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The Effect of Enzyme Focus on Reaction Rate

Determination of the effect of enzyme focus on catalysis using starch an amylase.

INTRODUCTION

Enzymes are reported to be catalytic proteins which escalates the rate of any chemical reaction without having to be altered along the way of that effect. [1] A substrate is a element which an enzyme acts upon. No bond is formed between the enzyme and the substrate in the reaction thus the enzyme goes back to its original shape and can be used again. [2]An enzyme binds to a substrate via the productive site thus developing an enzyme - substrate complex They are very specific in their effect and also to the substrate they are binding with. Enzymes function effectively when the form of the substrate matches the enzyme's energetic site and their performing would depend upon its 3d structure. They undertake catalysis by lowering the activation energy so that more substances will be turned on thus getting the reaction occurring easier [1] [2]

In this test amylase is use to breakdown the starch substances. Starch is the substrate used and amylase is the enzyme. There is a change when amylase reacts with starch. There is a release of your disaccharide - maltose. As time raises there will less abundance of starch and even more of the glucose present. So when this is put into iodine the blue/black colour will decrease to a light yellowish shade. [4]

The awareness of the enzyme is important in chemical response as it is needed to react with the substrate. Often a tiny amount of enzyme can ingest a large amount of substrate. But as enzyme amount rises so is the option of energetic sites thus these will convert substrate substances into products. What this is basically saying is the fact if the enzyme focus is to be increased there has to be an excessive amount of substrate present which in other words means that the response must be independent of the attentiveness of substrate. [3]

Apart from the concentration of substrate and enzyme there are other factors which can also affect the enzyme to function to its maximum capacity. Included in these are temperature, pH, and inhibitors. Higher temps would allow for much more collisions that occurs therefore allow substrate to bind to the enzyme's effective site more recurrent. Since enzymes just work at a certain temp range activity would decline once this range could have been exceeded and the enzyme is denatured. Each enzyme has its own optimum where it functions best. Pepsin, an enzyme found in our stomach, works best in acidic conditions. Some enzymes becomes denatured thus deactivated when pH rises down.

I anticipate that the pace of the response will increase as the attentiveness rises and vice versa. The reaction will occur fast after the enzyme is added but it'll slow down upon descending to the last test. I also assumed that just a few of the test tube will produce a blue/black colour since the starch within the perfect solution is will be hydrolyzed.

Apparatus/Materials

Water

Buffer solution ( pH 6. 8)

1% starch solution

1% amylase solution (Saliva)

Dropper

3 beakers

3 10 ml measuring cylinders

12 test tubes

Test pipe rack

Timer

Method:

Four test pipes were labeled A - D

2 ml of normal water was assessed and positioned in test tube A. 2 ml of amylase (saliva) was measured and put in the same test pipe.

Again 2 ml of normal water was measured and positioned in a second test pipe, test pipe B, also to this 2 ml of the solution in test tube A was added.

Another 2ml of drinking water was added to a 3rd test pipe, test tube C, and also to this, 2ml of the solution from test tube B was added.

A further 2ml of drinking water was added to test pipe D, and to this 2 ml of solution from test tube C was added. Two milliliters of solution from test pipe D was discarded so that will have equal amounts of solution.

Forty drops of buffer solution was put into test pipe A.

Eight (8) test tubes were accumulated and positioned in a test pipe rack. Two drops of iodine solution was located into each using a dropper.

To pipe A 0. 5 ml 1% starch solution was added.

One drop of solution from tube A was immediately used in test pipe #1 comprising iodine solution. The dropper was properly rinsed.

After 1 minute, one drop of solution from tube A was added using the dropper to the next tube including iodine. The dropper was rinsed carefully. This was done for all the other test pipes that remained.

The contents in all eight iodine test pipes were discarded. The tubes were completely rinsed and dried for use in the next round of testing.

Steps 6 - 11 was repeated for test tubes B, C, and D.

RESULTS

Test Tube

Test Tube with Iodine

Observations

A

B

1

2

3

4

5

6

7

8

1

2

3

4

5

6

7

8

Dark brown solution with smaller amounts of blue/dark-colored grains. We were holding apparent 17 mere seconds after adding solution A

Dark brown grainy solution.

Orange brownish solution with contaminants which were also orange -brown

Light orange - dark brown solution. No grainy allergens present

Lighter orange - brownish solution

Yellow - brownish solution

Yellow brown solution. This is lighter than tube No. 6

Light yellow brownish solution. This was remarkably lighter than others.

Blue- dark-colored with coarse allergens. Small traces ( 320 mere seconds)

Orange darkish solution

Light orange brown solution with grains present

Orange dark brown solution with tiny grains present

Orange brown solution

Orange brown solution

Light orange brownish solution

Light orange brownish solution

C

D

1

2

3

4

5

6

7

8

1

2

3

4

5

6

7

8

Dark brown with small traces of dark particles (less than with pipe B)

(455 secs)

Orange brown solution

Orange darkish solution

Orange brown

Dark orange brown

Dark orange brown

Very darkish solution with a few grainy particles

Very dark brown with plenty of grainy particles

Dark brownish solution with really small traces of dark-colored grains ( 560 mere seconds)

Dark orange darkish, no grainy particles present

Dark orange brown solution

Orange dark brown solution

Orange brownish solution

Yellow/ orange- dark brown solution

Yellow dark brown solution

Light yellow darkish solution

The graph shows the way the attentiveness of the enzyme affects the entire rate of the response. A higher concentration of the enzyme will create a faster occurring reaction when compared to a lower concentration. From graph as time proceeds the response rate drops significantly.

DISCUSSION:

This lab exercise demonstrated the ability associated with an enzyme to hydrolyze the substrate molecule. The enzyme used was amylase and the substrate was starch. The starch is exactly what the amylase actually functions upon to give the end products i. e amylase reduces starch.

Substrate ENZYME Products

Enzyme amount and substrate attentiveness play a vital role in enzymatic activity.

The more enzymes available, the quicker the reaction will occur before substrate is all used up

More substrates will also suggest quicker activity, before enzyme is fully saturated so that it

cannot continue increasing its activity. [1]

Based on the results from tube A, a blue/dark-colored colouration was known. This suggested that there is significant amount of starch present. Iodine can be an sign for the occurrence of starch. This same shade was observed for pipes B- D however the traces of blue /dark-colored colour lowered from pipe A -D. As the testing proceeded to the previous tube, the color of the answer for each collection changed from a dark brown way to light yellowish and in some cases to a light orange brownish solution.

A reasonable reason because of this is that we now have fewer enzymes present as you move from tube A-D thus the starch will not be divided. When there can be an inadequate amount of enzyme present the reaction will not improve as quick as it could because the effective sites present are occupied. When the attention or amount of enzymes is increased then this might make provision for an increase in effect rate. Reaction rate would increase due to the fact that you will see more vigorous sites that are unoccupied. However, if there is an excess of enzyme molecule, the speed wouldn't normally increase if more is added but it could reach at a point where it would level off. [2]

Another reasoning behind the colour change in that following the amylase reacted with the starch you will see a discharge of maltose which is a disaccharide. Less starch will be present as time proceeds and much more maltose will be there. In addition less starch will be available to respond with iodine thus the blue/dark-colored colour will decrease.

The predictions made were reasonably correct since a lower amount of enzyme produced a effect which was sluggish and the one that experienced less products being developed.

Various factors could have afflicted the results of the laboratory which may have given some amount of inaccuracy. Included in these are temperatures and pH. The enzyme perhaps would have functioned better in a certain temperature range rather than normal room heat range.

CONCLUSION

Based on the results obtained from the experiment it could be concluded that the concentration of enzymes influences the rate of the chemical reaction. If enzyme amount is decreased then your effect rate will also reduce. When there is sufficient enzyme to bind with substrate then your reaction will move forward fast if there are insufficient enzymes present then the reaction will slow down

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