Introduction
The human body contains thousands of biological molecules that assist in chemical reactions within cells. These biological molecules are called enzymes. Enzymes are the catalysts of biological systems. Although, some enzymes represent and depend on RNA (ribonucleic acid) most are made up of amino acids making them proteins. Since there are many chemical reactions that take place within very cell of the body, enzymes are ideal when keeping these cells alive because they serve as biological catalysts [3]. Enzymes are facilitators that speed up the chemical reactions by lowering the activation energy of reactions, without letting themselves be consumed during the catalytic activity. The coexistence of catabolic and anabolic pathways …show more content…
Enzymes can either speed up the reaction or become denatured resulting in no reaction. If an enzymes temperature increases, the enzyme will stop working because a permanent change to the shape of the active site is the result. A change in pH can also change the enzyme active site structure. If the pH increases, the H+ ions increase as well, changing the active site when the H +ions interact with polar molecules on the enzyme protein structure. This causes the protein sequence to unwind, meaning the active site is not complementary to the substrate and the rate of reaction decreases since small amounts of enzyme substrate formed. In the enzyme-catalyzed reaction, at low concentration of substrate, there is usually a steep increase in the rate of reaction with increasing substrate concentration. The catalytic site of the enzyme is empty ready for the substrate to bind with a restricted rate at which the product formed by the concentration of substrate available. Based on our experiment, some of the results are not the same as the theory. Our results depicted a high Km value compared to the substrate concentration range within the plot; as a result, the enzyme did not saturate with the substrate. Therefore, the rate of formation of the product depended on the amounts available of the substrate and its enzyme activity varied as the concentration varied. Even though the experimental lab procedures were self-explanatory, I do have a suggestion for the lab that can possibly improve the experiment. I suggest the instructor provides us with graphs of different types of enzymes, in addition, compare, and contrast those graph to one’s experimental results to see which would have a saturated enzyme and a more precise reaction rate. After all the lab covered the concepts of kinetic energy and the important
The human body contains thousands of biological molecules that assist in chemical reactions within cells. These biological molecules are called enzymes. Enzymes are the catalysts of biological systems. Although, some enzymes represent and depend on RNA (ribonucleic acid) most are made up of amino acids making them proteins. Since there are many chemical reactions that take place within very cell of the body, enzymes are ideal when keeping these cells alive because they serve as biological catalysts [3]. Enzymes are facilitators that speed up the chemical reactions by lowering the activation energy of reactions, without letting themselves be consumed during the catalytic activity. The coexistence of catabolic and anabolic pathways …show more content…
Enzymes can either speed up the reaction or become denatured resulting in no reaction. If an enzymes temperature increases, the enzyme will stop working because a permanent change to the shape of the active site is the result. A change in pH can also change the enzyme active site structure. If the pH increases, the H+ ions increase as well, changing the active site when the H +ions interact with polar molecules on the enzyme protein structure. This causes the protein sequence to unwind, meaning the active site is not complementary to the substrate and the rate of reaction decreases since small amounts of enzyme substrate formed. In the enzyme-catalyzed reaction, at low concentration of substrate, there is usually a steep increase in the rate of reaction with increasing substrate concentration. The catalytic site of the enzyme is empty ready for the substrate to bind with a restricted rate at which the product formed by the concentration of substrate available. Based on our experiment, some of the results are not the same as the theory. Our results depicted a high Km value compared to the substrate concentration range within the plot; as a result, the enzyme did not saturate with the substrate. Therefore, the rate of formation of the product depended on the amounts available of the substrate and its enzyme activity varied as the concentration varied. Even though the experimental lab procedures were self-explanatory, I do have a suggestion for the lab that can possibly improve the experiment. I suggest the instructor provides us with graphs of different types of enzymes, in addition, compare, and contrast those graph to one’s experimental results to see which would have a saturated enzyme and a more precise reaction rate. After all the lab covered the concepts of kinetic energy and the important