Ap Bio Enzyme Lab
Introduction
Enzymes are catalytic proteins. The purpose of a catalyst is to speed up metabolic reactions by lowering the free energy of activation or activation energy. Activation energy is known as the amount of energy needed to push the reactants over an energy barrier, so that the downhill part of the reaction can begin (Campbell 151). In an enzyme catalyzed reaction, the enzyme binds to its substrate, which is the reactant an enzyme acts on. In the reactions, the enzymes are very specific, where only a restricted region of the enzyme molecule binds to the substrate. This region is known as the active site (Campbell 152). The specificity of an enzyme results from its shape; the shape is form by the amino acid sequence since enzymes are proteins. If the shape of the substrate fits the shape of the active site, the enzyme will alters its shape so the active site embraces the substrate and maintains a firm grip, known as induced fit. This allows for great variations of enzymes.
Abstract
In this experiment, my lab partners and I tested how time effects a catalase reaction. The amount of hydrogen peroxide was recorded after the reaction for the certain time given has taken place. We used sulfuric acid to stop the reaction with the catalase from occurring. This process is known as denaturing (Campbell 152). The potassium permanganate in this experiment was used as hydrogen peroxide indicator. It determined the amount of hydrogen peroxide remaining after the reaction occurred. Based on our experiment we observed that the time does play a crucial role on the catalase reaction because as we increased the time of the reaction, the amount of hydrogen peroxide decreased.
Problem: How does time affect the amount of hydrogen peroxide remaining after the catalase and H2O2 reaction?
Hypothesis: I believe if you shorten the time of the catalase and H2O2 reaction, then there will be more H2O2 will be present. Materials and Methods
Materials: Beakers, 50mL of
Enzymes are catalytic proteins. The purpose of a catalyst is to speed up metabolic reactions by lowering the free energy of activation or activation energy. Activation energy is known as the amount of energy needed to push the reactants over an energy barrier, so that the downhill part of the reaction can begin (Campbell 151). In an enzyme catalyzed reaction, the enzyme binds to its substrate, which is the reactant an enzyme acts on. In the reactions, the enzymes are very specific, where only a restricted region of the enzyme molecule binds to the substrate. This region is known as the active site (Campbell 152). The specificity of an enzyme results from its shape; the shape is form by the amino acid sequence since enzymes are proteins. If the shape of the substrate fits the shape of the active site, the enzyme will alters its shape so the active site embraces the substrate and maintains a firm grip, known as induced fit. This allows for great variations of enzymes.
Abstract
In this experiment, my lab partners and I tested how time effects a catalase reaction. The amount of hydrogen peroxide was recorded after the reaction for the certain time given has taken place. We used sulfuric acid to stop the reaction with the catalase from occurring. This process is known as denaturing (Campbell 152). The potassium permanganate in this experiment was used as hydrogen peroxide indicator. It determined the amount of hydrogen peroxide remaining after the reaction occurred. Based on our experiment we observed that the time does play a crucial role on the catalase reaction because as we increased the time of the reaction, the amount of hydrogen peroxide decreased.
Problem: How does time affect the amount of hydrogen peroxide remaining after the catalase and H2O2 reaction?
Hypothesis: I believe if you shorten the time of the catalase and H2O2 reaction, then there will be more H2O2 will be present. Materials and Methods
Materials: Beakers, 50mL of