This experiment tested the cause and effect of environmental factors on enzymes reaction rate. The two environmental factors studied where temperature and pH. Enzymes are catalysts that lower the activation energy of specific reactions without themselves being consumed are altered in any way. When the activation energy is lowered it enables the reaction to be accelerated with less energy expenditure (Campbell, 2002). The rate is determined by speed at which a substrate binds to the enzyme to form an enzyme-substrate complex then decomposes to form the product. This speed is also determined by the concentration of the substrate, if the substrate concentration is higher then the possibility of forming an enzyme-substrate complex is also increased (Vliet, 2007).
The rate of enzymatic activity is based greatly on the surrounding environment. Catalytic activity occurs the most at optimum temperatures and pH's which are specific to each enzyme. Increased temperatures increases molecular motion which in turn allow for increased substrate-enzyme collisions and more rapid reactions. But if the temperature is too high the enzyme is at risk for becoming denatured. Denaturization is an alternation in the tertiary structure of the enzyme which does not allow for efficient product conversions. This same possibility is likely to occur when the optimum pH is not met (Vliet 2007). Neutral environments have a pH of around 7 (Campbell, 2002). So if the environment is too acidic or basic then the enzymatic reaction rate is lowered.
This particular experiment studies the effect of temperature and pH on the enzyme alpha-amylase. Alpha amylase hydrolyzes starch into glucose molecules (Vliet, 2007). The reaction rate of the enzyme will be measured by determining the absorbency of the starch substrate. Since starch and iodine form a dark purple/blue substance the concentration of the solution allows us to determine the rate at which alpha amylase is converting starch into glucose. Also, an iodine indicator stops the reaction, which makes it possible to read the absorbency at a specific time interval. Absorbency is measured through a spectrophotometer which reads the amount of light that is being transmitted through a solution at a set wavelength (Vliet, 20007)
The purpose of this lab was to determine the optimum temperature and pH for which the enzyme alpha-amylase is most effective at. I predict that catalytic activity will...