Enzymes Lab Report
Title: The Effect of Varying Amounts of Substrate and Enzyme on a Reaction Rate
Abstract In living organisms, certain reactions must take place rapidly to assist life. This occurs because of enzymes, because all reactions would take place too slowly to sustain life (Jacklet, 237). Enzymes are large protein molecules that catalyze specific chemical reactions without being used up in the process. Each enzyme has a region on its surface, called the active site, which recognizes a specific substrate molecule. The substrate is chemically attached to the active site and binds an enzyme-substrate complex. With the use of a spectrophotometer, the absorbance is recorded and the rate of reaction is observed when differing amounts of substrate and …show more content…
These activities are only possible because of the presence and activity of enzymes. Each enzyme reacts with a substrate molecule, and during the reaction, the substrate is broken down to products which are then released. Varying the enzyme concentration, as well as varying the amount of substrate, can change the rate of the reaction. A greater number of enzyme molecules mean more active sites, which will speed up the reaction as they bind with substrate molecules. As the substrate increases, the same can be said, up to a certain concentration known as the saturation point. According to these enzyme processes, it can be assumed that as the amount of the enzyme increases as the substrate remains constant, the absorbance will increase. Likewise, it can be assumed that as the amount of substrate increases as the enzyme stays constant, the absorbance will increase as
Abstract In living organisms, certain reactions must take place rapidly to assist life. This occurs because of enzymes, because all reactions would take place too slowly to sustain life (Jacklet, 237). Enzymes are large protein molecules that catalyze specific chemical reactions without being used up in the process. Each enzyme has a region on its surface, called the active site, which recognizes a specific substrate molecule. The substrate is chemically attached to the active site and binds an enzyme-substrate complex. With the use of a spectrophotometer, the absorbance is recorded and the rate of reaction is observed when differing amounts of substrate and …show more content…
These activities are only possible because of the presence and activity of enzymes. Each enzyme reacts with a substrate molecule, and during the reaction, the substrate is broken down to products which are then released. Varying the enzyme concentration, as well as varying the amount of substrate, can change the rate of the reaction. A greater number of enzyme molecules mean more active sites, which will speed up the reaction as they bind with substrate molecules. As the substrate increases, the same can be said, up to a certain concentration known as the saturation point. According to these enzyme processes, it can be assumed that as the amount of the enzyme increases as the substrate remains constant, the absorbance will increase. Likewise, it can be assumed that as the amount of substrate increases as the enzyme stays constant, the absorbance will increase as