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Enzyme Discussion

Enzymes are proteins that catalyze chemical reactions and contain an active site that binds to substrates. Amylase is an enzyme that catalyzes the hydrolysis of starch into sugars. Testing potatoes with iodine solution indicated the presence of starch as it turned blue-black. Increasing the temperature from 15 to 50 degrees Celsius increased the reaction rate of amylase on starch as observed by less intense color change, due to higher molecular energies allowing for more collisions between enzyme and substrate.

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48 views2 pages

Enzyme Discussion

Enzymes are proteins that catalyze chemical reactions and contain an active site that binds to substrates. Amylase is an enzyme that catalyzes the hydrolysis of starch into sugars. Testing potatoes with iodine solution indicated the presence of starch as it turned blue-black. Increasing the temperature from 15 to 50 degrees Celsius increased the reaction rate of amylase on starch as observed by less intense color change, due to higher molecular energies allowing for more collisions between enzyme and substrate.

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Student1010
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Enzymes are large ,complex ,globular proteins that have several polypeptides in their

structure. The polypeptide chains of an enzyme are folded to form a pocket on the
enzyme surface called the active site. The active site of an enzyme has a precise three-
dimensional shape and the correct orientation and array of bonding types. The active
site holds the substrate on the enzyme and orients the substrate correctly so that the
reaction can occur. The enzyme is not permanently altered or used up during a
chemical reaction.

Amylase is an enzyme that catalyses the hydrolysis of starch into  simple sugars such


as maltose. Starch   is a polymeric carbohydrate consisting of a large number
of glucose units joined by glyosidic bonds. Polysaccharides consist of many
monosaccharides molecules joined together in a condensation reaction, also called
dehydration synthesis. . When iodine is added to starch in water , it adheres to the beta
amylose molecules because of their solubility. The starch pushes the iodine into a line
in the middle of the amylose coils and creates a transfer of charge between the iodine
and starch. This causes a change in the arrangement of electrons and energy level
spacings. The new spacings absorb visible light differently and create a deep blue
colour .If starch is not present the solution remains dark brown. Therefore when the
crushed potato in each test tube was tested for starch using iodine solution, the potato
turned blue –black indicating starch was present

Temperature alters the rate of enzyme-catalysed reactions. In the experiment , test tube
A in the 50 degrees Celsius water bath turned completely cream/off white with no traces
of the blue-black colour obtained from reacting it with iodine solution . This indicated
that all the starch has turned to maltose and therefore there is no starch left for the
iodine to react with. The increase in temperature increases the kinetic energy of the
enzyme and substrate molecules hence they have a greater chance of colliding with
each other, therefore the substrate molecules have enough energy to provide activation
energy for the chemical reaction. Therefore test tube A had the fastest rate of reaction
with the amylase enzyme.

In test tube B that was left to react at room temperature (27 degrees Celsius) it was
found that after 10 minutes the blue black colour caused by the iodine solution was still
fairly dispersed in the mixture, indicating that all the starch had not been broken down to
maltose. Thus the rate of reaction in test tube B was moderate .

In test tube C which was reacted at 15 degrees Celsius with amylase the blue black
colour was more intensely dispersed in the solution after the ten minutes inferring that a
large amount of starch was not hydrolysed into maltose. Therefore we can infer that the
reaction at 15 degrees Celsius was the slowest. This lower temperature caused a
gradual decrease in the speed of molecules reducing the frequency of enzyme-
substrate collisions and therefore decreasing enzyme activity. However this cause may
be very minimal as the temperature was not too low to greatly inhibit the speed of the
reactant molecules.

PRECAUTIONS

1.) It was ensured that caution was taking around the flame of the Bunsen burner
2.) It was ensured that test tubes were labelled to prevent the confusion of results

SOURCES OF ERROR

1.) Parallax error occurred when measuring solutions and taking thermometer
readings due to the eye not being in the correct position above the meniscus
level.
2.) The reaction time of students was slow when using the stopwatch and placing
the amylase in the test tubes and in the water baths simultaneously

LIMITATIONS:
1.) It was difficult to regulate the temperatures at 5O 0C and 15 0C as the ice
began to melt and the water bath became too hot.

REFLECTION

I have gained a greater understanding of enzymatic-catalysed reactions and its


importance in the body for speeding up or slowing down chemical reactions to maintain
homeostasis. I find it incredibly fascinating the effect temperature has on the rate of
enzyme-catalysed reactions and the connection that the more kinetic energy a molecule
possesses the faster its rate of reaction . Therefore I was able to relate it too how
enzymes work in reagent sticks and extracting juice from fruit.

CONCLUSION

It is concluded that an increase in temperature to a certain degree increases the rate of


an enzymatic reaction

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