Enzymatic Activity of Salivary Amylase
Enzymatic Activity of Salivary Amylase
Abstract: Salivary amylase is an enzyme that can digest starch molecules and break them down to sugar molecules. In this experiment, the enzymatic activity and specificity of salivary amylase was examined depending on the changes in pH and temperature. In the first part of the experiment, the effect of temperature was determined, using constant temperature bath (4, room temp, 37, 50, 60, and 70°C). Having the room temp and 50°C as the highest and 37°C as infinite. In the second part of the experiment, the effect of pH was examined. Using the buffered solutions: acetate solutions (pH 4 and 5), phosphate buffer (pH 6.7 and 8), and bicarbonate buffer (pH 10). The results were recorded having all of them as infinite.
Keywords: enzyme, infinite, pH, temperature, salivary amylase, starch
I. Introduction
Enzymes are proteins that catalyze or speed up the rate of chemical reactions. Like all catalysts, enzymes work by lowering the activation energy for the reaction, thus dramatically increasing the rate of reaction.[1] As with all catalysts, enzymes are not consumed by the reactions they catalyze nor do they alter the equilibrium of these reactions. All known enzymes are proteins, they are high molecular weight compounds made up principally of chains of amino acids linked together by peptide bonds. See Figure 1.
Figure 1. Typical protein structure – two amino acids joined by peptide bonds Enzymes require the presence of other compounds - cofactors - before their catalytic activity can be exerted. This entire active complex is referred to as the holoenzyme; i.e., apoenzyme (protein portion) plus the cofactor (coenzyme, prosthetic group or metal-ionactivator) is called the holoenzyme.[1] Figure 2. Haloenzymes – apoenzymes plus various types of cofactors
One of the properties of enzymes that make them so important as diagnostic and research tools is the specificity they exhibit relative to the reactions they
Abstract: Salivary amylase is an enzyme that can digest starch molecules and break them down to sugar molecules. In this experiment, the enzymatic activity and specificity of salivary amylase was examined depending on the changes in pH and temperature. In the first part of the experiment, the effect of temperature was determined, using constant temperature bath (4, room temp, 37, 50, 60, and 70°C). Having the room temp and 50°C as the highest and 37°C as infinite. In the second part of the experiment, the effect of pH was examined. Using the buffered solutions: acetate solutions (pH 4 and 5), phosphate buffer (pH 6.7 and 8), and bicarbonate buffer (pH 10). The results were recorded having all of them as infinite.
Keywords: enzyme, infinite, pH, temperature, salivary amylase, starch
I. Introduction
Enzymes are proteins that catalyze or speed up the rate of chemical reactions. Like all catalysts, enzymes work by lowering the activation energy for the reaction, thus dramatically increasing the rate of reaction.[1] As with all catalysts, enzymes are not consumed by the reactions they catalyze nor do they alter the equilibrium of these reactions. All known enzymes are proteins, they are high molecular weight compounds made up principally of chains of amino acids linked together by peptide bonds. See Figure 1.
Figure 1. Typical protein structure – two amino acids joined by peptide bonds Enzymes require the presence of other compounds - cofactors - before their catalytic activity can be exerted. This entire active complex is referred to as the holoenzyme; i.e., apoenzyme (protein portion) plus the cofactor (coenzyme, prosthetic group or metal-ionactivator) is called the holoenzyme.[1] Figure 2. Haloenzymes – apoenzymes plus various types of cofactors
One of the properties of enzymes that make them so important as diagnostic and research tools is the specificity they exhibit relative to the reactions they
References: [1] Bennett, T. P. & Frieden, E. Modern Topics in Biochemistry, pg. 43-45, Macmillan, London (1969). [2] Holum, J. Elements of General and Biological Chemistry, 2nd ed., 377, Wiley, NY (1968). [3] Pfeiffer, J. Enzymes, the Physics and Chemistry of Life, pg 171-173, Simon and Schuster, NY (1954) [4] Martinek, R. Practical Clinical Enzymology: J. Am. Med. Tech., 31, 162 (1969). [5] Harrow, B., and Mazur, A.: Textbook of Biochemistry, 109, Saunders, Philadelphia (1958).