As the enzyme concentration increases, the rate of reaction will increase because there are many more enzymes present to aid break down the substrate. However, a point will be reached when no matter how much enzyme is present, the reaction will not occur any quicker. This is equilibrium. This happens because all the substrate is being broken down by the exact same amount of enzyme, so enzymes will be present which have no substrate to break down.
As the enzyme concentration increases the rate of enzyme activity increases up to a level where it becomes constant.
This is because the more the enzymes are available, the more substrates are broken in less time.
It then becomes constant as the substrate acts as a limiting factor, which means that there are not enough substrates to be broken down compared to the number of enzymes.
So there are enzymes and there are substrates.
Enzymes dissolves substrates.
= So the more enzymes you have, the more substrates can be dissolved.
so theres more activity.
**but it doesn't work the other way--> more substrate does not increase enzyme activity.
Rebuttal - Substrates do not dissolve due to enzyme action eg glucose can be a substrate but clearly does not require an enzyme to facillitate it's diffusion! Answer Increasing the amount of substate means that it is more likely for the substrate to come into position on the active site of the enzyme. The substrate must locate the active site before the enzyme can work on it and turn it into a product. The more molecules of substate there are the more likely collisions with the active site are and so the greater the rate of enzyme activity up to a point. The point is where the enzyme is acting at it's full capacity, everytime the active site is empty another substrate molecule fills it right away. Increasing the substrate concentration after this point has no effect on the enzyme's rate of reaction.
Increasing enzyme concentration increases the number of collisions between the enzyme molecules and the substrate molecules. This increases the number of successful collisions and the number of enzyme-substrate complexes. Therefore the reaction rate is increased as well and enzyme activity is promoted.
because once lipase enzyme concentration is increased more substrates have a place where to bind, therefore the reaction rate increses. the more emzymes the better, until they actually have reached a maximum. Once there are no more free ubstrates to bind then the rate of reaction reaches a plateau
As the enzyme concentration increases the rate of enzyme activity increases up to a level where it becomes constant.
This is because the more the enzymes are available, the more substrates are broken in less time.
It then becomes constant as the substrate acts as a limiting factor, which means that there are not enough substrates to be broken down compared to the number of enzymes.
The easiest model to visualise this is the "lock and key model". Enzymes are the locks and substrates the keys. The keys are randomly bouncing around in space and by increasing their temperature you increase the speed and which they move. The faster the keys move the more chance they have of "hitting" a lock. This way enzyme activity increases with temperature as there is more liklyhood of the substrates finding the active site in a unit of time when the substrates are moving faster.
It can also be the case that the enzymes are free to move but in nature they can be bound to a fixed surface and so are unable to move.
Increasing temperature allows for more molecule movement, which in turn allows for great chance of a molecule to contact a enzyme. To much heat will denature the enzyme though.
It will increase.
An enzymatic reaction is an equilibrium reaction and the determiners of rate include enzyme and substrate concentration. An increase in either enzyme or substrate concentration will increase the rate of the reaction until one or the other component becomes saturated, beyond its ability to react or be reacted at a higher rate.
The higher the substrate concentration, the higher the rate of reaction, up till the point when the limiting factor is no longer the concentration of substrate but other factors like enzyme concentration of temperature.
pH, temperature, substrate concentration and enzyme concentration influences the rate of reaction
An increase in temperature can increase the enzymatic reactions if it is not too hot and also if the pH is within the idea range it can speed up the reaction. The pH level is usually around 7 for most enzymes.
The rate of enzyme reaction is increased when the substrate concentration is also increased. However, when it reaches the maximum velocity of reaction, the reaction rate remains constant.
An enzymatic reaction is an equilibrium reaction and the determiners of rate include enzyme and substrate concentration. An increase in either enzyme or substrate concentration will increase the rate of the reaction until one or the other component becomes saturated, beyond its ability to react or be reacted at a higher rate.
TemperaturePressure, concentration, dispersion degreeCatalyst, enzyme
The higher the substrate concentration, the higher the rate of reaction, up till the point when the limiting factor is no longer the concentration of substrate but other factors like enzyme concentration of temperature.
As the substrate concentration increases so does the reaction rate because there is more substrate for the enzyme react with.
reaction will increase
There is a direct relationship; as the enzyme concentration increases, the rate of reaction increases.
Increasing enzyme concentration increases the number of collisions between the enzyme molecules and the substrate molecules. This increases the number of successful collisions and the number of enzyme-substrate complexes. Therefore the reaction rate is increased as well and enzyme activity is promoted.
The first factor is Enzyme concentration or subtrate concentration.The rate of enzyme action is directly proportional to to the availability of enzyme provided the substrate concentration unlimited.Or the rate is directly proportional to the substrate concentration if enzymes are limited but if enzyme concentration is kept constant then upto the certain level the increase in substrate amount will no longer increase the rate of enzyme action. Second factor is temperature.The rate if an enzyme action is always directly proportional to the increase in temperature but upto the specific limit called as optimum temperature. Third factor is the pH value.Enzymes can work efficiently over a narrow range of pH called as Optimum pH.A minor change in pH value can denature the enzyme.
No, since the reaction reaches a max rate depending on the speed of which the Enzyme bonds to the substrate and the speed at which the enzyme catalyzes the reaction to produce enzyme and product (shown below). E + S --> ES (E - enzyme, S - substrate, P - products) ES --> E + P Thus, if each reaction rate is not equal to each other, the rate of the overall reaction is not only proportional to both the concentration of enzyme and substrate.
pH, temperature, substrate concentration and enzyme concentration influences the rate of reaction
There is a direct relationship; as the enzyme concentration increases, the rate of reaction increases.