Independent Variable. pH 3. Controlled Variables. temperature; amount of substrate (sucrose) present; sucrase + sucrose incubation time Effect of Temperature on Enzyme Activity. 1.
Any increase in the rate of reaction will cause an increase in the pressure of the oxygen. The first line of the graph (top) represents the normal rate of the reaction in a water solution of hydrogen peroxide and catalase. The second line represents the rate of reaction when acid is added to the solution and the third line represents the rate of reaction when a base is added to the solution. 1. What variable is plotted on the x-axis?
The Ksp of Magnesium Oxalate Abstract The Ksp for the acid catalyzed titration of the saturated oxalate is 1.8 x 10-3. Introduction In this experiment, the solubility equilibrium for the salt magnesium oxalate must be found in order to determine a solubility product constant. Solubility equilibrium is a type of dynamic equilibrium which exists when a chemical compound in the solid state is in chemical equilibrium with a solution of that compound. At the point of equilibrium the solution becomes saturated. The chemical reaction used to find this constant is as follows: MgC2O4 (s) ↔Mg(aq)2++ C2O4 (aq)2- Kc= Mg2+[C2O42-][MgC2O4] Ksp=Mg2+[C2O42-] The solid salt magnesium oxalate is prepared through the following precipitation reaction: Mg(SO4)(aq)+NaC2O4 (aq) → MgC2O4 (s)+NaSO4 (aq) Next, the concentration of the Mg2+ and C2O42- ions is found through a redox titration.
Was the rate of increase of sucrase activity higher at a pH of 8.5 or a pH of 5.5? 3. State the optimum temperature for sucrase activity, and describe how sucrase activity changes at lower and higher temperatures. The optimum temperature for sucrase activity is 40˚ C. Sucrase activity drops at lower and higher temperatures (it kind of levels out with minimal change at higher temperatures but is still dropping). See Table 3: Effect of Sucrose Concentration on Sucrase Activity See Graph: Effect of Sucrose Concentration on Sucrase Activity 4.
The dependant variable of this experiment will be the rate of reaction of the enzyme catecholase with its substrate catechol. The independent variable of this experiment is the various pH levels that the catecholase and catechol are exposed
Title : Enzyme Activity Aim/Objective : Studying the effects of substrate B (starch suspension) concentration on the activity of enzyme A (salivary amylase). Introduction : Enzyme activities are influenced by various factors. Each enzyme has its own optimum condition whereby its activity is at the highest rate. One of the factors is the concentration of the substrate used. The rate of an enzyme-catalysed reaction increases in direct proportion to the substrate concentration until the reaction reaches a maximum rate.
Explain why denatured sucrase was used as a control. Denatured sucrose has less activity. Laboratory Report/ Raya Cupler/ Enzyme Activity/ Jennifer Frere/ 05.19.2015/ Page [1] of [4] 6. Addition of DNS at the end of the incubation period stopped the reaction by denaturing sucrase. Explain why it is important to denature sucrase before measuring product concentration.
Dependent Variable. amplitude and frequency of sEMG spikes 2. Independent Variable. muscle load 3. Controlled Variables.
This change is caused by the A. addition of a catalyst. B. increase in surface area. C. change in nature of the reactants. D. increase in concentration of reactants. 17.
MATERIALS AND METHODS Measurement of Threshold Stimulus 1. Dependent Variable is the contraction force 2. Independent Variable is the stimulation voltage 3. Controlled Variables are the muscle fiber length, temperature, freq of stimulation. Effect of Muscle Length on Contraction 1.