As the substrate concentration increases, so will the enzyme activity and hence there will be a quick reaction. however, only up to a certain point ( where, if you drew a graph of the reaction, the line will level off ) as all the active sites in the enzyme are occupied and the reaction cannot go any faster. Here more enzymes will be needed to speed up the reaction.
As the concentration of substrate decreases, due to its conversion to product(s), the rate of the reaction will slow. This is due to the less and less frequent random encounters between substrate and enzyme. As more of the peroxide is converted to oxygen and water, there is less remaining to interact with the enzyme; therefore, the reactions slows.
Most enzyme reaction rates are calculated using a steady state assumption, given that the enzyme concentration typically doesn't change once the reaction is started, The only effect increasing enzyme concentration has is to increase the initial rate of the reaction, until the avaiable enzyme concentration shifts to the concentration of the enzyme-substrate complex. Reference any text on Michaelis Menten Kinetics to see the derivation.
different enzymes require different PH to function effectively, PH too high or low may destroy the enzyme. increasing the substrate amount will increase the resulting products within a time period, this is limited though by the amount of enzyme.
Oddly phased question in my opinion. Vmax is only effected by the amount of enzyme present in the reaction. Substrate concentration has zero effect on Vmax. There for I believe the answer in no. {Enzyme concentration is responsible for this}
There is no straight forward relation between enzyme and activation energy because although energy of reaction is fixed and is governed by laws of chemistry but for biochemical reactions concentration of enzyme and conc. of substrate affect rate of reaction and energy, but in general enzymes decrease activation energy of reaction.
1. Temperature (high temperature might denature an enzyme) 2. Concentration of substrate 3. Presence of a catalyst
Following are the factors affectingenzymes:SalinityTemperatureInhibitorsAllosteric factorspH levelSubstate concentrationCatalystEnzyme concentration
A competitive inhibitor is a molecule that binds to the active site of an enzyme, to prevent substrates entering the active site and therefore lowering the rate of reaction. Some drugs act as competitive inhibitors to control reactions in the body, and the body also releases competitive inhibitors as a means of self control. But remember that the amount of product formed is still remain the same, only the time taken increased.
Oddly phased question in my opinion. Vmax is only effected by the amount of enzyme present in the reaction. Substrate concentration has zero effect on Vmax. There for I believe the answer in no. {Enzyme concentration is responsible for this}
At low concentration of substrate , rate of enzyme action is directly proportional to conc. of substrate .
Oxygen is the product of the catalase reaction causes bubbling. pH is varied when testing the effect of pH on enzyme activity.
Temperature, pH, substrate concentration
When an enzyme is saturated the amount of substrate added no longer as an effect on the rate of the reaction.
increasing the concentration increases the rate of the reaction
increasing the concentration increases the rate of the reaction
increasing the concentration increases the rate of the reaction
For the enzyme to work, its particles must collide with the particles of the substrate. The more particles there are per unit volume, the more frequent the collisions will be. Thus changing the concentration of either chemical will have the same effect.
Because you will still have the same number of enzymes inhibited. For example, you have 20 enzymes and 10 non-competitive inhibitors. Regardless of substrate concentration, at any one time, there will only be 10 enzymes available to accept a substrate. Increasing the substrate concentration does not affect this.
The effect of concentration of reactants on rate of reaction depends on the ORDER of the reaction. For many reactions, as the concentration of reactants increases, the rate of reaction increases. There are exceptions however, for example a zero order reaction where the rate of reaction does not change with a change in the concentration of a reactant.
Increasing the concentration of the reactants the rate of reaction increase.