (10cm3).

Temperature of yeast

I'm going to control this variable because if I didn’t I would get a
different froth height to if the temperature of the yeast was right,
because yeast is very receptive to change.

I am going to control this variable by making sure the temperature is
exact. I can do this by using a long thin thermometer to measure the
temperature of the yeast.

Temperature of hydrogen peroxide.

I'm going to control this variable because if I didn’t I would get a
different froth height to if the temperature of the yeast was right.

I am going to control this variable by making sure the temperature is
exact. I can do this by using a long thin thermometer to measure the
temperature of the hydrogen peroxide.

Concentration of hydrogen peroxide.

If the concentration of the hydrogen peroxide was lower than the
amount I had used in previous tests I would have anomalous results and
this wouldn’t be a fair test.

I am going to control this variable by making sure that there has been
no other liquid in the measuring cylinder and if there has I will wash
it thoroughly and after I wash it I will dry it thoroughly by drying
the inside of the measuring cylinder with a paper towel.

Concentration of yeast

If the concentration of the yeast was lower than the amount I had used
in previous tests I would have anomalous results and this wouldn’t be
a fair test.

I am going to control this variable by making sure that there has been
no other liquid in the measuring cylinder and if there has I will wash
it thoroughly and after I wash it I will dry it thoroughly by it by
drying the inside with a paper towel.


Scientific knowledge

Enzymes:

Because enzymes are proteins they can be destroyed at high
temperatures, this is called denaturing. Enzymes are used to catalyse
(speed up) chemical reactions. There are many types of enzymes and
they are all used to break down certain food molecules, this is
described in the lock and key theory and the induced fit theory.

Enzyme theory:

Lock and key theory.

Enzymes are biological catalysts. The lock and key theory was
suggested in 1894 by Emil Fischer and properly described as follows
"The specificity of an enzyme (the lock) for its substrate (the key)
arises from their geometrically complementary shapes".

[IMAGE][IMAGE] The lock and key theory is simply a way of describing
how specific an enzyme is for its substrate. Just like a lock requires
a specifically shaped key for it to work so does an enzyme. Each
enzyme is a protein which is a polypeptide chain folded into a complex
3 dimensional structure. Part of that structure contains the active
site which is where the enzyme can bind to the substrate on which it
will perform some chemical reaction. Because each enzyme performs a
specific task on a specific substrate the active centre of the enzyme
can be considered to be the "lock" which requires the specific "key"
or substrate to perform the function. Smaller keys, larger keys, or
incorrectly positioned teeth on keys (incorrectly shaped or sized
substrate molecules) do not fit into the lock (enzyme). Only the
correctly shaped key (substrate) opens a particular lock. If we
imagine the enzyme as the lock and the substrate the key - the key is
inserted in the lock and if this is his right enzyme for the substrate
the lock is turned, and the door is opened and the reaction proceeds.

The active site is the specific region of the enzyme which combines
with the substrate. The products are released from the enzyme surface
to regenerate the enzyme for another reaction cycle.

The active site has a unique geometric shape that is complementary to
the geometric shape of a substrate molecule. This means that enzymes
specifically react with only one or a very few similar compounds.

Induced Fit Theory:

This theory uses instead of the analogy the key in the lock but
instead the glove in the hand this theory also explains that a protein
is flexible. Enzymes act as biological catalysts. They are globular
proteins that have a specific shape within which there is a functional
portion known as the active site. Enzymes lower the activation energy
of a reaction, allowing it to proceed at a lower temperature than it
would normally. In an enzyme controlled reaction, the general term for
the substance on which the enzyme acts is substrate and the substances
formed at the end of there action are known as the products. The
enzyme molecule and the substance it acts on fit together very
precisely, giving rise to the name lock and key theory of enzyme
action. In practice, the enzyme is thought to change shape slightly
and so mould itself to the shape of the substance it acts on. This is
called the induced fit theory of enzyme action

Structure and Function of an Enzyme.

Enzymes are large proteins that speed up chemical reactions. In their
spherical structure, one or more polypeptide chains twist and fold,
bringing together a small number of amino acids to form the active
site, or the location on the enzyme where the substrate binds and the
reaction takes place.

Enzyme and substrate fail to bind if their shapes do not match
exactly. This ensures that the enzyme does not participate in the
wrong reaction. The enzyme itself is unaffected by the reaction. When
the products have been released, the enzyme is ready to bind with a
new substrate.

Properties of Enzymes
As the Swedish chemist Jöns Jakob Berzelius suggested in 1823, enzymes
are typical catalysts: they are capable of increasing the rate of
reaction without being consumed in the process.
Some enzymes, such as pepsin and trypsin, which bring about the
digestion of meat, control many different reactions, whereas others,
such as urease, are extremely specific and may accelerate only one
reaction. Still others release energy to make the heart beat and the
lungs expand and contract. Many facilitate the conversion of sugar and
foods into the various substances the body requires for
tissue-building, the replacement of blood cells, and the release of
chemical energy to move muscles.
Pepsin, trypsin, and some other enzymes have in addition, the peculiar
property known as autocatalysis, which permits them to cause their own
formation. As a consequence, these enzymes may be reproduced in a test
tube.
As a class, enzymes are extraordinarily efficient. Tiny quantities of
an enzyme can accomplish at low temperatures what would require
violent reagents and high temperatures by ordinary chemical means.
About 30g of pure crystalline pepsin, for example, would be capable of
digesting nearly 2 metric tons of egg white in a few hours.
Each enzyme is selectively specific for the substance in which it
causes a reaction and is most effective at a temperature peculiar to
it. Although an increase in temperature may accelerate a reaction,
enzymes are unstable when heated. Many enzymes require the presence of
another ion or a molecule called a cofactor, in order to function.
As a rule, enzymes do not attack living cells. As soon as a cell dies,
however, enzymes that break down protein rapidly digest it. The
resistance of the living cell is due to the enzyme's inability to pass
through the membrane of the cell as long as the cell lives. When the
cell dies, its membrane becomes permeable, and the enzyme can then
enter the cell and destroy the protein within it. Some cells also
contain enzyme inhibitors, known as anti-enzymes, which prevent the
action of an enzyme upon a substrate.

Enzyme reactions

An enzyme-catalysed reaction, the rate is usually expressed in the
amount of product produced per minute. The energy barrier between
reactions and products governs reaction rate. In general, energy must
be added to the reactants to overcome the energy barrier. This added
energy is termed "activation energy", and is recovered as the
reactants pass over the barrier and descend to the energy level of the
products. Enzymes can accelerate the rate of a reaction. Catalysts
accelerate the rates of reactions by lowering the activation energy
barrier between reactants and products. All chemical reactions speed
up as the temperature is raised. As the temperature increases, more of
the reacting molecules have enough kinetic energy to undergo the
reaction.

Enzyme classification

Enzymes are classified into several broad categories, such as
hydrolytic, oxidising, and reducing, depending on the type of reaction
they control. Hydrolytic enzymes accelerate reactions in which a
substance is broken down into simpler compounds through reaction with
water molecules. Oxidising enzymes, known as oxidises, accelerate
oxidation reactions; reducing enzymes speed up reduction reactions, in
which oxygen is removed. Many other enzymes catalyse other types of
reactions.

Individual enzymes are named by adding ASE to the name of the
substrate with which they react. The enzyme that controls urea
decomposition is called urease; those that control protein hydrolyses
are known as proteinases. Some enzymes, such as the proteinases,
trypsin and pepsin, retain the names used before this way of naming
was adopted. Enzymes are large proteins that speed up chemical
reactions. In their round structure, one or more polypeptide chains
twist and fold, bringing together a small number of amino acids to
form the active site, or the location on the enzyme where the
substrate binds and the reaction takes place. Enzyme and substrate
fail to bind if their shapes do not match exactly. This ensures that
the enzyme does not participate in the wrong reaction. The enzyme
itself is unaffected by the reaction. When the products have been
released, the enzyme is ready to bind with a new substrate.

Primary structure

AA1-AA2-AA3-AA4-AA5-AA6-AA7-AA8-AA9-AA10-AA11-AA12 etc

This structure twists and turns because of the R groups in the amino
acids. Every R group is different

If you zoom in on one of the amino acids and look at the structure you
will see:

H H R

NH3 - C – C – C - CooH

H H R

Because of the attraction between the r groups weak hydrogen bonds are
formed, these bonds are what hold the structure together and if the
enzyme its alpha helix or beta sheet shapes.

Measuring enzyme reactions

The two ways in which an enzyme reaction can be measured they are rate
of reaction and time course. Time course reactions are usually plotted
by measuring either the formation of products or the disappearance of
the substrate. If the temperature is increased the rate of an enzyme
reaction will rise/increase up to a point at which its molecular
structure is disrupted. At this point the enzyme is said to be
denatured. With a fixed amount of enzyme the addition of more
substrate will cause the rate of reaction to increase until all the
enzyme molecules are being used. At this point the rate of reaction
levels off because the enzyme is limiting the reaction. An increase in
the amount of enzyme will cause a proportional increase in the rate of
reaction provided that there is excess substrate. Enzymes work in a
narrow range of pH outside of which the hydrogen bonds between the NH
and CO groups are broken. A solution that prevents changes in pH is
called a buffer solution.


Scientific knowledge used to plan

Structure in enzymes

The different levels of protein structure are known as primary,
secondary, tertiary, and quaternary structure. There are 20 common
amino acids are classified by their functional group, or their "R"
group. When the weak hydrogen bonds that help the enzyme take its
shape break because of the heat the enzymes have become denatured.

Illustration of a polypeptide strand as described

Primary structure

The primary structure is the sequence of amino acids that make up a
polypeptide chain. 20 different amino acids are found in proteins. The
exact order of the amino acids in a specific protein is the primary
sequence for that protein.

AA1-AA2-AA3-AA4-AA5-AA6-AA7-AA8-AA9-AA10-AA11-AA12 etc

This structure twists and turns because of the R groups in the amino
acids. Every R group is different

If you zoom in on one of the amino acids and look at the structure you
will see:

H H R

NH3 - C – C – C - CooH

H H R

Because of the attraction between the r groups weak hydrogen bonds are
formed, these bonds are what hold the structure together and if the
enzyme its alpha helix or beta sheet shapes.

Secondary structure

The amino acids form regular repeating patterns folding along the
protein back bone.

There are two common structures, the alpha helix and the beta pleated
sheet.

Illustration of a alph helix as described[IMAGE]Alpha Helix
In an alpha helix, the polypeptide backbone coils around an imaginary
helix axis in clockwise direction to get its shape. The most common
structure is the alpha helix. This structure gives stability to the
unit because there is a weak hydrogen bond between the various peptide
bonds. Notice that the left handed helical backbone is made up of the
peptide chain. The R groups point out from the structure at a 90
degree angle.

[IMAGE]Beta sheet
In the beta sheet secondary structure, the polypeptide backbone is
nearly completely strait. Beta sheets are a combination of two or more
beta strands. The strands are held together and stabilized by hydrogen
bonding. There are two types of sheets: either parallel or anti
parallel depending on the orientation of the peptide chain.

Illustration of a beta sheet as described

Illustration of a tertiary structure of proteins as describedTertiary
structure

Tertiary structure refers to the overall folding of the entire
polypeptide chain into a specific 3D shape. The tertiary structure of
enzymes is often a compact, globular shape.

Quaternary structure

Many proteins are formed from more than one polypeptide chain. The
quaternary structure describes the way in which the different subunits
are packed together to form the overall structure of the protein.

How will the enzyme structure help me plan?

Knowing the enzyme structure will help me plan my experiment because
it will help me understand how an enzyme becomes denatured and that
will help me to plan my experiment because I will then know which
temperatures will be the best to use.

Plan of procedure

To do this experiment I will:

· Set each water bath to the right temperature because if I didn’t my
results would be inaccurate because yeast is very receptive to change
so I would be able to see that change in my results. I will need to
use a thermometer to measure the temperature to make sure the
temperature is right.

· Measure out 2 cm3 of yeast and hydrogen peroxide, using a pipette to
get the exact measurement and I will also use a small thin measuring
cylinder. I will also need to make sure each of the measuring
cylinders is clean and dry. If they weren’t clean and I added hydrogen
peroxide to a dirty measuring cylinder which had yeast in the reaction
would already start to happen this wouldn’t make it a fair test and it
would alter my results table. If the measuring cylinder had water or
any other liquid in it would lower the concentration of the hydrogen
peroxide because of that my results table would be inaccurate .If I
didn’t have the exact amount of yeast and hydrogen peroxide my results
would be inaccurate because the froth height would be higher or lower
because there is more of the yeast and hydrogen peroxide.

· Place a thermometer into the hydrogen peroxide and the yeast, so I
know when the yeast or hydrogen peroxide has reached the exact
temperature. I need to know the exact temperature because the yeast is
very receptive to change so if the temperature was higher or lower I
may get anomalous results.

· Place the yeast and hydrogen peroxide into the water bath making
sure that no water enters the measuring cylinders because if it did
the concentration of the yeast and hydrogen peroxide would be lowered
and if that happened would have anomalous results.

· When the yeast has reached the needed temperature (I will know this
by reading the thermometer) place either one of the liquids into
another measuring cylinder and then pour the other liquid into that
measuring cylinder and measure the max froth height by using the
markers on the measuring cylinder. If it exceeds the maximum height
place a ruler against the highest marking on the measuring cylinder,
this may not be accurate but it is the only way of measuring it as a
bigger beaker doesn’t have as many markings on it. I will be measuring
the maximum froth height reached because I think this is the best way
of measuring the maximum amount of oxygen produced.

· After measuring the maximum froth height I will note the results
then I will repeat the temperatures I have just done twice to make
sure that my results were not anomalous.

· I will repeat these steps for all of the temperatures.

· I will then average out the results.


Range of observations

I will repeat all of these temperatures twice to make sure that none
of my results are anomalous.

For this experiment I will be doing the temperatures:

· 0 oc

· 10 oc

· 20 oc

· 30 oc

· 40 oc

· 50 oc

· 60oc

After repeating the results twice I will look at my results and if any
are anomalous then I will repeat the experiment. After getting rid of
any anomalous results I will average out the results. I will also use
other group’s results to check my results to see if any of the results
are anomalous.


Precision

I have decided to use the following equipment:

* measuring cylinders (10cm3)

* water baths

* ice baths

* pipettes

* Paper towels

* Ruler

* Thermometer

I used a small measuring cylinder to measure out the amounts of
hydrogen peroxide and the yeast because in a smaller measuring
cylinder I can achieve more accurate results because there are more
detailed markings so I will know if I have done 2cm3 or 1.9cm3.

I am going to use water baths to keep the water at a certain
temperature. I think that using a water bath to keep the water heated
is the best apparatus to use for certain temperatures because a water
bath can keep the water at a specific temperature for a long time
whereas a beaker of water heated by a Bunsen burner can begin to lose
heat and when you try to reheat the water you could go above the
required temperature. You could also go above the required temperature

I will be using an ice bath to keep the temperature at 0oc. I think
that an ice bath would be the best apparatus to use for this
temperature because I couldn’t use a water bath because that would
keep the temperature above o and a Bunsen burner would keep the
temperature above 0 oc.

I will use a small pipette to add more of the liquid into the
measuring cylinder because then if I need to add 1 more drop of a
liquid into a measuring cylinder it would be a lot easier than pouring
it strait from the bottle and it works the other way round as well
because if I have added to much liquid to the measuring cylinder I can
take out small amounts of the liquid using the pipette.

I will be using paper towels to dry the measuring cylinders. I think
that using a paper towel is the best thing to use when drying a
measuring cylinder because a paper towel can be twisted and pushed
into the measuring cylinder to dry it out.

If the froth exceeds the maximum height on the measuring cylinder I
will use a ruler to measure how high the froth has gone. I think that
a cm ruler will be the best thing to use because 1cm on the ruler is
the same height as 1cm3 on the measuring cylinder.

I will be using a thermometer to measure the temperature of each of
the liquids; I will be using a long thin thermometer to get an
accurate reading. I think that using a thermometer will be the best
apparatus to because a thermometer can give accurate readings and when
a longer thinner thermometer is used it can give more accurate
readings because I can get decimal point answers.


Justified prediction

For this experiment I think that the froth height will be at its
highest at 40 oc because that it the temperature that is closest to
body temperature. I know that enzymes work best at body temperature
because the human body is very well designed to make sure that
everything works well and if the enzymes and other body functions
worked better at higher or lower temperatures then the body
temperature would change to have better conditions for the enzymes to
work so I think that the optimum temperature will be 40oc. I predict
that the enzyme will become denatured, and therefore will work at a
slower rate after 40 - 45°C. I think the reason for this prediction is
because every enzyme has a temperature range of optimum activity.
Outside that temperature range the enzyme is rendered inactive. This
occurs because as the temperature changes enough energy is supplied to
break some of the molecular bonds. When these forces are disturbed and
changed the active site becomes altered in its ability to accommodate
the substrate molecules it was intended to catalyse. Most enzymes in a
human body shut down beyond certain temperatures. This can happen if
body temperature gets too low (hypothermia), or too high
(hypothermia).

From my background knowledge it is evident that as temperature
increases, the rate of reaction also increases. However, the stability
of the protein also decreases due to thermal degradation. Holding the
enzyme at a high enough temperature for a long period of time may cook
the enzyme.

I think that the froth height will not be very high at the temperature
0 oc in-fact it will be the lowest out of all of the temperatures
because I know that enzymes work best at around 37-39oc because that
is body temperature and 0 oc it way below that temperature so I think
that the froth height for 0 oc will be around 6-10cm3.

I also think that when I do the next temperature in my experiment
which is 10 oc higher the froth height will be higher until it reaches
40 oc because the after that the enzymes begin to denature because of
the extreme temperatures the weak hydrogen bonds which the primary
structure of amino acids have formed begin to break.

I predict that that if it took 50 seconds for the froth to reach the
10cm3 mark then at 20 oc it would take 40 seconds for it to reach the
10cm3 mark and the time taken for it to reach the 10cm3 mark will take
a smaller amount of time, each time the temperature increased until it
reached 40oc because the heat speeds up the reaction. My prediction is
supported by Kinetic Theory in that if I apply twice as much heat
there will be twice as much particle vibration therefore the reaction
will happen twice as quickly. It is also backed by Collision Theory in
that if I apply twice as much heat there will be twice as many
collisions and therefore the rate of reaction will double. This will
only be so until the enzyme denatures after its optimum temperature

Since enzymes are catalysts for chemical reactions, enzyme reactions
also tend to go faster with increasing temperature. However, if the
temperature of an enzyme catalysed reaction is raised still further,
an optimum is reached: above this point the kinetic energy of the
enzyme and water molecules is so great that the structure of the
enzyme molecules starts to be disrupted. The positive effect of
speeding up the reaction is now more than offset by the negative
effect of denaturing more and more enzyme molecules. Many proteins are
denatured by temperatures around 40 - 50°C, but some are still active
at 70 - 80°C, and a few withstand being boiled. So, my first
prediction is that the enzyme will become denatured at around 40°C,
and secondly, that as the temperature increases the reaction rate will
increase by 50%, due to the molecules colliding together at a higher
speed (kinetic theory) due to their extra energy obtained by the
increase in temperature. My prediction is supported by Kinetic Theory
in that if I apply twice as much heat there will be twice as much
particle vibration therefore the reaction will happen twice as
quickly. It is also backed by Collision Theory in that if I apply
twice as much heat there will be twice as many collisions and
therefore the rate of reaction will double. This will only be so until
the enzyme denatures after its optimum temperature: 45°C.

On the next page there is a graph of what I think the actual graph of
the results is going to look.

From the graph you can see that the maximum froth height rises until
it reaches its optimum temperature (40 oc) then the graph starts to
fall.


Secondary source data

In this experiment I intend to use at least 1 other piece of data to
check my results against I am also going to use a set of results from
a computer program called focus education software. In total I am
using 3 sets of data including mine.



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1666 Words7 Pages

Introduction Enzymes are macromolecules that act as a catalyst, and it’s a chemical agent that accelerates the reaction without being consumed by the feedback or the results (Campbell and Reece, 2005). After the adjustment by the enzymes, the chemical movement through the pathways of metabolism will become awfully crowded because many chemical reactions are taking a long time (Campbell and Reece, 2005). There are two kinds of reactions in nature. The first one is Catabolic reaction and the second one is Anabolic reaction. Catabolic reactions are large molecules that are broken up into smaller molecules (Ahmed, 2013). Anabolic reactions are small molecules that join to make larger molecules, like polymerization (Ahmed, 2013). If you…show more content…

Introduction Enzymes are macromolecules that act as a catalyst, and it’s a chemical agent that accelerates the reaction without being consumed by the feedback or the results (Campbell and Reece, 2005). After the adjustment by the enzymes, the chemical movement through the pathways of metabolism will become awfully crowded because many chemical reactions are taking a long time (Campbell and Reece, 2005). There are two kinds of reactions in nature. The first one is Catabolic reaction and the second one is Anabolic reaction. Catabolic reactions are large molecules that are broken up into smaller molecules (Ahmed, 2013). Anabolic reactions are small molecules that join to make larger molecules, like polymerization (Ahmed, 2013). If you put all the reactions together, catabolic and anabolic is called Metabolism (Ahmed, 2013). Basically enzymes are protein molecules that can be composed of one or more multiple polypeptide (Ahmed, 2013). Enzymes can also have non-protein parts that are called cofactors and they are attached to them (Ahmed, 2013). “If the cofactors are organic nature they are called coenzymes” (Ahmed, 2013). For a catalytic of an enzyme to extend its speed of the reaction varies, depending of the factors such as temperature, pH, concentration of substrate, concentration of enzyme and so on (Ahmed, 2013). Enzyme has five properties: first one is Enzyme bind to substrate, second one is Enzyme are substrate specific, third one is substrate binds an enzyme

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