The Effect of Enzyme Concentration on Reaction Rate

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Enzymes are said to be catalytic proteins which increases the rate of a chemical reaction without being altered in the procedure of that reaction. A substrate is a substance which an enzyme acts upon. No bond is formed between the enzyme and the substrate in the reaction therefore the enzyme goes back to its original form and can be used once more.

An enzyme binds to a substrate via the active site therefore organizing an enzyme – substrate composite They are really specific in their reaction and besides to the substrate they are adhering with. Enzymes function right when the form of the substrate matches the enzyme ‘s active site and their operation is dependent upon its three dimensional construction. They undergo contact action by take downing the activation energy so that more molecules will be activated therefore holding the reaction happening more easy.

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In this experiment amylase is use to interrupt down the amylum molecules. Starch is the substrate used and amylase is the enzyme. There is a alteration when amylase reacts with amylum. There is a release of a disaccharide – malt sugar. As clip additions at that place will less copiousness of amylum and more of the sugar nowadays. So when this is added to iodine the blue/black coloring material will diminish to a light xanthous shadiness.

The concentration of the enzyme is of import in chemical reaction as it is needed to respond with the substrate. Often a little sum of enzyme can devour a big sum of substrate. But as enzyme concentration additions so is the handiness of active sites therefore these will change over substrate molecules into merchandises. What this is fundamentally stating is that if the enzyme concentration is to be increased at that place needs to be an surplus of substrate nowadays which in other words means that the reaction must be independent of the concentration of substrate.

Apart from the concentration of substrate and enzyme there are other factors which can besides act upon the enzyme to map to its optimal capacity. These include temperature, pH, and inhibitors. Higher temperature would let for more hits to happen hence allow substrate to adhere to the enzyme ‘s active site more frequent. Since enzymes work at a certain temperature scope activity would worsen one time this scope would hold been exceeded and the enzyme is denatured. Each enzyme has its ain optimum where it functions best. Pepsin, an enzyme found in our tummy, works best in acidic conditions. Some enzymes becomes denatured therefore deactivated when pH goes up down.

I predict that the rate of the reaction will increase as the concentration additions and frailty versa. The reaction will happen fast once the enzyme is added but it will decelerate down upon falling to the last trial. I besides believed that merely a few of the trial tubing will bring forth a blue/black coloring material since the amylum nowadays in the solution will be hydrolyzed.


  • Water
  • Buffer solution ( pH 6.8 )
  • 1 % amylum solution
  • 1 % amylase solution ( Saliva )
  • Dropper
  • 3 beakers
  • 3 10 milliliter measurement cylinders
  • 12 trial tubings
  • Test tubing rack
  • Timer


  • Four trial tubings were labeled A – Calciferol
  • 2 milliliter of H2O was measured and placed in trial tubing A. 2 milliliter of amylase ( spit ) was measured and placed in the same trial tubing.
  • Again 2 milliliter of H2O was measured and placed in a 2nd trial tubing, trial tubing B, and to this 2 milliliter of the solution in trial tubing A was added.
  • Another 2ml of H2O was added to a 3rd trial tubing, trial tubing C, and to this, 2ml of the solution from trial tubing B was added.
  • A farther 2ml of H2O was added to prove tubing D, and to this 2 milliliter of solution from trial tubing C was added. Two millilitres of solution from trial tubing D was discarded so that all will hold equal sums of solution.
  • Forty beads of buffer solution was added to prove tubing A.
  • Eight ( 8 ) trial tubings were collected and placed in a trial tubing rack. Two beads of iodine solution was placed into each utilizing a dropper.
  • To tube A 0.5 milliliter 1 % starch solution was added.
  • One bead of solution from tubing A was instantly transferred to prove tubing # 1 incorporating iodine solution. The dropper was decently rinsed.
  • After 1 minute, one bead of solution from tubing A was added utilizing the dropper to the 2nd tubing incorporating I. The dropper was rinsed exhaustively. This was done for all the other trial tubings that remained.
  • The contents in all eight iodine trial tubings were discarded. The tubings were exhaustively rinsed and dried for usage in the following unit of ammunition of trials.
  • Stairss 6 – 11 was repeated for trial tubing B, C, and D.

The graph shows how the concentration of the enzyme affects the overall rate of the reaction. A higher concentration of the enzyme will bring forth a faster happening reaction than a lower concentration. From the graph as clip proceeds the reaction rate beads significantly.


This lab exercising demonstrated the ability of an enzyme to hydrolyse the substrate molecule. The enzyme used was amylase and the substrate was amylum. The amylum is what the amylase really acts upon to give the terminal merchandises i.e amylase interruptions down amylum.

Enzyme concentration and substrate concentration play a critical function in enzymatic activity. The more enzymes available, the quicker the reaction will happen until the substrate is all used up. More substrates will besides intend quicker activity, until the enzyme is to the full saturated so that it can non go on increasing its activity.

Based on the consequences obtained from tubing A, a blue/black color was noted. This indicated that there was important sum of amylum nowadays. Iodine is an index for the presence of amylum. This same coloring material was noted for tubes B- D but the hints of bluish /black coloring material decreased from tubing A -D. As the trials proceeded to the last tubing, the coloring material of the solution for each set changed from a dark brown solution to light xanthous and in some instances to a light orange brown solution.

A sensible account for this is that there are fewer enzymes nowadays as you move from tube A-D therefore the amylum will non be broken down. When there is an deficient sum of enzyme present the reaction will non come on every bit speedy as it would because the active sites present are occupied. If the concentration or sum of enzymes is increased so this would do proviso for an addition in reaction rate. Chemical reaction rate would increase due to the fact that there will be more active sites that are unoccupied. However, if there is an surplus of enzyme molecule, the rate would non increase if more is added but it would make at a point where it would level off.

Another logical thinking behind the color alteration in that after the amylase reacted with the amylum there will be a discharge of malt sugar which is a disaccharide. Less amylum will be present as clip returns and more malt sugars will be present. In add-on less amylum will be available to respond with iodine therefore the blue/black coloring material will diminish.

The anticipations made were reasonably right since a lower concentration of enzyme produced a reaction which was slow and one that had less merchandises being formed. Assorted factors could hold affected the consequences of the lab which may hold given some sum of inaccuracy. These include temperature and pH. The enzyme possibly would hold functioned better in a certain temperature scope alternatively of normal room temperature.


Based on the consequences obtained from the experiment it can be concluded that the concentration of enzymes influences the rate of a chemical reaction. If enzyme concentration is decreased so the reaction rate will besides diminish. If there is sufficient enzyme to adhere with substrate so the reaction will continue fast and if there are deficient enzymes present so the reaction will decelerate down.

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The Effect of Enzyme Concentration on Reaction Rate. (2016, Dec 07). Retrieved from

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