Environmental Factors Influencing Amylase Enzyme Activity

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  • Topic: Enzyme, PH, Amylase
  • Pages : 9 (2678 words )
  • Download(s) : 718
  • Published : September 26, 2012
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Abstract:
Enzymes are specific-type proteins that act as a catalyst by lowering the activation energy of a reaction. Each enzyme binds closely to the substrate; this greatly increases the reaction rate of the bounded substrate. Amylase enzyme, just like any other enzyme, has an optimum PH and temperature range in which it is most active, and in which the substrate binds most easily. The purpose of this experiment was to determine (1) the reaction rate of an amylase enzyme in starch and (2) the environmental factors that can affect the enzymatic activity. The hypothesis, in relation to the enzymatic activity by variables such as the substrate concentrations, temperature, PH and chemical interactions on the rate of reaction, stated the following scenarios: (1) If the substrate concentration is increased, then the enzymatic rate will increase (2) If the temperature is increased, then the enzymatic rate will also increase (3) If the PH level is increased, then the enzymatic rate will decrease. To test the effect of a substrate concentration on enzyme activity, the amylase enzymes were combined with a different substrate concentration (starch) and the rate of the reaction was determined with the aid of I2kI. If starch was detected, the solution turned to dark blue; if the starch was already broken down, then reaction stayed colorless. To test the optimal PH, the starch and a buffer were combined at a specific PH level and the rate of reaction was tested. To determine the optimal temperature of amylase enzyme, the solution and amylases enzyme were held at various temperatures and the rate of reaction was determined. The rate of reaction for amylase enzyme with less of the substrate concentration (1% starch) with concentration of 0.125% happened at a faster rate of only 20 seconds. The rate of reaction for amylase enzyme with the effect of varied PH occurred at a quicker rate with PH range of 5-6 close to neutral PH of 7.0 in less than 10 second. Finally, the rate of reaction for amylase enzyme at different temperature happened faster at 37°C (close to body temperature) as compared to other temperatures. The results from collected data showed that the smaller the concentration of starch in the amylase enzyme, the faster the rate of reaction and the quicker the breakdown of starch; note: the PH 7.0 was the optimal PH for amylase activity, and the temperature of 37°C was the optimal temperature for amylase enzyme activity.

Introduction:

Enzymes are of primary importance in many chemical reactions which take place in living organisms. When digestion occurs, enzymes released into the mouth, stomach, and intestines catalyze or accelerate reaction which results in the breakdown of large food molecules into small building block molecules. The molecules upon which an enzyme acts are called substrates. Each enzyme binds to the substrate; this binding process is called the “Lock and Key Theory” (i.e. the active site in the enzyme is the keyhole and has a very specific shape. This specific keyhole can only bind with a specific key which will match the keyhole. The key is the substrate molecule. Once the key binds with the keyhole, the reaction takes place.) This process significantly reduces the activation energy necessary for a bound substrate to undergo a particular reaction.

Every enzyme has an optimum PH and temperature range at which the enzyme is structurally most stable and most active, and for which the substrate most easily undergoes the binding process. Any environmental conditions which destroy protein molecules will also eliminate enzymatic activity. The rate of the reaction or enzyme activity can be changed. The environmental factors influencing enzyme activity are the concentration of substrate (or enzymes themselves), the effect of PH, and the variance in temperature. The rate of an enzymatic reaction rises with increasing temperature because substrates collide with active...
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