Investigating the Best Temperatures betweem Calf Trypsin and Fugal Trypsin

Investigating the Best Temperatures betweem Calf Trypsin and Fugal Trypsin

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Investigating the Best Temperatures betweem Calf Trypsin and Fugal Trypsin

PROBLEM BEING INVESTIGATED

BACKGROUND

Trypsin is an enzyme so to be able to conduct a suitable plan, this
idea will help me to predict the best temperature that can be achieved
on its activities in different conditions. “Collins Advanced Science
Biology defines an enzyme as biological catalysts, speeding up
reactions that would otherwise happen too slowly to be any use to the
organism, that is it has catalytic properties, in other words they
alter the rate of reaction without themselves undergoing a permanent
change. Most chemical reactions require an initial input of energy
called activation energy, to enable them to occur. Enzymes reduce the
need for activation energy and so allow reactions to take place more
readily than would otherwise be. An active enzyme may speed up a
particular reaction, but living organisms do not need all reactions to
be going at the maximum rate all of the time. It would be perfect to
say after considering this fact that, enzymes do actually control
rather than speeding up, because they interact with other molecules to
produce an ordered, stable reaction system in which the products of
any reaction are made when they are needed in the amount needed.
Enzymes are globular proteins. They have complex tertiary structure in
which polypeptides are folded around each other to form a roughly
globular shape. This ship is very important once altered, the enzyme
cannot bind to its substrate and so cannot function, this shape is
maintained by hydrogen bonds and ionic forces and their function can
be affected by changes in temperature and pH, these are not the only
factors that can affect enzymes are competitive inhibitors they
compete with the substrate for the active site, The greater the
concentration of the substrate the more likely it is to occupy the
active sites and the less the effect of the inhibitor. and
non-competitive inhibitors which attach themselves to the enzyme other
than the active site, As the substrate and inhibitor are not competing

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for the same site, an increase in substrate concentration does not
diminish the effect of the inhibitor

TEMPERATURE

As temperature increases, the molecules move faster, due to increased
energy. Therefore, the enzyme and substrate molecules will meet more
often and the rate at which the product is formed will increase this
is according to the Kinetic Theory. However, as the temperature
continues to raise the hydrogen and ionic bonds, which hold the enzyme
in shape, break and the active site will no longer accommodate the
substrate. The enzyme will denature and when this occurs it cannot be
reversed.

PH

Changes in pH may not only affect the shape of an enzyme but it may
also change the shape or charge properties of the substrate so that
either the substrate connot bind to the active site or it cannot
undergo catalysis. In general enzymes have a pH optimum. However the
optimum is not the same for each enzyme.

THE INDUCED FIT HYPOTHESIS

This is a simply hypothesis explaining the way that an enzyme breaks
up its substrate. It is recently known that the active site in many
enzymes is not exactly the same shape as the substrate, but moulds
itself around the substrate as the enzyme-substrate complex is formed.
The hypothesis explains my comment that enzyme binds to a substrate
momentarily, allowing a reaction to happen, but do not themselves
undergo any chemical change.

The image below explains the induced fit hypothesis better.

[IMAGE]

SIMPLE PROCEDURE AND SCIENTIFIC COMMUNICATION

Trypsin is an enzyme secreted by the pancreas, it digest proteins
breaking them down into shorter chain of amino acids. I am going to
find the optimum temperatures between normal trypsin which is found in
the pancreas of most warm blooded animals and a genetically engineered
trypsin. I will do so by mixing and heating these different types of
trypsin and it’s substrate a suspension of powdered milk in various
water baths at various temperatures. This will help me determine the
various optimum temperatures of these different trypsins. I will
repeat the procedure several times at the different water bath and
then conclude my experiment.

I also know that enzymes work best at an optimum temperature. For warm
blooded enzymes such as trypsin it is close to the normal body
temperature (37°C). Below this temperature, the molecule of enzyme and
substrate have less kinetic energy and are moving less slowly and the
chances of colliding is high. At high temperatures (50°C) enzymes are
destroyed or denatured by heat. I will therefore carry out the my
experiment at range of temperatures from room temperature (20°C) to a
temperature that should cause denaturing(80°C)


PRECAUTIONS AND KEY FACTORS NEEDED TO OBTAIN VALID DATA

I am going to use same concentration of trypsin in all my experiment,
If I increase the concentration it will mean that the chance of the
trypsin colliding with the substrate would be higher which would
affect the rate of reaction and my results as well, I would also use
the same concentration of my substrate throughout the experiment for
the same reason. The volume of trypsin and the milk suspension should
also be constant. If either varies this would upset the final
concentration of the enzyme and substrate which would make it
difficult to determine the optimum temperatures

The end point of the optimum temperatures is difficult to judge with
accuracy, so I will attempt to measure the volume of trypsin solution
using a graduated pipette, which I believe is accurate to 0.1cm3 which
is a 2% margin of error. I will repeat the experiment 3 times at each
temperature to check whether my findings are reliable

EQUIPMENTS

* Test tube rack

* Test tubes.

* Milk solution

* Trypsin 1(cow) and trypsin 2(fungal)

* Water bath

* Pipette

* Thermometer

SAFETY

Some people are allergic to enzymes so I will mop up any spillages and
will wash my hands after. I will take care when using the water bath.
I will also ware safety goggles and lab coat throughout.

METHOD

1. Collect all equipment, and set out the water bath at temperatures
ranging from 20°C, 40°C, 60°C, and 80°C.Test with the thermometer to
check if the temperatures are set to the required ranges.

2. Measure 5ml of milk solution with graduated pipette into 8
different test tubes. Add 4 drops of each type of trypsin ( 4 drops of
calf trypsin and 4 drops of fungal trypsin) and mix with test tube
containing 5ml of milk solution.

3. Shack well and place each type of trypsin mixed with milk into the
various water bath with different temperature ranges.( So in each
water bath 1 calf trypsin and 1 fungal trypsin would be placed in)

4. Check every 5mins to check, and record the temperatures each time
you check. When the temperatures start to drop down remove the test
tubs.

5. Repeat at least 3 times and record you final results, compare the
temperatures ranges for each trypsin and milk solution in various
water baths .

6. plot a graph of temperature against time and comment on your graph.

PREDICTED GRAPH OF RESULTS

when the temperature start going down because it has denatured the
graph will look like this

Effect of temperature

REFERENCE:

1. Collins Advanced Science Biology by Mike Boyle and Kathryn Senior

2. Collins Advanced Modular Sciences Biology AS by Mike Bailey and
Keith Hirst

3. Longman (www.longman.com)

4. Class notes Enzymes

5. Sci-Journal (www.sci-journal.com )
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