This experimentation was to evaluate absorbance and the reaction rate of an enzyme, '-amylase in starch-iodine solution. We will be testing the relationship between enzymatic reaction affected by temperature and pH. Through the testing the enzyme at different temperatures, and different pH levels; it would determine at which temperature and pH level the enzyme worked the most efficiently. Analyzing absorbance of the solutions with spectrophotometery will determine the reaction rate.
To test the optimal pH, the starch and a buffer were combined at a specific pH level and tested the absorbance of a solution at various times. To resolve the reaction rate of a solution at various temperatures, the solution was put into water both set to a specific temperature and its absorbance was recorded at different times.
Four specific graphs were drawn to determine at which pH level and temperature was the optimum for the enzyme after the experiment. Although hypothesis that I made that it would work best under temperature near 40'' and at a pH of around 4, through my results the enzyme worked more efficiently under the temperature of 55''and pH level at 4.5. However, since the whole testing experimental was taken only once; we can not state that the result was precisely accurate. Introduction: The catalysts are the substance that speeds up chemical reactions in living organisms. The enzymes are the protein catalysts to lower the activation energy of a reactant. Enzymes are not able cause an inefficient reaction to occur and only able to increase the rate of biochemical reaction. The molecule that is reacting in enzymatic reaction is called a substrate. When an enzyme and substrate congregate together, then it forms an enzyme-substrate complex. As the enzyme works to accelerate the chemical reaction changes catalytic property and ultimately it decomposed.
The rate of the enzymatic reaction is when the rate at which the enzyme-substrate complex forms and it decomposes to form the product. There are two factors that formulate enzymatic reaction. The first factor is that time required by the enzyme to alter the substrate to its product, and the second factor is the rate that it takes to form the enzyme-substrate complex. A typical enzymatic reaction shows a fading of the substrate after an extended period of time. The substrate becomes a part of the product during this reaction, diminishing the probability that an enzyme molecule would have during the reaction, reducing the chances that an enzyme molecule would have to meet with substrate molecule leading to a decrease of the reaction rate. Temperature and pH would be the other factors that related with a change in the rate of an enzymatic reaction. At particular pH and temperature levels, the enzyme performs its best but if the two factors are either excessively high or excessively low, it can cause the enzyme to denature and diminishing the reaction rate.
In this research, we used the enzyme '-amylase, where found in both plants and animals. Amylase hydrolyzes starch, glycogen, and dextrin to form glucose and maltose. (Brewing 2002) In animals '-amylase is digestive enzymes that made from mainly within the pancreas and salivary glands to break down starches form the nutrients. (Great Vista Chemicals, 2005) Human amylase has an optimum pH of 7.2-7.4, and denatures at temperatures above 60??. (Research Machines, 2005) With the warm condition enzymes like '-amylase have been said to work the most efficiently, which is around 40??. It was also stated that they work best in the acidic rage from 3.5 to 5.5. (Thermophilic Moulds in Biotechnology, 1999)
With preceding experiments, a hypothesis can be stated that the optimal pH of '-amylase would occur m at a temperature near 40'' and pH at around 4. This experiment would examine the hypothesis and would confirm the optimal of both the temperature and pH of the enzyme '-amylase. Materials and Methods:
Cited: Amylase Enzyme. Great Vista Chemicals URL:(www.greatvistachemicals.com/biochemicals/amylase.html) B N Johri, T Satyanarayana, J Olsen. 1999. Thermophilic Moulds in Biotechnology. Kluwer Academic Publishers. AA Dordrecht. Netherlands. Michael Lewis, Tom W Young 2002. Brewing. Kluwer Academic/Plenum Publishers New York, New York. Research Machines. Plc 2.5 Helicon Publishing. URL:(www.tiscali.co.uk/reference/encyclopedia/hutchinson/m0007936.html) Vliet, K.A.(ed.). 1996. A Laboratory Manual for Integrated Principles of Biology: Part One BSC2010L. Ginn Press, Needham Heights, Massachusetts.
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